DETAILED ACTION
Status of the Application
Claims 1-19 are pending.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
A preliminary amendment of claims 1, 4, 6 and 16-18 as submitted in a communication filed on 07/06/2026 is acknowledged.
Applicant’s species election with traverse as submitted in a communication filed on 07/06/2026 is acknowledged below:
Species Group I: F207T.
Species Group II: surfactants.
Species Group III: R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F.
Species Group IV: PET.
Species Group V: builders.
Species Group VI: PET.
Applicant’s traverse is on the grounds that Claims 1-19 are readable on the elected species at least since independent claim 1 reads on the elected F207T enzyme species and elected surfactant ingredient species; dependent claims 4, 5, and 11 further read on the elected substitution-combination, PET-activity, and builder species, respectively; and method claims 15-19 read on use of the elected composition with the elected PET polyester species. Applicant respectfully submits that the election requirement is improper, or at least overbroad, because the Office has not established that the identified alternatives are patentably distinct species lacking unity of invention. The claims are centered on a common technical relationship: a cleaning or fabric conditioning composition comprising a variant lipolytic enzyme having the recited common substitution framework and esterase or polyesterase activity in combination with detergent/fabric-care ingredients, and corresponding methods of using such compositions on polyester-containing textiles or fabrics. The Office also acknowledges that claim 1 is generic. Thus, the record itself recognizes that the elected and nonelected species are linked through a generic claim, and that the claims share the same core variant lipolytic enzyme framework and detergent/fabric-care use context. Applicants’ arguments filed on 07/06/2026 have been fully considered but they are not persuasive. As stated in the requirement for election of species, each of the species are physically distinct structures or distinct functions that require separate searches of different databases and do not share unity of invention. Thus, the requirement is deemed proper and therefore is made FINAL.
Claims 1-19 are at issue and will be examined to the extent they encompass the elected invention.
Priority
Acknowledgment is made of applicants’ claim for domestic priority under 35
U.S.C. 119 (e) to provisional Application No. 63/216,552 filed on 06/30/2021. This is the US national application which entered the national stage from Application No. PCT/EP2022/067508 filed on 06/27/20222.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 12/19/2023 is acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Objections
Claims 1, 3-4, 15 and 18 are objected to because of the following informalities:
Claim 1, 4, 15 and 18 recite “T064V”, T64V”, “T064V” and “T064V”, respectively. It is suggested that applicants maintain consistency throughout the claims. Appropriate correction is required.
Claim 1, 4, 15 and 18 are similarly objected as above in the references to positions “V014S” and “V14S”, “R040A/T”, “R40A” and “R40T”, “G059Y” and “G59Y”, “G061D” and “G61D”, “A066D” and “A66D” and “S070E” and “S70E” for a lack of consistency. Appropriate correction is required.
Claim 1 is objected to for the large space between “L258F,” and the word “and” and between “and” and the word “further”. Appropriate correction is required.
Claim 1 is objected to due to the spaces between amino acid substitutions “G061 D” and “Q161 H”. The claim should be amended to remove unnecessary spaces/gaps. Appropriate correction is required.
Claim 3 is objected to for to a lack of consistency as there is a space between the “%” and number in some instances and no space in others. For example, “90%, 91 %, 92%”. Appropriate correction is required.
Claim 4 is objected to due to the spaces between/among amino acid substitutions. The claim should be amended to remove unnecessary spaces/gaps. Appropriate correction is required.
Specification
The disclosure is objected to because of the following informalities:
The use of the terms: Triton X-100 (2X on pg. 56), TWEEN (pg. 30, second paragraph) and SPAN (pg. 30, second paragraph) which are a trade name or a mark used in commerce, have been used in this application. The terms should be accompanied by the generic terminology; furthermore, the terms should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, ℠, or ® following the terms.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Applicants’ specification recites “T064V” and “T64V” throughout. It is suggested that applicants maintain consistency throughout the specification.
The specification is similarly objected as above in the references to positions V14, R40, G59, G6 1, A66 and S70E for lack of consistency.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims
particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 2-4, 14 and 17 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 2-3 are indefinite in the recitation of a broader range followed by a narrow range “75%...99%”. Correction is required.
Claim 4 is indefinite because some of the recited amino acid substitutions do not comprise all “T064V-T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F” that are required in claim 1. For example, the first set is missing I178L. Correction is required.
Claim 14 is indefinite due to the recitation of “unit dose” for the following reasons:
It is unclear because it lacks objective boundaries and the term is not well-defined in the art, making it unclear what ingredient dosage meets the limitation. For examination purposes, claim 14 will be interpreted as a duplicate of claim 1. Correction is required.
Claim 17 is indefinite in the recitation of “wear comfort” because it is a relative term that varies from person to person and environment. Correction is required.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 4 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 4 does not further limit claim 1 as some of the combinations do not require the required substitutions of claim 1. Applicants may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-19 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
As stated in MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow.
Claims 1-14 are directed in part to a cleaning or fabric conditioning composition, comprising: (a) any variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having a mere 70% identity to the full-length amino acid sequence of SEQ ID NO: 2, comprising the substitutions T064V -T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of V014S,R040A/T, G059Y, G061D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, and wherein the variant has esterase activity; (b) at least one additional ingredient selected from the group consisting of: performance polymers, complexing agents, surfactants, and combinations thereof. There is no disclosure of any particular structure to function/activity relationship in the disclosed species. The specification also fails to describe additional representative species of these compositions and variant lipolytic enzymes by any identifying structural characteristics or properties, for which no predictability of structure is apparent.
The claims encompass a large genus of enzymes which are structurally unrelated or
substantially unrelated. A polypeptide having at least 70 % sequence identity with the
polypeptide of SEQ ID NO: 2 allows for any combination of 77 amino acid modifications within
SEQ ID NO: 2 (77.4 = 0.3x258; SEQ ID NO: 2 has 258 amino acids). The total number of
variants of a polypeptide having a specific number of amino acid substitutions can be calculated
from the formula N!x19A/(N-A)!/A!, where N is the length in amino acids of the reference
polypeptide and A is the number of allowed substitutions. Thus, the total number of variants
having at least 70% sequence identity with the polypeptide of SEQ ID NO: 2 that result from
amino acid substitutions is 258!x1977/(258-77)!/77! or 3.136239 × 10165 variants with exception of the recited substitutions. A sufficient written description of a genus of lipolytic enzyme may be achieved by a recitation of a representative number of enzymes defined by their amino acid sequence or a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. However, in the instant case, there is either no recited structural feature which is representative of all the members of the genus of lipolytic enzymes recited in the claims, or the recited structural feature, i.e., 70% sequence identity to SEQ ID NO: 2 with the recited substitutions, is not representative of all the members of the genus of enzyme recited since there is no information as to which are the structural elements within the enzyme variants of SEQ ID NO: 2 with the recited substitutions that is essential for lipolytic activity, which are the remaining structural elements required in the recited enzymes in addition to those recited in the claims such that the desired lipolytic activity is displayed , or a correlation between structure and function which would provide those unknown structural features. Furthermore, while one could argue that the few species disclosed are representative of the structure of all the members of the genus, it is noted that the art teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyzes two different reactions: deamination and dehalogenation, therefore having different function. Therefore, since minor structural differences may result in changes affecting function, and no additional information correlating structure with the desired functional characteristics has been provided, one cannot reasonably conclude that the few species disclosed are representative of the structure of all the lipolytic enzymes in the claimed composition.
Claim 15 is directed to a method of cleaning or conditioning a textile or fabric, comprising: a composition (a) any variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having a mere 70% identity to the full-length amino acid sequence of SEQ ID NO: 2, comprising the substitutions T064V -T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of V014S,R040A/T, G059Y, G061D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, and wherein the variant has polyesterase activity and at least one additional ingredient selected from the group consisting of: performance polymers, complexing agents, surfactants, and combinations thereof; and (b) contacting the textile or fabric with the composition, wherein the textile or fabric comprises or consists of polyester, and wherein the polyester is preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof, more preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), and combinations thereof. The specification also fails to describe additional representative species of these compositions and variant lipolytic enzymes by any identifying structural characteristics or properties, for which no predictability of structure is apparent.
The claims encompass a large genus of enzymes which are structurally unrelated or
substantially unrelated. A polypeptide having at least 70 % sequence identity with the
polypeptide of SEQ ID NO: 2 allows for any combination of 77 amino acid modifications within
SEQ ID NO: 2 (77.4 = 0.3x258; SEQ ID NO: 2 has 258 amino acids). The total number of
variants of a polypeptide having a specific number of amino acid substitutions can be calculated
from the formula N!x19A/(N-A)!/A!, where N is the length in amino acids of the reference
polypeptide and A is the number of allowed substitutions. Thus, the total number of variants
having at least 70% sequence identity with the polypeptide of SEQ ID NO: 2 that result from
amino acid substitutions is 258!x1977/(258-77)!/77! or 3.136239 × 10165 variants with exception of the recited substitutions. A sufficient written description of a genus of lipolytic enzyme may be achieved by a recitation of a representative number of enzymes defined by their amino acid sequence or a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. However, in the instant case, there is either no recited structural feature which is representative of all the members of the genus of lipolytic enzymes recited in the claims, or the recited structural feature, i.e., 70% sequence identity to SEQ ID NO: 2 with the recited substitutions, is not representative of all the members of the genus of enzyme recited since there is no information as to which are the structural elements within the enzyme variants of SEQ ID NO: 2 with the recited substitutions that is essential for lipolytic activity, which are the remaining structural elements required in the recited enzymes in addition to those recited in the claims such that the desired lipolytic activity is displayed , or a correlation between structure and function which would provide those unknown structural features. Furthermore, while one could argue that the few species disclosed are representative of the structure of all the members of the genus, it is noted that the art teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyzes two different reactions: deamination and dehalogenation, therefore having different function. Therefore, since minor structural differences may result in changes affecting function, and no additional information correlating structure with the desired functional characteristics has been provided, one cannot reasonably conclude that the few species disclosed are representative of the structure of all the lipolytic enzymes in the claimed composition.
Claims 16-17 & 19 are directed to a method for improving the thermophysiological properties of a textile or fabric comprising or consisting of polyester, the method comprising; a) providing a composition comprising at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions T064V- T117L-T 177N/R-I178L-F180P-Y 182A-R 190L-S205G-S212D-F226L-Y239I-L249P-S252I- L258F, and further comprising at least one additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061D, A066D, S070E, Q161H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and b) contacting the fabric or textile with the composition.
The claims encompass a large genus of enzymes which are structurally unrelated or
substantially unrelated. A polypeptide having at least 70 % sequence identity with the
polypeptide of SEQ ID NO: 2 allows for any combination of 77 amino acid modifications within
SEQ ID NO: 2 (77.4 = 0.3x258; SEQ ID NO: 2 has 258 amino acids). The total number of
variants of a polypeptide having a specific number of amino acid substitutions can be calculated
from the formula N!x19A/(N-A)!/A!, where N is the length in amino acids of the reference
polypeptide and A is the number of allowed substitutions. Thus, the total number of variants
having at least 70% sequence identity with the polypeptide of SEQ ID NO: 2 that result from
amino acid substitutions is 258!x1977/(258-77)!/77! or 3.136239 × 10165 variants with exception of the recited substitutions. A sufficient written description of a genus of lipolytic enzyme may be achieved by a recitation of a representative number of enzymes defined by their amino acid sequence or a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. However, in the instant case, there is either no recited structural feature which is representative of all the members of the genus of lipolytic enzymes recited in the claims, or the recited structural feature, i.e., 70% sequence identity to SEQ ID NO: 2 with the recited substitutions, is not representative of all the members of the genus of enzyme recited since there is no information as to which are the structural elements within the enzyme variants of SEQ ID NO: 2 with the recited substitutions that is essential for lipolytic activity, which are the remaining structural elements required in the recited enzymes in addition to those recited in the claims such that the desired lipolytic activity is displayed , or a correlation between structure and function which would provide those unknown structural features. Furthermore, while one could argue that the few species disclosed are representative of the structure of all the members of the genus, it is noted that the art teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyzes two different reactions: deamination and dehalogenation, therefore having different function. Therefore, since minor structural differences may result in changes affecting function, and no additional information correlating structure with the desired functional characteristics has been provided, one cannot reasonably conclude that the few species disclosed are representative of the structure of all the lipolytic enzymes in the claimed composition.
Claim 18 is directed in part to a method for increasing the hydrophilicity of a textile or fabric comprising or consisting of polyester, the method comprising; a) providing a composition comprising at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions T064V-T117L-T 177N/R-I178L-F 180P-Y 182A-R 190L-S205G-S 212D-F226L-Y239I- L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061D, A066D, S070E, Q161H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and b) contacting the fabric or textile with the composition.
The claim encompass a large genus of enzymes which are structurally unrelated or
substantially unrelated. A polypeptide having at least 70 % sequence identity with the
polypeptide of SEQ ID NO: 2 allows for any combination of 77 amino acid modifications within
SEQ ID NO: 2 (77.4 = 0.3x258; SEQ ID NO: 2 has 258 amino acids). The total number of
variants of a polypeptide having a specific number of amino acid substitutions can be calculated
from the formula N!x19A/(N-A)!/A!, where N is the length in amino acids of the reference
polypeptide and A is the number of allowed substitutions. Thus, the total number of variants
having at least 70% sequence identity with the polypeptide of SEQ ID NO: 2 that result from
amino acid substitutions is 258!x1977/(258-77)!/77! or 3.136239 × 10165 variants with exception of the recited substitutions. A sufficient written description of a genus of lipolytic enzyme may be achieved by a recitation of a representative number of enzymes defined by their amino acid sequence or a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. However, in the instant case, there is either no recited structural feature which is representative of all the members of the genus of lipolytic enzymes recited in the claims, or the recited structural feature, i.e., 70% sequence identity to SEQ ID NO: 2 with the recited substitutions, is not representative of all the members of the genus of enzyme recited since there is no information as to which are the structural elements within the enzyme variants of SEQ ID NO: 2 with the recited substitutions that is essential for lipolytic activity, which are the remaining structural elements required in the recited enzymes in addition to those recited in the claims such that the desired lipolytic activity is displayed , or a correlation between structure and function which would provide those unknown structural features. Furthermore, while one could argue that the few species disclosed are representative of the structure of all the members of the genus, it is noted that the art teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyzes two different reactions: deamination and dehalogenation, therefore having different function. Therefore, since minor structural differences may result in changes affecting function, and no additional information correlating structure with the desired functional characteristics has been provided, one cannot reasonably conclude that the few species disclosed are representative of the structure of all the lipolytic enzymes in the claimed composition.
Claims 1-14 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first
paragraph, because the specification, while being enabling for a cleaning or fabric conditioning composition, comprising at least one variant lipolytic enzyme having the amino acid sequence of SEQ ID NO: 2 with the recited substitutions, does not reasonably provide enablement for a cleaning or fabric conditioning composition, comprising at least one variant lipolytic enzyme having any structure, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2 having the recited substitutions. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are
summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2nd 1400 (Fed. Cir. 1988)) as follows:
1) quantity of experimentation necessary, 2) the amount of direction or guidance presented, 3)
the presence and absence of working examples, 4) the nature of the invention, 5) the state of
prior art, 6) the relative skill of those in the art, 7) the predictability or unpredictability of the art,
and 8) the breadth of the claims. The factors which have led the Examiner to conclude that the
specification fails to teach how to make and/or use the claimed invention without undue
experimentation, are addressed in detail below.
The breadth of the claims. Claims 1-14 are so broad as to encompass all possible cleaning or fabric conditioning compositions comprising: (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, and comprising the substitutions: T064V-T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S,R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and (b) at least one additional ingredient selected from the group consisting of: performance polymers, complexing agents, surfactants, and combinations thereof.
The amount of direction or guidance presented and the existence of working examples. The specification discloses SEQ ID NO: 2 and lists substitutions corresponding to SEQ NO: 2. However, the specification fails to provide any clue as to the structural elements required in any lipolytic enzyme having 70% identity with SEQ ID NO: 2 with the recited substitutions corresponding to SEQ ID NO: 2.
The state of prior art, the relative skill of those in the art, and the predictability or
unpredictability of the art. The structure of an enzyme determines its structural and functional
properties. While the art discloses a limited number of lipolytic enzymes or SEQ ID NO: 2
polypeptide variants, neither the specification nor the art provides a correlation between structure and function such that one of skill in the art can envision the structure of an enzyme or any SEQ ID NO: 2 polypeptide variant that can be a lipolytic enzyme. The art clearly teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl
decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R
Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA
and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyze two different reactions: deamination and dehalogenation,
therefore having different function (Abstract).
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While methods of determining the function and activity of enzyme variants were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process for an essentially infinite number of enzymes and SEQ ID NO: 2 variants to find an enzyme or SEQ ID NO: 2 variant with the desired lipolytic activity. In the absence of (i) a rational and predictable scheme for selecting the enzyme or SEQ ID NO: 2
variant most likely to have the desired features, (ii) a correlation between structure and function,
one of skill in the art would have to test an infinite number of enzymes and SEQ ID NO: 2 variants.
Claims 15 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first
paragraph, because the specification, while being enabling for a method of cleaning or conditioning a textile or fabric, providing a composition comprising at least one variant lipolytic enzyme having the amino acid sequence of SEQ ID NO: 2 with the recited substitutions, does not reasonably provide enablement for a method of cleaning or conditioning a textile or fabric providing a composition, comprising at least one variant lipolytic enzyme having any structure, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2 having the recited substitutions. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are
summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2nd 1400 (Fed. Cir. 1988)) as follows:
1) quantity of experimentation necessary, 2) the amount of direction or guidance presented, 3)
the presence and absence of working examples, 4) the nature of the invention, 5) the state of
prior art, 6) the relative skill of those in the art, 7) the predictability or unpredictability of the art,
and 8) the breadth of the claims. The factors which have led the Examiner to conclude that the
specification fails to teach how to make and/or use the claimed invention without undue
experimentation, are addressed in detail below.
The breadth of the claims. Claim 15 is broad as to encompass a method of cleaning or conditioning a textile or fabric comprising all possible cleaning or fabric conditioning compositions comprising: (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, and comprising the substitutions: T064V-T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S,R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity and at least one additional ingredient selected from the group consisting of: performance polymers, complexing agents, surfactants, and combinations thereof; and (b) contacting the textile or fabric with the composition, wherein the textile or fabric comprises or consists of polyester, and wherein the polyester is preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof, more preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), and combinations thereof
The amount of direction or guidance presented and the existence of working examples. The specification discloses SEQ ID NO: 2 and lists substitutions corresponding to SEQ NO: 2. However, the specification fails to provide any clue as to the structural elements required in any lipolytic enzyme having 70% identity with SEQ ID NO: 2 with the recited substitutions corresponding to SEQ ID NO: 2.
The state of prior art, the relative skill of those in the art, and the predictability or
unpredictability of the art. The structure of an enzyme determines its structural and functional
properties. While the art discloses a limited number of lipolytic enzymes or SEQ ID NO: 2
polypeptide variants, neither the specification nor the art provides a correlation between structure and function such that one of skill in the art can envision the structure of an enzyme or any SEQ ID NO: 2 polypeptide variant that can be a lipolytic enzyme. The art clearly teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl
decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R
Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA
and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyze two different reactions: deamination and dehalogenation,
therefore having different function (Abstract).
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While methods of determining the function and activity of enzyme variants were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process for an essentially infinite number of enzymes and SEQ ID NO: 2 variants to find an enzyme or SEQ ID NO: 2 variant with the desired lipolytic activity. In the absence of (i) a rational and predictable scheme for selecting the enzyme or SEQ ID NO: 2
variant most likely to have the desired features, (ii) a correlation between structure and function,
one of skill in the art would have to test an infinite number of enzymes and SEQ ID NO: 2 variants.
Claims 16-17 and 19 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method for improving the thermophysiological properties of a textile or fabric , providing a composition comprising at least one variant lipolytic enzyme having the amino acid sequence of SEQ ID NO: 2 with the recited substitutions, does not reasonably provide enablement for a method of cleaning or conditioning a textile or fabric providing a composition, comprising at least one variant lipolytic enzyme having any structure, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2 having the recited substitutions. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are
summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2nd 1400 (Fed. Cir. 1988)) as follows:
1) quantity of experimentation necessary, 2) the amount of direction or guidance presented, 3)
the presence and absence of working examples, 4) the nature of the invention, 5) the state of
prior art, 6) the relative skill of those in the art, 7) the predictability or unpredictability of the art,
and 8) the breadth of the claims. The factors which have led the Examiner to conclude that the
specification fails to teach how to make and/or use the claimed invention without undue
experimentation, are addressed in detail below.
The breadth of the claims. Claims 16-17 and 19 are broad as to encompass a method of cleaning or conditioning a textile or fabric comprising all possible cleaning or fabric conditioning compositions comprising: (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, and comprising the substitutions: T064V-T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S,R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and b) contacting the fabric or textile with the composition.
The amount of direction or guidance presented and the existence of working examples. The specification discloses SEQ ID NO: 2 and lists substitutions corresponding to SEQ NO: 2. However, the specification fails to provide any clue as to the structural elements required in any lipolytic enzyme having 70% identity with SEQ ID NO: 2 with the recited substitutions corresponding to SEQ ID NO: 2.
The state of prior art, the relative skill of those in the art, and the predictability or
unpredictability of the art. The structure of an enzyme determines its structural and functional
properties. While the art discloses a limited number of lipolytic enzymes or SEQ ID NO: 2
polypeptide variants, neither the specification nor the art provides a correlation between structure and function such that one of skill in the art can envision the structure of an enzyme or any SEQ ID NO: 2 polypeptide variant that can be a lipolytic enzyme. The art clearly teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl
decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R
Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA
and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyze two different reactions: deamination and dehalogenation,
therefore having different function (Abstract).
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While methods of determining the function and activity of enzyme variants were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process for an essentially infinite number of enzymes and SEQ ID NO: 2 variants to find an enzyme or SEQ ID NO: 2 variant with the desired lipolytic activity. In the absence of (i) a rational and predictable scheme for selecting the enzyme or SEQ ID NO: 2
variant most likely to have the desired features, (ii) a correlation between structure and function,
one of skill in the art would have to test an infinite number of enzymes and SEQ ID NO: 2 variants.
Claim 18 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method for increasing the hydrophobicity of a textile or fabric , providing a composition comprising at least one variant lipolytic enzyme having the amino acid sequence of SEQ ID NO: 2 with the recited substitutions, does not reasonably provide enablement for a method of cleaning or conditioning a textile or fabric providing a composition, comprising at least one variant lipolytic enzyme having any structure, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2 having the recited substitutions. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are
summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2nd 1400 (Fed. Cir. 1988)) as follows:
1) quantity of experimentation necessary, 2) the amount of direction or guidance presented, 3)
the presence and absence of working examples, 4) the nature of the invention, 5) the state of
prior art, 6) the relative skill of those in the art, 7) the predictability or unpredictability of the art,
and 8) the breadth of the claims. The factors which have led the Examiner to conclude that the
specification fails to teach how to make and/or use the claimed invention without undue
experimentation, are addressed in detail below.
The breadth of the claims. Claim 18 is broad as to encompass a method of cleaning or conditioning a textile or fabric comprising all possible cleaning or fabric conditioning compositions comprising: (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, and comprising the substitutions: T064V-T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S,R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and b) contacting the fabric or textile with the composition.
The amount of direction or guidance presented and the existence of working examples. The specification discloses SEQ ID NO: 2 and lists substitutions corresponding to SEQ NO: 2. However, the specification fails to provide any clue as to the structural elements required in any lipolytic enzyme having 70% identity with SEQ ID NO: 2 with the recited substitutions corresponding to SEQ ID NO: 2.
The state of prior art, the relative skill of those in the art, and the predictability or
unpredictability of the art. The structure of an enzyme determines its structural and functional
properties. While the art discloses a limited number of lipolytic enzymes or SEQ ID NO: 2
polypeptide variants, neither the specification nor the art provides a correlation between structure and function such that one of skill in the art can envision the structure of an enzyme or any SEQ ID NO: 2 polypeptide variant that can be a lipolytic enzyme. The art clearly teaches several examples of how even highly structurally homologous polypeptides can have different enzymatic activities. For example, Witkowski et al. (Biochemistry 38:11643-11650, 1999) teach that one conservative amino acid substitution transforms a β-ketoacyl synthase into a malonyl
decarboxylase and completely eliminates β-ketoacyl synthase activity. Tang et al. (Phil Trans R
Soc B 368:20120318, 1-10, 2013) teach that two Dehalobacter reductive dehalogenases, CfrA
and DcrA, having 95.2% sequence identity to teach other have exclusively different substrate
(Abstract; page 7, left column, Discussion, CfrA and DcrA). Seffernick et al. (J. Bacteriol.
183(8):2405-2410, 2001) teach that two naturally occurring Pseudomonas enzymes having 98%
amino acid sequence identity catalyze two different reactions: deamination and dehalogenation,
therefore having different function (Abstract).
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While methods of determining the function and activity of enzyme variants were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process for an essentially infinite number of enzymes and SEQ ID NO: 2 variants to find an enzyme or SEQ ID NO: 2 variant with the desired lipolytic activity. In the absence of (i) a rational and predictable scheme for selecting the enzyme or SEQ ID NO: 2
variant most likely to have the desired features, (ii) a correlation between structure and function,
one of skill in the art would have to test an infinite number of enzymes and SEQ ID NO: 2 variants.
Therefore, taking into consideration the extremely broad scope of the claim, the lack of
guidance, the amount of information provided, the lack of knowledge about a correlation
between structure and the desired function, the high degree of unpredictability in the prior art regarding enzymatic activity and polypeptide variance, one of ordinary skill in the art would
must go through the burden of undue experimentation in order to practice the claimed
invention. Thus, Applicant has not provided sufficient guidance to enable one of ordinary skill
in the art to make and use the invention in a manner reasonably correlated with the scope of the
claims.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-7 and 9-19 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Adams et al. (WO2022/197810A1 published 09/22/2022, filed 03/17/2021).
Claims 1-7 and 9-19 as interpreted are directed in part to a cleaning or fabric conditioning composition, (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, and comprising the substitutions: T064V-T117L-T177N/R-I178L- F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S,R040A/T, G059Y, G061D, A066D, S070E, Q161H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and (b) at least one additional ingredient selected from the group consisting of: performance polymers, complexing agents, surfactants, and combinations thereof, wherein the variant lipolytic enzyme comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the full-length amino acid sequence of SEQ ID NO:2, wherein the variant lipolytic enzyme is derived from a parent enzyme comprising an amino acid sequence having at least 75%, 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to the full-length amino acid sequence of SEQ ID NO:2, wherein the variant lipolytic enzyme comprises a combination of substitutions selected from the group consisting of: R40T-T64V-T117L-G175E-T177N-F180P-Y182A-R190L-S205G- F207L-S212D-F226L-Y239I-L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L- T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I- L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A- R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A- T64V-S70E-T117L-T 177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N- I178L-F 180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-G175A-T177N-I178L-F180P-Y182A-R190L- S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-T 177N-I178L-F 180P-Y 182A-R 190L-S205G-F207T-V210I-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L- F180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L- S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K- L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L- S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-T177R-I178L- F180P-Y 182A-R 190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-R256K-L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, wherein the variant lipolytic enzyme has lipolytic activity on a polyester selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof, wherein the variant lipolytic enzyme is contained in the composition in an amount of from 0.00001 to 1 wt.%, wherein the at least one additional ingredient comprises a performance polymer, wherein the at least one additional ingredient comprises a complexing agent, wherein the complexing agent comprises citric acid/citrate, EDTA or a combination thereof, wherein the cleaning or fabric conditioning composition comprises at least one further ingredient selected from the group consisting of builders, bleaching agents, bleach activators, water- miscible organic solvents, sequestering agents, electrolytes, pH regulators, optical brighteners, graying inhibitors, foam regulators, dyes and fragrances and combinations thereof, wherein the cleaning or fabric conditioning composition has a pH of 7.0 to 11.0, as measured in 1 wt.% aqueous solution at 20°C, wherein the cleaning or fabric conditioning composition is present in liquid form, and wherein the cleaning or fabric conditioning composition is in unit dose form. A method of cleaning or conditioning a textile or fabric, comprising: a) providing a composition comprising at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO: 2, comprising the substitutions T064V-T117L-T177N/R-1178L-F180P-Y182A-R190L-S205G-S212D-F226L- Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity; and at least one additional ingredient selected from the group consisting of complexing agents, surfactants, performance polymers and combinations thereof; and b) contacting the textile or fabric with the composition, wherein the textile or fabric comprises or consists of polyester, and wherein the polyester is preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof, more preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), and combinations thereof. A method for improving the thermophysiological properties of a textile or fabric comprising or consisting of polyester, the method comprising; a) providing a composition comprising at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions T064V- T117L-T177N/R-I178L-F180P-Y182A-R 190L-S205G-S212D-F226L-Y239I-L249P-S252I- L258F, and further comprising at least one additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061D, A066D, S070E, Q161H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and b) contacting the fabric or textile with the composition, wherein the thermophysiological properties comprise heat and moisture management, wear comfort or a combination thereof, wherein the polyester is preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof, more preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), and combinations thereof. A method for increasing the hydrophilicity of a textile or fabric comprising or consisting of polyester, the method comprising; a) providing a composition comprising at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions T064V-T117L-T 177N/R-I178L-F 180P-Y 182A-R 190L-S205G-S 212D-F226L-Y239I- L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061D, A066D, S070E, Q161H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has esterase activity; and b) contacting the fabric or textile with the composition.
Adams et al. teaches variant lipolytic enzymes comprising an amino acid sequence having at least 70% identity to the full-length amino acid sequence of SEQ ID NO: 2, where the lipase variant comprises one, two, three, four or more substitutions selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K and L258F, where the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, where the variant has esterase activity (see paragraph [008], pg. 2). It is noted that SEQ ID NO: 2 of Adams is 100% identical to SEQ ID NO: 2 of the instant case (see attachment below).
Adams et al. teaches the cleaning composition comprising a variant lipolytic enzyme and at least one adjunct selected from the group consisting of surfactants, builders, bleaches, bleach activators, bleach catalysts, other enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, preservatives, antioxidants, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides color speckles, silvercare, anti-tarnish and/or anti-corrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, and pH control agents (see paragraph [0014], pg. 10).
Adams et al. teaches variant lipolytic enzymes comprising an amino acid sequence having at least 70% identity to the full-length amino acid sequence of SEQ ID NO: 2, where the lipase variant comprises one, two, three, four or more substitutions selected from the group consisting of V014S, R040A/T, G059Y, G061D, T064V, A066D, S070E, T117L, Q161H, G175A, T177N/R, I178L, F180P, Y182A/L, R190L, S205G, F207T, V210I, S212D, F226L, A236P, Y239I, L249P, S252I, E254Q, R256K and L258F (see paragraph [008], pg. 2).
Adams et al. teaches the variant lipolytic enzymes have esterase activity on at least one polyester selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene
succinate (PBS), polybutylene succinate adipate (PBSA). polybutylene adipate terephthalate
(PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate
(PEN), polyester polyurethane, poly(ethylene adipate) (PEA), and combinations thereof (see paragraph [0063], pg. 29).
Adams et al. teaches the composition comprising from about 0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or 0.005% to about 0.5% lipase by weight composition (see paragraph [00110], pg. 46-47).
Adams et al. teaches the cleaning composition comprising soil release polymers and dispersants which are performance polymers (see paragraph [0089], pg. 39).
Adams et al. teaches the composition having a complexing agent (see paragraph [0095], pg. 40) and teaches the use of sodium citrate (see table 3, pg. 74) and citric acid (see table 1, pg. 69).
Adams et al. teaches the laundry detergent compositions include one or more detergent builders (see paragraph [0095], pg. 40).
Adams et al. teaches the cleaning composition to have a neat pH of from about 9.0 to about 11.0 (see paragraph [00101], pg. 42). Adams et al. teaches that the detergent compositions may be utilized at a temperature of from about 10°C to about 60°C. Adams et al. teaches that the cleaning compositions can be in granular or liquid compositions (see paragraph [0090], pg. 39).
Adams et al. teaches methods of using a variant lipolytic enzyme with esterase activity with the same mutations and contacting a fabric with the composition (see paragraph [00127], pg. 52) and where the fabric or textiles contain at least one polyester (see paragraph [00126, pg. 51) and these mutations would provide the detergent with the same improvement in thermophysiological properties as the detergent of the instant application which would improve heat and moisture management do to the enzymes being the exact same with the same mutations. Adams et al. teaches that substitutions at certain residues changed the hydrophobicity (see paragraph [00189, pg. 80). Therefore, the teachings of Adams anticipate the instant claims as written/interpreted.
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The applied reference has a common inventor with the instant application. Based upon
the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C.
102(a)(2). This rejection under 35 U.S.C. 102(a)(2) might be overcome by: (1) a showing under
37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in
accordance with 35 U.S.C. 102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public
disclosure under 35 U.S.C. 102(b)(2)(B) if the same invention is not being claimed; or (3) a
statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing
date of the claimed invention, the subject matter disclosed in the reference and the claimed
invention were either owned by the same person or subject to an obligation of assignment to the
same person or subject to a joint research agreement.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Adams et al. (WO2022/197810A1 published 09/22/2022, filed 03/17/2021) in view of Batchelor (WO2013171210A1, published 11/21/2013).
Adams et al. teaches the use of anti-redeposition agents (see paragraph [0098], pg. 41).
Batchelor teaches that alkoxylated polyethylene imine is an anti-redeposition polymer (ARP) (see Technical Field, pg. 1).
Claim 8 is directed to the cleaning or fabric conditioning composition of claim 7, wherein the performance polymer is an alkoxylated polyethylene imine.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use alkoxylated polyethylene imine as the anti-redeposition agent in Adams et al. because Batchelor teaches that it is a well-known anti-redeposition agent.
A person of ordinary skill in the art is motivated to use alkoxylated polyethylene imine because it prevents soil redeposition.
One of ordinary skill in the art has a reasonable expectation of success because the proposed substitution is well-known in the art. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-6 and 11-19 are rejected on the grounds of nonstatuatory double patenting as being unpatentable over claims 1-4, 7-9 & 13 of copending Application No. 18/571816 (‘816).
Claim 1 of ‘816 as interpreted is directed in part to a cleaning composition comprising:
(a) a variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid
sequence having at least 70% identity to the full-length amino acid sequence of SEQ ID NO:2,
comprising the substitutions T064V-T117L-T177N/R-I178L-F180P-Y182A- R190L-S205G-
S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional
substitution selected from the group consisting of V014S, R040A/T, G059Y, G061 D, A066D,
S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2,
and wherein the variant has polyesterase activity.
Claim 2 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1
of ‘816; wherein the variant lipolytic enzyme comprises an amino acid sequence having at least
80% identity to the full-length amino acid sequence of SEQ ID NO:2.
Claim 3 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1
of ‘816; wherein the variant lipolytic enzyme is derived from a parent enzyme comprising an
amino acid sequence having at least 75%, 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%,
97%, 98%, or 99% identity to the full-length amino acid sequence of SEQ ID NO:2.
Claim 4 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1
of ‘816; wherein the variant lipolytic enzyme comprises a combination of substitutions selected
from the group consisting of R40T-T64V-T117L-G175E-T177N-F180P-Y182A-R190L-S205G-
F207L- S212D-F226L-Y239I-L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L-T177N-
I178L-F180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P-
S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L- S205G-
F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V- S70E-T 117L-
T 177N-I178L-F180P-Y 182A-R 190L-S205G-F207T-S212D-F226L-A236P- Y239I-L249P-
S252I-E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N-I178L- F180P-Y 182A-R
190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q- L258F, R40T-T64V-
S70E-T117L-G175A-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T 177N-I178L-F180P-Y
182A-R 190L-S205G-F207T-V210I-S212D-F226L-A236P- Y239I-L249P-S252I-E254Q-
L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P- Y182A-R 190L-S205G-F207T-S212D-
F226L-A236P-Y239I-S244E-L249P-S252I-E254Q- L258F, R40T-T64V-S70E-T117L-T177N-
I178L-F180P-Y182A-R190L-S205G-F207T- S212D-F226L-A236P-Y239I-L249P-S252I-
E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-
I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-
S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-
I178L-F180P-Y182A-R190L-S205G- F207T-V210I-S212D-F226L-A236P-Y239I-L249P-
S252I-E254Q-R256K-L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-
Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-
R256K-L258F, and V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-
T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-
L249P-S252I-E254Q-R256K- L258F, wherein the positions are numbered by reference to the
amino acid sequence of SEQ ID NO:2.
Claim 7 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1
of ‘816; wherein the variant lipolytic enzyme has lipolytic activity on a polyester selected from
the group consisting of polyethylene terephthalate (PET).
Claim 8 of ‘816 as interpreted is directed in part to the cleaning composition of Claim 1
of ‘816; wherein the variant lipolytic enzyme is contained in the composition in an amount of
from 0.00001 to 1 wt%.
Claim 9 of ‘816 as interpreted Is directed to wherein (i) it comprises at least one additional ingredient selected from the group consisting of builders, bleaching agents, bleach activators, water-miscible organic solvents, sequestering agents, electrolytes, pH regulators, optical brighteners, graying inhibitors, foam regulators, dyes and fragrances and combinations thereof; and/or (ii) it has a pH of 7.0 to 11 .0, preferably 7.5 to 10.5, more preferably more preferably 8.0 to 10.0, even more preferably 8.0 to 9.0, as measured in 1 wt.% aqueous solution at 20°C; and/or (iii) it is present in solid or liquid, preferably liquid, form; and/or (iv) it is in unit dose, in particular pouch or caps.
Claim 13 as interpreted is directed to a method of cleaning an item comprising: (i) providing the cleaning composition according to claim 1 and (ii) washing the item with the composition, wherein the item is a textile or fabric comprising or consisting of polyester, and wherein the polyester is preferably selected from the group consisting of: polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-5 are provisionally rejected on the grounds of nonstatutory double patenting as
being unpatentable over claims 1-4 and 7 of copending Application No. 18/569,808 (‘808).
Claim 1 of ‘808 as interpreted is directed in part to a variant lipolytic enzyme comprising
an amino acid sequence having at least 70% identity to the full-length amino acid sequence of
SEQ ID NO: 2, comprising the substitutions T064V-T117L-T177N/R-I178L-F180P-Y182A-
R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one
additional substitution selected from the group consisting of V014S, R040A/T, G059Y, G061D,
A066D, S070E, Q161H, G175A/E, F207TL/T, V210I, Q227H, A236P, S244E, E254Q, and
R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO: 2, and wherein the variant has esterase activity.
Claim 2 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim
1 of ‘808, wherein the variant comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%,97%, 98%, or 99% identity to the full-length amino acid sequence of SEQ ID NO: 2.
Claim 3 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim
1 of ‘808 the variant lipolytic enzyme of claim 1 or 2, wherein the variant is derived from a
parent enzyme comprising an amino acid sequence having at least 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%,97%, 98%, or 99% identity to the full-length amino acid sequence of
SEQ ID NO: 2.
Claim 4 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim
1 of ‘808, wherein the variant comprises a combination of substitutions selected from the group
consisting of R40T-T64V-T117L-G175E-T177N-F180P-Y182A-R190L-S205G-F207L-S212D-
F226L-Y239I-L249P-S252I-L258F, R40T-G61D-T64V-S70E-T117L-T177N-I178L-F180P-
Y182A-R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P-S252I-E254Q-
L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-S212D-
F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V-S70E-T117L-T177N-I178L-
F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-
L258F, R40T-T64V-S70E-T117L-Q161H-T177N-I178L-F180P-Y182A-R190L-S205G-F207T-
S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-G175A-
T177N-1178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-
S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G-
F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-
T117L-T177N-1178L-F180P-Y182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-
S244E-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-
R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F,
V14S-R40A-G59Y-G61D-T64V-A66D-S70E-T117L-Q161H-T177R-I178L-F180P-Y182A-
R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-
L258F, V14S-R40A-G59Y-G61D-T64V-S70E-T117L-Q161H-T177R-I178L-F180P-Y182A-
R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-
L258F, R40T-G61D-T64V-S70E-T117L-Q161H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-
R40A-G59Y-G61D-T64V-A66D-S70E-T117L-Q161H-G175A-T177R-I178L-F180P-Y182A-
R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-
L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID
NO: 2.
Claim 7 of ‘808 as interpreted is directed in part to the variant lipolytic enzyme of claim
1 of ‘808, wherein the variant has hydrolytic activity on a polyester selected from the group
consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT),
polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid
(PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate
adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF),
polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, poly(ethylene
adipate) (PEA), and combinations thereof.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-6, 11, and 13-15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 9 and 11 of copending Application No. 18/571,886 (‘886).
Claim 1 of ‘886 as interpreted is directed in part to a cleaning composition, comprising (a) at least one variant lipolytic enzyme, wherein said variant lipolytic enzyme comprises an amino acid sequence having at least 70% identity to the full length amino acid sequence of SEQ ID NO:2, comprising the substitutions: T064V-T117L-T177N/R-I178L-F180P-Y182A-R190L-S205G-S212D-F226L-Y239I-L249P-S252I-L258F, and further comprising at least one additional substitution selected from the group consisting of: V014S, R040A/T, G059Y, G061 D, A066D, S070E, Q161 H, G175A/E, F207L/T, V210I, Q227H, A236P, S244E, E254Q, and R256K, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2, and wherein the variant has polyesterase activity.
Claim 2 of ‘886 as interpreted is directed in part to the cleaning composition of claim 1, wherein the variant lipolytic enzyme comprises an amino acid sequence having at least 75% identity to the full-length amino acid sequence of SEQ ID NO:2.
Claim 3 of ‘886 as interpreted is directed in part to the cleaning composition of claim 1, wherein the variant lipolytic enzyme is derived from a parent enzyme comprising an amino acid sequence having at least 90% identity to the full-length amino acid sequence of SEQ ID NO:2.
Claim 4 of ‘886 as interpreted is directed in part to the cleaning composition of claim 1, wherein the variant lipolytic enzyme comprises a combination of substitutions selected from the group consisting of R40T- T64V-T 117L-G175E-T 177N-F180P-Y 182A-R190L-S205G-F207L-S212D-F226L-Y239I- L249P-S252I-L258F, R40T-G61 D-T64V-S70E-T117L-T177N-I178L-F180P-Y182A- R190L-S205G-F207T-S212D-F226L-Q227H-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D- F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40A-T64V-S70E-T117L-T177N- I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-Q161 H-T177N-I178L-F180P-Y182A-R190L- S205G-F207T-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-G175A-T 177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L- A236P-Y239I-L249P-S252I-E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L- F180P-Y 182A-R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I- E254Q-L258F, R40T-T64V-S70E-T117L-T177N-I178L-F180P-Y182A-R190L-S205G- F207T-S212D-F226L-A236P-Y239I-S244E-L249P-S252I-E254Q-L258F, R40T-T64V- S70E-T 117L-T177N-I178L-F180P-Y 182A-R190L-S205G-F207T-S212D-F226L-A236P- Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A-G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, V14S-R40A- G59Y-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G- F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, R40T-G61 D-T64V-S70E-T117L-Q161 H-T177R-I178L-F180P-Y182A-R190L-S205G-F207T- V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K-L258F, and V14S-R40A- G59Y-G61 D-T64V-A66D-S70E-T117L-Q161 H-G175A-T177R-I178L-F180P-Y182A- R190L-S205G-F207T-V210I-S212D-F226L-A236P-Y239I-L249P-S252I-E254Q-R256K- L258F, wherein the positions are numbered by reference to the amino acid sequence of SEQ ID NO:2.
Claim 5 of ‘886 as interpreted is directed in part to the cleaning composition of claim 1, wherein the variant lipolytic enzyme has lipolytic activity on a polyester selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof.
Claim 6 of ‘886 as interpreted is directed in part to the cleaning composition of claim 1, wherein the variant lipolytic enzyme is contained in the composition in an amount of from 0.00001 to 1 wt.%.
Claim 9 of ‘886 as interpreted is directed in part to the cleaning composition of claim 1, the cleaning composition further comprises at least one additional ingredient selected from the group consisting of; builders, bleaching agents, bleach activators, water- miscible organic solvents, sequestering agents, electrolytes, pH regulators, optical brighteners, graying inhibitors, foam regulators, dyes and fragrances and combinations thereof; and/or (ii) it has a pH of 7.0 to 11.0 as measured in 1 wt.% aqueous solution at 20°C; and/or (iii) it is present in solid or liquid form; and/or (iv) it is in unit dose.
Claim 11 of ‘886 as interpreted is directed in part to the cleaning composition of claim 1, a method of cleaning an item comprising:a) providing a cleaning composition according to claim 1; andb) washing the item with the composition,wherein the item is selected from the group consisting of:(i) a textile or fabric comprising or consisting of polyester, and wherein the polyester is preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), polyethylene isosorbide terephthalate (PEIT), polylactic acid (PLA), polyhydroxy alkanoate (PHA), polybutylene succinate (PBS), polybutylene succinate adipate (PBSA), polybutylene adipate terephthalate (PBAT), polyethylene furanoate (PEF), polycaprolactone (PCL), polyethylene naphthalate (PEN), polyester polyurethane, polyethylene adipate) (PEA), and combinations thereof, more preferably selected from the group consisting of polyethylene terephthalate (PET), polytrimethylene terephthalate (PTT), polybutylene terephthalate (PBT), and combinations thereof.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claim is allowed.
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/DALTON EDWARD KIEFER/Examiner, Art Unit 1652
/ROBERT B MONDESI/Supervisory Patent Examiner, Art Unit 1652
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