DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Action Is Final, Necessitated by Amendment
Applicants' response to the Non-Final Office Action mailed on 10 July 2025, has been entered and the Remarks therein, filed on 10 October 2025, are fully considered here.
This action is a Final Office Action, based on new grounds under 35 U.S.C. §112(b) and under 35 U.S.C. §112(a), necessitated by Applicants’ amendment received on 10 October 2025, specifically, amended claim 1. See MPEP 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
Status of Claims
Claims 1, 5-11 and 13-15 are pending.
Claims 7-11 and 13-15 are withdrawn from consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected Group II. Election was made without traverse in the reply filed on 18 October 2023 to the Restriction/Election Office Action mailed on 06 September 2023.
Claims 1, 5 and 6 are rejected.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. §119(e) or under 35 U.S.C. §120, §121, or §365(c) is acknowledged. Applicant has complied with all of the conditions for receiving the benefit of an earlier filing date under 35 U.S.C. §120 or §365(c). As explained in the Non Final Office Action mailed on 10 July 2025, claims 1, 5 and 6 have the effective filing date of 28 June 2018.
Claim Objections
The objection to Claim 1, in the Non-Final Office Action mailed on 10 July 2025, is withdrawn in view of Applicants' amendment received on 10 October 2025, in which the cited claim was amended.
Claim Rejections - 35 U.S.C. § 112
35 U.S.C. § 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.
35 U.S.C. §112(a) and pre-AIA 35 U.S.C. §112, first paragraph require that the specification include the following (MPEP 2161 (I)):
(A) A written description of the invention;
(B) The manner and process of making and using the invention (the enablement requirement); and
(C) The best mode contemplated by the inventor of carrying out his invention.
Claims 1, 5 and 6 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) contain(s) 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
[Claims 5 and 6 are dependent on claim 1, contain the limitations of claim 1, and, therefore, are rejected for the same reason.]
Claims 1, 5 and 6 fail to comply with the written description requirement, because they contain new matter.
[This rejection cited in view of Applicant's amendment.]
(1) Claim 1 recites: "...and a polyesterase having at least 98% conserved sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length;..."
However, there is no support in the original disclosure nor in the originally-filed claims for a polyesterase having at least 98% conserved sequence identity. Applicant’s disclosure is limited to SEQ ID NO:1 per se and the specification fails to provide identifying characteristics of a conserved polyesterase sequence.
The specification recites, for example: "The broader concept of homology takes conserved amino acid exchanges into account in the case of amino acid sequences, i.e. amino acids having similar chemical activity, since they usually perform similar chemical activities within the protein" (clean copy specification filed 12 September 2020, pg. 5, para. [0019]); and "Conservative amino acid substitutions within the scope include, for example·. G=A=S ' I=V=L=M, D=E, N=Q , K=R, Y=F , S=T, G=A=I=V=L=M=Y=F=W=P=S=T. The homology of the polyesterases modified in this way to the polyesterase having SEQ ID NO: 1 is as defined above" (spec., pg. 8, para. [0029]).
That is, the specification does not provide support for the term 'conserved' sequence identity.
To overcome this rejection, Applicant may attempt to demonstrate (by means of argument or evidence) that the original disclosure establishes that he or she was in possession of the amended claim, the claim may be amended to recite a sequence identity that is supported by the specification, or the limitation describing conserved sequence identity may be deleted.
(2) Claims 1, 5 and 6 fail to comply with the written description requirement, because they do not adequately describe the manner and process of making the claimed invention.
[This rejection cited in the Non-Final Office Action mailed 10 July 2025.]
Claim 1 recites: "A mixture, comprising: a washing or cleaning agent comprising at least one surfactant; and, a polyesterase having at least 98% conserved sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length; and, wherein the mixture exhibits increased anti-pilling performance when compared to a reference washing agent."
However, the specification does not describe a polypeptide/polyesterase (by sequence) that is 98% identical to the amino acid sequence of SEQ ID NO.: 1 and which also functions as a washing or cleaning agent, including as an agent with increased anti-pilling performance; i.e., that represents a polyesterase that is enzymatically active. With regard to a polyesterase having 98% sequence identity with SEQ ID NO.: 1, Applicant has not provided guidance as to which amino acid residues must be conserved (or which can be altered) in order for the polypeptide to maintain functional activity, including increased anti-pilling performance. This guidance must be provided by Applicant providing the amino acid sequence(s) of polyesterases which are 98% identical to SEQ ID NO.: 1.
The hybrid polyesterase identified as SEQ ID NO.: 1 is the only polypeptide provided by Applicant which retains enzymatic activity as a washing or cleaning agent, including increased anti-pilling performance. Therefore, it is not clear that a 'representative number of species' have been sufficiently described which are representative of the entire genus of polyesterases that represents a percentage (e.g., 98%) of SEQ ID NO.: 1, and which are active washing or cleaning agents with the cited increased anti-pilling performance. Applicant has provided no examples of acceptable polypeptides/polyesterases which are 98% identical to the amino acid sequence of SEQ ID NO.: 1. See MPEP 2163 (II)(A)(3)(a)(ii).
To overcome this rejection, Applicant may attempt to demonstrate (by means of argument or evidence) that the original disclosure establishes that he or she was in possession of the amended claim or the claim may be amended to recite amino acids within the polyesterase protein which are amenable to alteration (or which must be conserved), resulting in the polyesterase as instantly claimed.
35 U.S.C. § 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 1, 5 and 6 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 pre-AIA the applicant regards as the invention.
[Claims 5 and 6 are dependent on claim 1, contain the limitations of claim 1, and, therefore, are rejected for the same reason.]
Claims 1, 5 and 6 are indefinite because the metes and bounds of the claimed subject matter are not clear.
[This rejection cited in view of Applicant's amendment.]
Claim 1 recites: "...and a polyesterase having at least 98% conserved sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length;..."
However, it is not clear how the description '98% conserved sequence identity' is different or distinct from the non-amended claim language of '98% sequence identity'. There is no description, definition or explanation in the specification with regard to the meaning of '98% conserved sequence identity'.
For the purpose of compact prosecution, the claim will be interpreted to read according to its non-amended language: "...and a polyesterase having at least 98% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length;..."
Claim Interpretations
(1) Claim 1 recites intended use language.
Claim 1 recites: “A mixture, comprising: a washing or cleaning agent comprising a polyesterase having at least 98% conserved sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length;...”
The terms (i.e., ‘washing’ and ‘cleaning’) as intended uses merely state the purpose or intended use of the invention, rather than any distinct definition of any of the claimed invention's limitations. Also, the intended use terminology does not limit the structure or method steps of the claimed invention. Therefore, the phrase as an intended use does not limit the scope of the claimed subject matter. (See MPEP 2111.02 (I)(II).) That is, the intended uses recited in the claim do not result in a structural or manipulative difference between the claimed invention and the prior art. Deletion of the preamble phrase does not affect the structure or steps of the claimed invention (MPEP 2111.02 (II)).
On the other hand, prior art documents that teach or show the use of a described (poly)esterase agent or mixture as a washing or cleaning agent will be indicated at the discretion of the Examiner.
(2) Claim 1 recites a functional limitation.
Claim 1 recites: “A mixture, comprising: a washing or cleaning agent comprising a polyesterase having at least 98% conserved sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length; and, wherein the mixture exhibits increased anti-pilling performance when compared to a reference washing agent.”
It is noted that claim 1 recites language that is analogous to ‘wherein’ clause-type language. MPEP 2111.04 (I) states, in part: Claim scope is not limited by claim language that suggests or makes optional, but does not require steps to be performed or by claim language that does not limit a claim to a particular structure. However, examples of claim language, although not exhaustive, that may raise a question as to the limiting effect of the language in a claim are: (A) "adapted to" or "adapted for" clauses; (B) "wherein" clauses; and (C) "whereby" clauses..., the court noted that a “whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.” Id. (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)).
Claim Rejections - 35 U.S.C. § 103
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 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.
Claims 1, 5 and 6 are rejected under 35 U.S.C. §103 as being unpatentable over Tournier et al. ((2018 Jan.) Pub. No. WO 2018/011281 A1) as evidenced by STIC search results (Tournier et al. -SEQ ID NO.: 1, Datasheet [online].Search results retrieved 08-18-2023) and NCBI Blast Global Align (instant SEQ ID NO.: 1 vs Tournier et al. SEQ ID NO.: 1. Downloaded 11-30-2023) in view of Meine et al. (Pub. No. DE102007005419 A1; Date of Pub.: 2008-07-31; see English machine translation (EngMT) as NPL for page/para. numbers), and Betts et al. (Amino acid properties. In: Bioinform. Genetic. 2003, Chapter 14, pp. 289-316).
[This rejection cited in the Non-Final Office Action mailed 10 July 2025.]
Regarding claim 1, pertaining to a mixture comprising a washing or cleaning agent comprising a polyesterase,
[See Claim Interpretations section above- (1) and (2).]
Tournier et al. shows esterases having improved activity for degrading polyester containing material (pg. 1, lines 1-4). The described invention provides variants of an esterase having the amino acid sequence as set forth in SEQ ID NO.: 1 (pg. 2, lines 10-14). It is a further object of the described invention to provide a composition comprising an esterase (pg. 20, line 10 [i.e., a mixture comprising a washing or cleaning agent comprising a polyesterase]).
Tournier et al. does not explicitly show the relationship between the described SEQ ID NO.: 1 and instantly-claimed SEQ ID NO.: 1, with regard to claim 1.
STIC sequence search results and NCBI Blast Global Align show that the amino acid sequence of SEQ ID NO.: 1, shown by Tournier et al., has 94.3% amino acid sequence identity with instant SEQ ID NO.: 1.
Regarding claim 5, a preferred composition comprises between 0.1 and 5% by weight of the esterase of the described invention (pg. 21, lines 1-2).
Regarding claim 6, pertaining to pH regulators,
Tournier et al. shows that the composition may be liquid or dry. The composition comprises appropriate excipients including, minimally, agents for adjusting pH (pg. 20, lines 14-23).
Tournier et al. further teaches that esterases are able to catalyze the hydrolysis of a variety of polymers, including polyesters. In this context, esterases have shown promising effects in a number of industrial applications, including as detergents for dishwashing and laundry applications, as degrading enzymes for processing biomass and food, as biocatalysts in detoxification of environmental pollutants or for the treatment of polyester fabrics in the textile industry (pg. 1, lines 8-12).
That is, Tournier et al. teaches that (poly)esterases can be used as a washing or a cleaning agent, per claim 1.
Tournier et al. as evidenced by STIC search results and NCBI Blast Global Align does not show: 1) at least one surfactant [Claim 1]; and 2) the polyesterase has at least 98% sequence identity with the amino acid sequence given in SEQ ID NO.: 1 over its entire length [Claim 1].
Regarding claim 1, pertaining to at least one surfactant,
Meine et al. shows a detergent or a cleaning agent containing surfactant(s), an enzyme and other common ingredients of detergents or cleaning agents (pg. 2, para. [0001]). The enzyme is selected from a group the includes, minimally, esterases/polyesterases (pg. 4, para. [0009] [nexus to Tournier et al.- esterase used for cleaning purposes]).
Tournier et al. as evidenced by STIC search results and NCBI Blast Global Align provide information from which one of ordinary skill in the art of enzyme mutagenesis would have understood that the esterase sequence shown by Tournier et al., which has 94.3% identity with the amino acid sequence of SEQ ID NO.: 1, could have been altered such that conservative amino acid mutations could have been made in order to produce a(n) (poly)esterase that is 98% identical with SEQ ID NO.: 1, by way of further addressing the limitations of claim 1.
Further regarding claim 1, Tournier et al. as evidenced by STIC search results shows that amino acid sequence SEQ ID NO.: 1, shown by Tournier et al., has 94.3% amino acid sequence identity to instant SEQ ID NO.: 1. NCBI Blast Global Align shows that SEQ ID NO.: 1, shown by Tournier et al., contains at least six conservative amino acid substitutions compared to instant SEQ ID NO.: 1. These conservative amino acid substitutions occur at various amino acid locations, e.g., 150, 171 and 178 (i.e., “I” to “V”); 160 (i.e., “N” to “T”); 174 (i.e., "D" to "E"); and 165 ("T" to "S"). It is noted that “I” (isoleucine) and “V” (valine) are amino acids with hydrophobic side chains; “N” (asparagine) and “T” (threonine) are amino acids with uncharged side chains; "D" (aspartic acid) and "E" (glutamic acid) are acidic and polar amino acids; and "T" (threonine) and "S" (serine) are polar amino acids.
Altering the amino acid sequence shown by Tournier et al. to contain the six amino acids shown in instant SEQ ID NO.: 1, would result in the SEQ ID NO.: 1 shown by Tournier et al. to be 98% identical to instant amino acid sequence SEQ ID NO.: 1. (i.e., 255 amino acids/261 amino acids = 97.7% or 98%).
Betts et al. provides information from which one of ordinary skill in the art would have understood that conservative amino acid substitutions in the SEQ ID NO.: 1 sequence shown by Tournier et al. could have been made, by way of addressing the limitations of claim 1.
Regarding claim 1, Betts et al. teaches that the function of valine (V) and isoleucine (I) are the same. Valine is described as preferring to be buried in protein hydrophobic cores and is also Cβ branched (pg. 301, entry# 14.5.4). Isoleucine can be substituted by other hydrophobic, particularly aliphatic, amino acids. Being hydrophobic, isoleucine prefers to be buried in protein hydrophobic cores. Like valine it is Cβ branched. The isoleucine side chain is very non-reactive and is thus rarely directly involved in protein functions like catalysis, although it can play a role in substrate recognition. In particular, hydrophobic amino acids can be involved in binding/recognition of hydrophobic ligands such as lipids (pg. 300, entry# 14.5.2).
Betts et al. also teaches that threonine (T) can be substituted with other polar amino acids, particularly serine (S). Being a fairly indifferent amino acid, threonine can reside both within the interior of a protein or on the protein surface. Threonine is also Cβ branched (see Isoleucine). Threonines are quite common in protein functional centers. The hydroxyl group is fairly reactive, being able to form hydrogen bonds with a variety of polar substrates (pg. 307, entry# 14.5.17). Asparagine (N) can be substituted by other polar amino acids. Being polar asparagine prefers generally to be on the surface of proteins, exposed to an aqueous environment. Asparagines are quite frequently involved in protein active or binding sites (pg. 306, entry# 14.5.14).
Betts et al. also teaches that aspartate (D) can be substituted by glutamate (E) or other polar amino acids (pg. 305, entry# 14.5.12.1).
That is, Betts et al. teaches that amino acids that have the same side chain characteristics (e.g., hydrophobic or polar) also have similar functions with regard to protein-protein interactions.
It is noted that of the sixteen (16) amino acid differences between the SEQ ID NO.: 1 amino acid sequence, as shown as Tournier et al., and instantly-claimed SEQ ID NO.: 1, fourteen (14) are amino acid substitutions and include: three (3) valine for isoleucine substitutions (hydrophobic side chain amino acids); one (1) threonine for asparagine (uncharged side chains); one (1) phenylalanine for tryptophan (hydrophobic side chains); one (1) asparagine for serine (uncharged side chains); one (1) threonine for serine (uncharged side chains); one (1) serine for threonine (uncharged side chains); one (1) glutamic acid for aspartic acid (negatively-charged side chains); and one (1) alanine to leucine (hydrophobic side chains).
That is, 10 of the 16 amino acid substitutions are conservative amino acid substitutions.
In addition, the sequence of Tournier et al. does not show the last two amino acids (leucine and glutamic acid) at the C-terminal end of instantly-claimed SEQ ID NO.: 1.
Accordingly, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention, to have substituted the polyesterase having the amino acid sequence of SEQ ID NO.: 1, as instantly-claimed, with a polyesterase which comprises an amino acid sequence which is 98% or more identical to the amino acid sequence of SEQ ID NO.: 1 [Claim 1], with a reasonable expectation of success, because Tournier et al. as evidenced by STIC search results and NCBI Blast Global Align shows a (poly)esterase enzyme that is 94.3% identical in amino acid sequence to the amino acid sequence of instant SEQ ID. NO.: 1, and also shows that most of the amino acid differences between the SEQ ID NO.: 1 shown by Tournier et al. and instant SEQ ID NO.: 1 are conservative amino acid substitutions which would render SEQ ID NO.: 1 in Tournier et al. 98% identical to instant SEQ ID NO.: 1 (MPEP 2143 (I)(G)).
Therefore, it would have been obvious to one of ordinary skill in the art of producing mutagenized enzymes to have made conservative amino acid substitutions in amino acid sequence SEQ ID NO.: 1 shown by Tournier et al., so that the resulting amino acid sequence is 98% identical to instant SEQ ID NO.: 1, with the reasonably predictable expectation that the polyesterase resulting from the said conservative amino acid substitutions would maintain its enzymatic (functional) activity.
One of ordinary skill in the art would have been motivated to have made those modifications, because Betts et al. teaches that amino acids that have similar side chain biochemical characteristics (and, therefore, could be substituted for each other as conservative substitutions) have the same function. For example, Betts et al. teaches that isoleucine (I) and valine (V) have hydrophobic side chains and that hydrophobic amino acids can be involved in binding/recognition of hydrophobic ligands such as lipids. Therefore, one of ordinary skill in the art would have been motivated to have substituted I for V (or vice versa) depending on which amino acid would result in improved polyesterase activity, e.g., with regard to the binding of the polyesterase to its substrate.
Betts et al. also teaches that, although asparagine (N), serine (S) and threonine (T) are polar amino acids, N prefers generally to be on the surface of proteins, while T can reside both within the interior of a protein or on the protein surface. Therefore, one of ordinary skill in the art would have been motivated to have substituted N for T (or vice versa) (or T for S) depending on which amino acid would result in improved polyesterase activity, e.g., the binding of the polyesterase to its substrate. Betts et al. also teaches that aspartate (D) can be substituted by glutamate (E) or other polar amino acids (pg. 305, entry# 14.5.12.1).
It would have been further obvious to have added at least one surfactant to the mixture [Claim 1], as shown by Meine et al., with a reasonable expectation of success, because Meine et al. shows that a detergent or cleaning agent can comprise both (a) surfactant(s) and (an) esterase(s)/polyesterase(s), such the detergent or cleaning agent comprising (an) esterase(s) as shown by Tournier et al. (MPEP 2143 (I)(G)).
One of ordinary skill in the art would have been motivated to have made that modification, because one of ordinary skill in the art of manufacturing mixtures comprising washing or cleaning agents containing an enzyme, such as a polyesterase, would consider the addition of a surfactant as an improvement to the washing or cleaning properties of the mixture. Meine et al. teaches that some of the described surfactants exhibit good washing or cleaning performance on specific, but not enzyme-specific, soilings, such as oil-based soilings, so that the range of soilings possessed by a detergent or cleaning agent according to the invention is improved, in particular expanded (pg. 5, cont. para. [0013]).
In addition, when a structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent (MPEP 2112.01 (I)).
In addition, it is well known that “[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer.” Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977) (MPEP 2112 (I)).
A rejection under 35 USC §102/103 can be made when the prior art product seems to be identical except that the prior art is silent as to an inherent characteristic…This same rationale should also apply to product, apparatus, and process claims claimed in terms of function, property or characteristic MPEP 2112 (III). The PTO can require an applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his [or her] claimed product. Whether the rejection is based on 'inherency' under 35 USC 102, on 'prima facie obviousness' under 35 USC 103, jointly or alternatively, the burden of proof is the same. In re Best, 562 F .2d 1252, 1255, 195 USPQ 430, 433-34 (CCPA 1977) (MPEP 2112 (V)).
Therefore, prior art which shows a polyesterase having (or a mixture having a polyesterase which has) at least 98% sequence identity with the amino acid sequence given in SEQ ID NO: 1 over its entire length will be considered to also exhibit increased anti-pilling performance when compared to a reference washing agent.
On the other hand, prior art documents that teach or show the use of a described (poly)esterase agent or mixture with increased anti-pilling performance will be indicated at the discretion of the Examiner.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Response to Arguments
Applicant’s arguments, pp. 5-6, filed 03 June 2025, with respect to the prior art references cited in the 35 U.S.C. §103 rejection, have been fully considered but they are not persuasive.
1. Applicant remarks (pg. 4, para. 2 and 3), with regard to the instant claim amendment, and the written description rejection under 112(a), that amendment to claim 1 is for correction of an informality with additional support found at least at ¶[0016, 0022, and 0105] of the published Specification. Hence, no new matter is added.
However, in response to Applicant, the cited paragraphs [0016], [0017], [0018] and [0022] merely describe the polyesterase as being obtainable by single or multiple conservative amino acid substitutions of the starting molecule; and/or fragmentation or deletion, insertion or substitution mutagenesis, and comprises an amino acid sequence which matches the starting molecule over a length of at least 180, 190, 200, 210, 220, 230, 240, 245, 250, 251, 252, 253, 254, 255, 256, 257, 258, 259 or 260 contiguous amino acids of the starting molecule. However, these descriptions in the specification do not show specific amino acid sequences which are 98% identical to the polyesterase represented by SEQ ID NO.: 1, and which retain functional activity as described in claim 1 as an intended use and inherent property (see Claim Interpretations section above).
Further in response to Applicant, Zabin et al. (Biochem. 1991, 30: 6230-6240 (provided here)) teaches that it is not possible, at present, to predict with certainty whether a protein differing from a natural protein by an amino acid substitution is likely to be functional, even if detailed structural information on the wild-type protein is available. Nevertheless, it is widely thought that chemically conservative amino acid substitutions will generally not affect the function of a protein (pg. 6230, column 1, para. 1). However, results from the described study concluded that neither the frequency of exchange of amino acids between homologous proteins nor any other measure of the properties of the amino acids will be particularly useful by themselves in predicting whether a protein with an amino acid substitution will be functional. The context of a mutation plays such a strong role in determining the activity of a mutant that such a prediction would be very uncertain. A reasonable prediction of the effects of amino acid substitutions can be made, however, by considering the sensitivity to substitution of the site of a mutation (pg. 6237, column 2, para. 3).
Therefore, in view of Zabin et al., although Applicant has suggested a general approach for performing conservative amino acid substitutions that could be made in SEQ ID NO.:1 so as to produce a polypeptide which is 98% identical thereto (clean copy specification filed 09 December 2020, pg. 8, para. [0029]), it would not be conclusory that any conservative amino acid substitution could be made and render the polyesterase represented by SEQ ID NO.:1 enzymatically functional. Applicant has not provided either specific amino acid sequences as acceptable variants of SEQ ID NO.: 1 or a schematic showing the regions of SEQ ID NO.: 1 which would be amenable to conservative amino acid substitutions.
2. Applicant remarks (pg. 5 thru pg. 6, para. 1), with regard to the 103 rejections, that Applicant amended claim 1 as above presented. Applicant submits that the references are entirely silent with regards to teaching improved pilling performance as taught and claimed by Applicant.
However, in response to Applicant, the anti-pilling performance is considered to be an inherent property of a mixture comprising a polyesterase having at least 98% sequence identity with the amino acid sequence given in SEQ ID NO.: 1. See Claim Interpretations section- (2) above. In addition, it is well known that when a structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent (MPEP 2112.01 (I)).
3. Applicant remarks (pg. 5, thru pg. 6, para. 3) that, in addition, a careful review of the cited references (Tournier with Meine) reveals that such a combination is unsupported by the teachings of the art and would not be reasonably expected to succeed. Tournier is directed to biodegradation of bulk plastics, specifically polyethylene terephthalate (PET), and describes processes carried out at elevated temperatures. The focus is exclusively on enzymatic recycling of plastics, not on detergent formulation or textile cleaning.
However, in response to Applicant, although Tournier et al. is focused on degrading polyester in plastic products, Tournier et al. also acknowledges that esterases have shown promising effects in a number of industrial applications, including as detergents for dishwashing and laundry applications, as degrading enzymes for processing biomass and food, as biocatalysts in detoxification of environmental pollutants or for the treatment of polyester fabrics in the textile industry (pg. 1, lines 8-12; see 103 rejection above). Therefore, in view of the breadth of potential uses for polyesterases (including as a washing or cleaning agent, as acknowledged by Tournier et al.), it would have been obvious to have produced a mixture comprising a polyesterase having at least 98% sequence identity with the amino acid sequence given in SEQ ID NO.: 1 for use as a washing or cleaning agent.
Further in response to Applicant, it is well known that when a structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent (MPEP 2112.01 (I)).
4. Applicant remarks (pg. 6, para. 4 thru pg. 7) that Meine, in contrast, addresses stabilization of conventional detergent enzymes; including examples such as proteases, amylases, and lipases and using nitrogen-containing surfactants. Polyesterase is mentioned once in a boilerplate list of possible enzymes. The Office relies on Meine solely to supply the missing "washing or cleaning agent comprising at least one surfactant." However, Meine's stabilization strategy is fundamentally incompatible with Tournier's high-temperature PET-recycling process. Thus, modifying Tournier's process to include Meine's surfactant regime would render the process inoperable, which is prohibited under MPEP 2143.
However, in response to Applicant, the instantly-claimed subject matter is not directed to a method of making or a method of using the polyesterase having at least 98% amino acid sequence identity to SEQ ID NO.: 1. The claims are directed to a mixture/composition and both Tournier et al. and Meine et al. show mixtures/compositions comprising polyesterases. Meine et al. shows detergent or cleaning agents containing surfactants and shows that enzymes can also be included in said agents, the enzymes comprising, minimally, esterase/polyesterases (see 103 rejection above).
5. Applicant remarks (pg. 7, para. 2) that none of the cited references provides a science-based reason to expect that a surfactant-laden detergent bath would not denature Tournier' s enzyme. Betts et al. is silent on formulation and does not address compatibility of polyesterases with detergent surfactants. The absence of motivation, coupled with the expected incompatibility, negates any rationale for combination under KSR.
However, in response to Applicant, Meine et al. shows that compositions containing surfactants can also contain enzymes; therefore, Betts et al. is not required to show their compatibility. Betts et al. was cited to show that the prevailing understanding of protein variant production is that conservative amino acid substitutions can be made which would not adversely affect the protein's function, and provides specific examples of how certain amino acids are interchangeable. In summary, Tournier et al. shows a polyesterase which, by altering six of its amino acids, would represent an amino acid sequence which is 98% identical to the amino acid sequence of instant SEQ ID NO.: 1. Tournier et al. also teaches that polyesterases are used in cleaning processes. Meine et al. shows that surfactants and enzymes, including polyesterases, may be combined in an agent used as a detergent or cleaning agent.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
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/SMP/Examiner, Art Unit 1651
/Michelle F. Paguio Frising/Primary Examiner, Art Unit 1651