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 .
Claims Status
Claims 13-28 are pending.
Claims 1-12 are canceled.
The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 02/22/2022 and 05/29/2026 and 01/23/2026 and 06/25/2026 is acknowledged. The submission is in compliance with the provision of 37 CFR 1.97. Accordingly, the information disclosure statements have been considered.
Claim Objections
The numbering of claims is not in accordance with 37 CFR 1.126 which requires the original numbering of the claims to be preserved throughout the prosecution. When claims are canceled, the remaining claims must not be renumbered. When new claims are presented, they must be numbered consecutively beginning with the number next following the highest numbered claims previously presented (whether entered or not).
Claim 24 is misnumbered. The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations.
Claim Rejections - 35 USC § 112
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 25-26 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.
With regards to claim 25, the claim recites “wherein the amount of fragrance compound …is reduced compared to a fragrance bead composition without the enzyme having cellulase activity”. It is unclear what the composition being compared to is therefore the claim is rendered indefinite.
With regards to claim 26, the claim recites “relative to the corresponding comparable composition without the enzyme having cellular activity”. It is unclear what the composition that is being compared to is therefore the claim is rendered indefinite.
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 13 (and claims 14-21 dependent from), 22 (and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations) dependent from) and claim 25 (and claims 26-28 dependent from) 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.
Claim 13 (and claims 14-21 dependent from) is directed to a method comprising all possible enzymes having cellulase activity. There is no disclosure of any particular structure to function/activity relationship in the disclosed species.
Claim 21 is drawn to a method of claim 13 wherein the enzyme having cellulase activity is all possible polypeptides having at least 60%-100% sequence identity to any of the mature polypeptides of SEQ ID NO: 1-6. There is no disclosure of any particular structure to function/activity relationship in the disclosed species.
Claim 22 (and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations) dependent from) is drawn to a fragrance bead composition comprising all possible enzymes having cellulase activity having at least 60%-100% sequence identity to SEQ ID NO: 1-6. There is no disclosure of any particular structure to function/activity relationship in the discloses species.
Claims 25 (and claim 26-28 dependent from) are drawn to a method comprising all possible enzymes having cellulase activity. There is no disclosure of any particular structure to function/activity relationship in the discloses species.
Claim 28 is drawn to a method wherein all possible enzymes having cellulase activity are polypeptides having at least 60%-100% sequence identity with SEQ ID NO: 1-6. There is no disclosure of any particular structure to function/activity relationship in the discloses species.
There are reports of more than 200 genes encoding cellulases and related enzymes (see pg. 365 and pg. 367-377, Ohmiya et al., Biotechnology and Genetic Engineering Reviews, Vol. 14, pg. 365-414, published online April 15, 2014). Although biochemical analysis has generated a comprehensive insight into the action of cellulses, several questions remain unanswered such as the substrate specificity of the enzymes, molecular structure, and how introduction of cellulases in genes for industrial important organisms can be exploited (see pg. 189, Gilbert et al, Journal of General Microbiology, Vol. 139, pg. 187-194; published 1993). Additionally, commercial interests have been escalating worldwide on cellulate enzymes. However, understanding accurate cellulase catalytic activities has remained a major technological challenge (see Abstract, Hamid et al, Cellulose, Vol. 22, pg. 2157-2182, published 2015). The specification also fails to describe additional representative species of these proteins by identifying structural characteristics or properties for which no predictability of structure is apparent.
Regarding the level of skill and knowledge in the art of amino acid mutation, the reference of Singh et al., (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached PTO0-892) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see pg. 7, column 1, top). Also, the unpredictability associated with amino acid mutations is exemplified by the reference of Zhang et al. (Structure 26: 1474-1485, 2018, cited on the attached Form PTO-82) which discloses that even a mutation of a surface residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1).
Given this lack of additional representative species as encompassed by the claims, Applicants have failed to sufficiently describe the claimed invention, in such full, clear, concise, and exact terms that a skilled artisan would recognize Applicants were in possession of the claimed invention.
Claims 13 (and claims 14-21 dependent from), 22 (and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations) dependent from) and claim 25 (and claims 26-28 dependent from) 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Claims 13 (and claims 14-20 dependent from) and 21are 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 an enzyme having cellulase activity where the polypeptide has 100% sequence identity to SEQ ID NO: 1-6, does not reasonably provide enablement for all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6. The specification, however, only provides representative species of SEQ ID NO: 1 (see specification pg. 22) and polypeptides having 100% sequence identity with SEQ ID NO: 1-6. 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 use the invention commensurate in scope with these claims.
Claim 22 and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations) 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 an enzyme having cellulase activity where the polypeptide has 100% sequence identity to SEQ ID NO: 1-6, does not reasonably provide enablement for all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6. The specification, however, only provides representative species of SEQ ID NO: 1 (see specification pg. 22) and polypeptides having 100% sequence identity with SEQ ID NO: 1-6. 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 use the invention commensurate in scope with these claims.
Claim 25 (and claims 26-28 dependent from) 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 an enzyme having cellulose activity where the enzyme having cellulose activity is a polypeptide having 100% sequence identity to SEQ ID NO: 1-6, does not reasonably provide enablement for to all possible enzymes having cellulose activity where the enzyme having cellulose activity is a polypeptide having 60-99% sequence identity to SEQ ID NO: 1-6. The specification, however, only provides representative species of SEQ ID NO: 1 (see specification pg. 22) and polypeptides having 100% sequence identity with SEQ ID NO: 1-6. 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 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, 8 USPQ 2nd 1400 (Fed. Cir. 1988)) as follows: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the 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 claim(s).
Claims 13 (and claims 14-20 dependent from) and 21 is so broad as to encompass all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6 encompassed by the claim.
Claim 22 and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations) is so broad as to encompass all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6 encompassed by the claim.
Claim 25 (and claims 26-28 dependent from) is so broad as to encompass all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6 encompassed by the claim.
The claims rejected under this section of U.S.C. 112, first paragraph, place minimal structural limits on the required variant polypeptides encompassed by the claims. Since the amino acid sequence of a protein determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. However, in this case the disclosure is limited to:
(Claims 13 (and claims 14-20 dependent from) and 21): an enzyme having cellulase activity wherein the enzyme having cellulase activity is a polypeptide having 100% sequence identity with SEQ ID NO: 2-6 and representative species of SEQ ID NO: 1.
(Claim 22 and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations): an enzyme having cellulase activity wherein the enzyme having cellulase activity is a polypeptide having 100% sequence identity with SEQ ID NO: 1-6 and representative species of SEQ ID NO: 1.
Claim 25 (and claims 26-28 dependent from): ): an enzyme having cellulase activity wherein the enzyme having cellulase activity is a polypeptide having 100% sequence identity with SEQ ID NO: 1-6 and representative species of SEQ ID NO: 1.
While recombinant and mutagenesis techniques are known, it is not routine in the art to screen for multiple substitutions or multiple modifications, as encompassed by the instant claims, and the positions within a protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
The specification does not support the broad scope of the claims which encompass any possible:
(Claims 13 (and claims 14-20 dependent from) and 21): enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6.
Claim 22 and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations): enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6.
Claim 25 (and claims 26-28 dependent from): ): enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6
because the specification does not establish: (A) regions of the polypeptide which may be modified affecting the polypeptide of claims 13, 22, 24, and 25; (B) the general tolerance of enzymes of the polypeptide of claims 13, 22, 24, and 25 to modification and extent of such tolerance; (C) a rational and predictable scheme for modifying any amino acid residue of a protein of the polypeptide of claims 13, 22, 24, and 25 protein group with an expectation of obtaining the desired biological function; and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. Because of this lack of guidance, the extended experimentation that would be required to determine which substitutions would be acceptable to retain the required functions of the polypeptide of claims 13, 22, 24, and 25 and the fact that the relationship between the sequence of a peptide and its tertiary structure (i.e. its activity) are not well understood and are not predictable (e.g., see Ngo et al. in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495; Franceus et al., J. Ind. Microbiol. Biotechnol. Vol 44, pp 687-695, 2017), it would require undue experimentation for one skilled in the art to arrive at the majority of polypeptides having the function of the polypeptide of claims 13, 22, 24, and 25 of the claimed genus.
Thus, applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims broadly including any:
(Claims 13 (and claims 14-20 dependent from) and 21): enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6.
Claim 22 and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations): enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6.
Claim 25 (and claims 26-28 dependent from): enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6.
The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of:
(Claims 13 (and claims 14-20 dependent from) and 21): all enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6,
Claim 22 and claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations): all enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6,
Claim 25 (and claims 26-28 dependent from): all enzymes having cellulase activity and having a polypeptide having at least 60-99% sequence identity to any mature polypeptide of SEQ ID NO: 1-6,
is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
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 13-15 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck.
With regards to claim 13, Baeck discloses a method of treating a fabric with a composition comprising a chemical entity, surfactant, and a protease for fabric cleaning (see claims 18-19) . Baeck discloses that the composition comprises a chemical entity that comprises a deposition aid having high affinity for cellulose and a benefit agent (see claim 1). Baeck discloses that cellulases are preferred as the deposition aid (see lines 1-10, pg.5). Baeck further discloses that the deposition aid is selected from an enzyme comprising a cellulose binding domain (see claim 2). Baeck discloses that the benefit agent is selected from a perfume (see claim 4). Baeck discloses that the fabric care composition can be a liquid (see lines 9-10).
With regards to claim 14-15, Baeck discloses that the composition comprises a deposition aid having high affinity for cellulose (see claim 1) and that the preferred deposition aid is cellulose (see lines 9-10, pg. 5). Baeck further discloses that the composition can be formulated as a laundry detergent including laundry additive compositions and compositions suitable for use in soaking of stained fabrics (see lines 34-36, pg. 58 and line 1, pg. 59).
Therefore, claims 13-15 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck.
Claims 22 and 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the examiner will examine the claim in such limitations; see claims status) are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert.
With regards to claim 22, Schubert discloses fabric care composition comprising a detersive enzyme and a perfume (See Field of invention, lines 5-6, pg. 1, and claim 1 (iii),pg. 88). Schubert teaches that detersive enzyme is preferably selected from cellulases (see lines 30-31, pg. 18). Schubert further teaches that the composition is in the form of a bead (see claim 11, pg. 94).
With regards to claim 24 (The Examiner notes that the second claim number 24 is non-compliant and should be canceled and renumbered as claim 29. In favor of compact prosecution, the Examiner will examine the claim in such limitations; see claims status), in addition to the teachings of Schubert as applied to claim 22 above, Schubert discloses that the composition provides fabric care benefits such as perfume longevity (see lines 10-14, pg. 49).
Therefore, claims 22 and 24 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert.
Claim Rejections - 35 USC § 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 (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 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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 16-17 and 22 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck, as applied to claim 13 above, and further in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert.
The teachings of Baeck as applied to claim 13 are summarized above.
With regards to claim 16, Baeck does not teach that the enzyme having cellulase activity and the one or more fragrance compounds are comprised within a fragrance bead composition.
However, Schubert teaches a fabric care composition comprising a detersive enzyme and a perfume (See Field of invention, lines 5-6, pg. 1, and claim 1 (iii),pg. 88). Schubert teaches that detersive enzyme is preferably selected from cellulases (see lines 30-31, pg. 18). Schubert further teaches that the composition is in the form of a bead (see claim 11, pg. 94).
It would have been obvious to one of ordinary skill in the art of protein chemistry before the effective date of the current instant application to incorporate the enzyme having cellulase activity and the one or more fragrance compounds taught by Baeck into a bead composition taught by Schubert. One of ordinary skill in the art would be motivated to do so since Schubert teaches that the fabric care composition comprising a cellulase and perfume are in the form of a bead and that his would be a practical way of using the composition for fabric care. One of ordinary skill in the art would have expectations of success in doing so as the combined teachings of Baeck and Schubert provide the necessary guidance and teachings to do so.
With regards to claim 17, Baeck does not specifically teach that the fabric/textile is cotton.
However, Schubert teaches that the composition includes a fabric care agent such as an ingredient that can provide fabric care benefits such as perfume longevity to cotton garments and fabrics (see lines 10-14, pg. 49).
It would have been obvious to one of ordinary skill in the art of protein chemistry before the effective filing date of the current instant application to apply the fabric care composition comprising a cellulase and perfume (fragrance) taught by Baeck to a cotton garment or fabric taught by Schubert. One of ordinary skill in the art would be motivated to do so since Schubert teaches that application of the fabric care composition provides fabric care benefits such as perfume (fragrance) longevity. One of ordinary skill in the art would have expectations in doing so as Baeck and Schubert provide all the necessary guidance and teachings to do so.
Therefore, claims 16-17 and 22 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck, as applied to claim 13 above, and further in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert.
Claims 18-19 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck, and further in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert, as applied to claim 17 above, and further in view of Hochberg et al. (United States Patent No: US 8556993 B2; published October 15, 2013), hereinafter referred to as Hochberg.
The teachings of Baeck and Schubert as applied to claim 17 are summarized above.
With regards to claim 18-19, the combined teachings of Baeck and Schubert are silent on whether the textile is a mixture of at least 50% polyester and at least 20% cotton or a mixture of at least 30% polyester and at least 40% cotton.
However, Hochberg teaches a laundry composition that is a detergent composition in liquid form (see Column 9, lines 14-16) that comprises perfumes (see Column 22, lines 22-34) and cellulase (see Column 24, lines 17-27). Hochberg teaches using the composition in a laundering process for brightening a polyester/cotton textile (see Column 30, claim 1). Hochberg further teaches that the ratio of polyester to cotton in the blended textile is 80:20 to 20:80 (see column 2, lines 3-5).
It would have been obvious to one of ordinary skill of the art of protein chemistry to apply the fabric care composition taught by Baeck to a cotton textile (taught by Schubert) and a polyester/cotton blended textile comprising a ratio of polyester to cotton in the blended textile is in the range of 80:20 to 20:80 (taught by Hochberg) as a laundering process to clean and provide fragrance scent to the textile. One of ordinary skill in the art would be motivated to do so as a way of cleaning and providing a fragrance to the textiles. One of ordinary skill in the art would have expectations of success in doing since Baeck, Schubert, and Hochberg provide all the necessary teachings and guidance needed to do so.
Therefore, claims 18-19 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck, and further in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert, as applied to claim 17 above, and further in view of Hochberg et al. (United States Patent No: US 8556993 B2; published October 15, 2013), hereinafter referred to as Hochberg.
Claims 20-21 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck, as applied to claim 13 above, and further in view of Uniprot Database entry (Q8J0K8_MELAO ; deposited March 1, 2003), hereinafter referred to as Q8J0K8.
The teachings of Baeck as applied to claim 13 are summarized above.
With regards to claims 20-21, Baeck does not teach that the enzyme having cellulase activity is selected from the group consisting of glycoside hydrolase family 45 (GH45) or that the enzyme having cellulase activity has at least 60% sequence identity to SEQ ID NO: 6.
However, Q8J0K8 teaches a cellulase belonging to the glycosyl hydrolase 45 family that has 100% sequence identity to SEQ ID NO: 6 of the current instant application (see sequence alignment below).
RESULT 1
Q8J0K8_MELAO
ID Q8J0K8_MELAO Unreviewed; 235 AA.
AC Q8J0K8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 28-JAN-2026, entry version 91.
DE RecName: Full=Cellulase {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE Flags: Precursor;
GN Name=cel45A {ECO:0000313|EMBL:CAD56665.1};
OS Melanocarpus albomyces (Myriococcum albomyces).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Melanocarpus.
OX NCBI_TaxID=204285 {ECO:0000313|EMBL:CAD56665.1};
RN [1] {ECO:0007829|PDB:1L8F}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 22-228, AND DISULFIDE BONDS.
RX PubMed=12657806; DOI=10.1107/s0907444903002051;
RA Valjakka J., Rouvinen J.;
RT "Structure of 20K endoglucanase from Melanocarpus albomyces at 1.8 A
RT resolution.";
RL Acta Crystallogr. D 59:765-768(2003).
RN [2] {ECO:0007829|PDB:1OA7, ECO:0007829|PDB:1OA9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-235, AND DISULFIDE BONDS.
RX PubMed=12767825; DOI=10.1016/s0022-2836(03)00467-4;
RA Hirvonen M., Papageorgiou A.C.;
RT "Crystal structure of a family 45 endoglucanase from Melanocarpus
RT albomyces: mechanistic implications based on the free and cellobiose-bound
RT forms.";
RL J. Mol. Biol. 329:403-410(2003).
RN [3] {ECO:0000313|EMBL:CAD56665.1}
RP NUCLEOTIDE SEQUENCE.
RA Haakana H., Miettinen-Oinonen A., Joutsjoki V., Mantyla A., Suominen P.,
RA Vehmaanpera J.;
RT "Cloning of cellulase genes from Melanocarpus albomyces and their
RT efficientexpression in Trichoderma reesei.";
RL Enzyme Microb. Technol. 34:159-167(2004).
RN [4] {ECO:0000313|EMBL:QCO31627.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang J.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966, ECO:0000256|PROSITE-
CC ProRule:PRU10069};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000256|ARBA:ARBA00007793}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ515703; CAD56665.1; -; Genomic_DNA.
DR EMBL; MH910614; QCO31627.1; -; mRNA.
DR PDB; 1L8F; X-ray; 1.80 A; A=22-228.
DR PDB; 1OA7; X-ray; 2.00 A; A=22-235.
DR PDB; 1OA9; X-ray; 2.00 A; A=22-235.
DR PDBsum; 1L8F; -.
DR PDBsum; 1OA7; -.
DR PDBsum; 1OA9; -.
DR AlphaFoldDB; Q8J0K8; -.
DR SMR; Q8J0K8; -.
DR CAZy; GH45; Glycoside Hydrolase Family 45.
DR BRENDA; 3.2.1.4; 3208.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd22278; DPBB_GH45_endoglucanase; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR052288; GH45_Enzymes.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR39730; ENDOGLUCANASE 1; 1.
DR PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1.
DR Pfam; PF02015; Glyco_hydro_45; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CAD56665.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAD56665.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..235
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044488622"
FT DOMAIN 26..37
FT /note="Glycosyl hydrolases family 45 active site"
FT /evidence="ECO:0000259|PROSITE:PS01140"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069"
FT DISULFID 32..155
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 33..68
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 37..106
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 52..76
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 107..219
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 109..209
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 176..187
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
SQ SEQUENCE 235 AA; 25001 MW; BF9850E83666CD76 CRC64;
Query Match 100.0%; Score 1221; Length 235;
Best Local Similarity 100.0%;
Matches 214; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ANGQSTRYWDCCKPSCGWRGKGPVNQPVYSCDANFQRIHDFDAVSGCEGGPAFSCADHSP 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 22 ANGQSTRYWDCCKPSCGWRGKGPVNQPVYSCDANFQRIHDFDAVSGCEGGPAFSCADHSP 81
Qy 61 WAINDNLSYGFAATALSGQTEESWCCACYALTFTSGPVAGKTMVVQSTSTGGDLGSNHFD 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 82 WAINDNLSYGFAATALSGQTEESWCCACYALTFTSGPVAGKTMVVQSTSTGGDLGSNHFD 141
Qy 121 LNIPGGGVGLFDGCTPQFGGLPGARYGGISSRQECDSFPEPLKPGCQWRFDWFQNADNPS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 142 LNIPGGGVGLFDGCTPQFGGLPGARYGGISSRQECDSFPEPLKPGCQWRFDWFQNADNPS 201
Qy 181 FTFERVQCPEELVARTGCRRHDDGGFAVFKAPSA 214
||||||||||||||||||||||||||||||||||
Db 202 FTFERVQCPEELVARTGCRRHDDGGFAVFKAPSA 235
Therefore, it would have been obvious to one of ordinary skill in the art of protein chemistry before the effective filing date of the current instant application to select the glycosyl hydrolase 45 family cellulase taught by Q8J0K8 and substitute as the enzyme in the wash liquor comprising an enzyme having cellulase activity taught by Baeck. One of ordinary skill in the art would be motivated to do so as Q8JOK8 teach an enzyme having cellulase activity belonging to the glycoside hydrolase family 45 and has 100% sequence identity with SEQ ID NO: 6 of the current instant application in order to provide a functional enzyme with cellulase activity to the wash liquor. One of ordinary of ordinary skill in the art would have expectations in do so as the combined teachings of Baeck and Q8J0K8 provide all the teachings and guidance needed to do so.
Therefore, claims 20-21 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck, as applied to claim 13 above, and further in view of Uniprot Database entry (Q8J0K8_MELAO ; deposited March 1, 2003), hereinafter referred to as Q8J0K8.
Claims 23-24 are rejected under 35 U.S.C. 103 as being unpatentable over Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert, as applied to claim 22 above, and further in view of Uniprot Database entry (Q8J0K8_MELAO ; deposited March 1, 2003), hereinafter referred to as Q8J0K8.
The teachings of Schubert as applied to claim 22 are summarized above.
With regards to claims 23-24, Schubert does not teach that the enzyme having cellulase activity is selected from the group consisting of glycoside hydrolase family 45 (GH45) or that the enzyme having cellulase activity has at least 60% sequence identity to SEQ ID NO: 6.
However, Q8J0K8 teaches a cellulase belonging to the glycosyl hydrolase 45 family that has 100% sequence identity to SEQ ID NO: 6 of the current instant application (see sequence alignment below).
RESULT 1
Q8J0K8_MELAO
ID Q8J0K8_MELAO Unreviewed; 235 AA.
AC Q8J0K8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 28-JAN-2026, entry version 91.
DE RecName: Full=Cellulase {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE Flags: Precursor;
GN Name=cel45A {ECO:0000313|EMBL:CAD56665.1};
OS Melanocarpus albomyces (Myriococcum albomyces).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Melanocarpus.
OX NCBI_TaxID=204285 {ECO:0000313|EMBL:CAD56665.1};
RN [1] {ECO:0007829|PDB:1L8F}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 22-228, AND DISULFIDE BONDS.
RX PubMed=12657806; DOI=10.1107/s0907444903002051;
RA Valjakka J., Rouvinen J.;
RT "Structure of 20K endoglucanase from Melanocarpus albomyces at 1.8 A
RT resolution.";
RL Acta Crystallogr. D 59:765-768(2003).
RN [2] {ECO:0007829|PDB:1OA7, ECO:0007829|PDB:1OA9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-235, AND DISULFIDE BONDS.
RX PubMed=12767825; DOI=10.1016/s0022-2836(03)00467-4;
RA Hirvonen M., Papageorgiou A.C.;
RT "Crystal structure of a family 45 endoglucanase from Melanocarpus
RT albomyces: mechanistic implications based on the free and cellobiose-bound
RT forms.";
RL J. Mol. Biol. 329:403-410(2003).
RN [3] {ECO:0000313|EMBL:CAD56665.1}
RP NUCLEOTIDE SEQUENCE.
RA Haakana H., Miettinen-Oinonen A., Joutsjoki V., Mantyla A., Suominen P.,
RA Vehmaanpera J.;
RT "Cloning of cellulase genes from Melanocarpus albomyces and their
RT efficientexpression in Trichoderma reesei.";
RL Enzyme Microb. Technol. 34:159-167(2004).
RN [4] {ECO:0000313|EMBL:QCO31627.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang J.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966, ECO:0000256|PROSITE-
CC ProRule:PRU10069};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000256|ARBA:ARBA00007793}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ515703; CAD56665.1; -; Genomic_DNA.
DR EMBL; MH910614; QCO31627.1; -; mRNA.
DR PDB; 1L8F; X-ray; 1.80 A; A=22-228.
DR PDB; 1OA7; X-ray; 2.00 A; A=22-235.
DR PDB; 1OA9; X-ray; 2.00 A; A=22-235.
DR PDBsum; 1L8F; -.
DR PDBsum; 1OA7; -.
DR PDBsum; 1OA9; -.
DR AlphaFoldDB; Q8J0K8; -.
DR SMR; Q8J0K8; -.
DR CAZy; GH45; Glycoside Hydrolase Family 45.
DR BRENDA; 3.2.1.4; 3208.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd22278; DPBB_GH45_endoglucanase; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR052288; GH45_Enzymes.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR39730; ENDOGLUCANASE 1; 1.
DR PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1.
DR Pfam; PF02015; Glyco_hydro_45; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CAD56665.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAD56665.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..235
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044488622"
FT DOMAIN 26..37
FT /note="Glycosyl hydrolases family 45 active site"
FT /evidence="ECO:0000259|PROSITE:PS01140"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069"
FT DISULFID 32..155
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 33..68
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 37..106
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 52..76
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 107..219
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 109..209
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 176..187
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
SQ SEQUENCE 235 AA; 25001 MW; BF9850E83666CD76 CRC64;
Query Match 100.0%; Score 1221; Length 235;
Best Local Similarity 100.0%;
Matches 214; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ANGQSTRYWDCCKPSCGWRGKGPVNQPVYSCDANFQRIHDFDAVSGCEGGPAFSCADHSP 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 22 ANGQSTRYWDCCKPSCGWRGKGPVNQPVYSCDANFQRIHDFDAVSGCEGGPAFSCADHSP 81
Qy 61 WAINDNLSYGFAATALSGQTEESWCCACYALTFTSGPVAGKTMVVQSTSTGGDLGSNHFD 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 82 WAINDNLSYGFAATALSGQTEESWCCACYALTFTSGPVAGKTMVVQSTSTGGDLGSNHFD 141
Qy 121 LNIPGGGVGLFDGCTPQFGGLPGARYGGISSRQECDSFPEPLKPGCQWRFDWFQNADNPS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 142 LNIPGGGVGLFDGCTPQFGGLPGARYGGISSRQECDSFPEPLKPGCQWRFDWFQNADNPS 201
Qy 181 FTFERVQCPEELVARTGCRRHDDGGFAVFKAPSA 214
||||||||||||||||||||||||||||||||||
Db 202 FTFERVQCPEELVARTGCRRHDDGGFAVFKAPSA 235
Therefore, it would have been obvious to one of ordinary skill in the art of protein chemistry to select the glycosyl hydrolase 45 family cellulase taught by Q8J0K8 and substitute as the enzyme in the fragrance bead composition comprising an enzyme having cellulase activity taught by Schubert. One of ordinary skill in the art would be motivated to do so as Q8JOK8 teach an enzyme having cellulase activity belonging to the glycoside hydrolase family 45 and has 100% sequence identity with SEQ ID NO: 6 of the current instant application in order to provide a functional enzyme with cellulase activity to the fragrance bead. One of ordinary of ordinary skill in the art would have expectations in do so as the combined teachings of Schubert and Q8J0K8 provide all the teachings and guidance needed to do so.
Therefore, claims 23-24 are rejected under 35 U.S.C. 103 as being unpatentable over Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert, as applied to claim 22 above, and further in view of Uniprot Database entry (Q8J0K8_MELAO ; deposited March 1, 2003), hereinafter referred to as Q8J0K8.
Claim 25-26 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert.
With regards to claim 25 , Baeck teaches a method of treating a fabric with a composition comprising a chemical entity, surfactant, and a protease for fabric cleaning (see claims 18-19) . Baeck teaches that the composition comprises a chemical entity that comprises a deposition aid having high affinity for cellulose and a benefit agent (see claim 1). Baeck teaches that cellulases are preferred as the deposition aid (see lines 1-10, pg.5). Baeck further teaches that the deposition aid is selected from an enzyme comprising a cellulose binding domain (see claim 2). Baeck teaches that the benefit agent is selected from a perfume (see claim 4).
With regards to claim 16, Baeck does not teach that the enzyme having cellulase activity and the one or more fragrance compounds are comprised within a fragrance bead composition or that the fragrance compound in the fragrance bead is reduced.
However, Schubert teaches a fabric care composition comprising a detersive enzyme and a perfume (See Field of invention, lines 5-6, pg. 1, and claim 1 (iii),pg. 88). Schubert teaches that detersive enzyme is preferably selected from cellulases (see lines 30-31, pg. 18). Schubert further teaches that the composition is in the form of a bead (see claim 11, pg. 94). Schubert also teaches that the composition comprises from about 0.005% to about 30%, from about 0.01% to about 20%, or from about 0.02%- to about 10% of a perfume.
It would have been obvious to one of ordinary skill in the art of protein chemistry before the effective date of the current instant application to incorporate the enzyme having cellulase activity and the one or more fragrance compounds taught by Baeck into a bead composition taught by Schubert. One of ordinary skill in the art would be motivated to do so since Schubert teaches that the fabric care composition comprising a cellulase and perfume are in the form of a bead and that his would be a practical way of using the composition for fabric care. One of ordinary skill in the art would have expectations of success in doing so as the combined teachings of Baeck and Schubert provide the necessary guidance and teachings to do so.
It would have been also obvious to one of ordinary skill in the art of protein chemistry before the effective date of the current instant application to adjust the perfume content in the fabric care composition taught by Baeck to be incorporated into the bead composition taught by Schubert according to the ranges of perfume content taught by Schubert. The ranges taught by Schubert allow for a reduction in the amount of perfume in the bead composition. . It is well settled that “discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art. In re Boesch, 617 F.2d 272, 276, 205 USPQ 215, 219 (CCPA 1980) and where the general conditions of a claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art . In re Aller, 220 F2d 454, 456, 105 USPQ 233; 235 (CCPA 1955). One of ordinary skill in the art would be motivated to do so in order to use less fragrance compound which could also lead to cost savings. One of ordinary skill in the art would have expectations of success in doing so as Baeck and Schubert provide all the necessary teachings and guidance needed to do so.
Therefore, claims 25-26 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert.
Claims 27-28 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert, as applied to claim 25 above, and further in view of Uniprot Database entry (Q8J0K8_MELAO ; deposited March 1, 2003), hereinafter referred to as Q8J0K8.
The teachings of Baeck and Schubert as applied to claim 25 above are summarized above.
Niether Baeck or Schubert teach that the enzyme having cellulase activity is selected from GH5, GH7, GH12, GH44 and glycoside hydrolase family 45 (GH45) or that the enzyme having cellulase activity is a polypeptide having at least 60% sequence identity to SEQ ID NO: 1-6.
However, Q8J0K8 teaches a cellulase belonging to the glycosyl hydrolase 45 family that has 100% sequence identity to SEQ ID NO: 6 of the current instant application (see sequence alignment below).
RESULT 1
Q8J0K8_MELAO
ID Q8J0K8_MELAO Unreviewed; 235 AA.
AC Q8J0K8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 28-JAN-2026, entry version 91.
DE RecName: Full=Cellulase {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE Flags: Precursor;
GN Name=cel45A {ECO:0000313|EMBL:CAD56665.1};
OS Melanocarpus albomyces (Myriococcum albomyces).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Melanocarpus.
OX NCBI_TaxID=204285 {ECO:0000313|EMBL:CAD56665.1};
RN [1] {ECO:0007829|PDB:1L8F}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 22-228, AND DISULFIDE BONDS.
RX PubMed=12657806; DOI=10.1107/s0907444903002051;
RA Valjakka J., Rouvinen J.;
RT "Structure of 20K endoglucanase from Melanocarpus albomyces at 1.8 A
RT resolution.";
RL Acta Crystallogr. D 59:765-768(2003).
RN [2] {ECO:0007829|PDB:1OA7, ECO:0007829|PDB:1OA9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-235, AND DISULFIDE BONDS.
RX PubMed=12767825; DOI=10.1016/s0022-2836(03)00467-4;
RA Hirvonen M., Papageorgiou A.C.;
RT "Crystal structure of a family 45 endoglucanase from Melanocarpus
RT albomyces: mechanistic implications based on the free and cellobiose-bound
RT forms.";
RL J. Mol. Biol. 329:403-410(2003).
RN [3] {ECO:0000313|EMBL:CAD56665.1}
RP NUCLEOTIDE SEQUENCE.
RA Haakana H., Miettinen-Oinonen A., Joutsjoki V., Mantyla A., Suominen P.,
RA Vehmaanpera J.;
RT "Cloning of cellulase genes from Melanocarpus albomyces and their
RT efficientexpression in Trichoderma reesei.";
RL Enzyme Microb. Technol. 34:159-167(2004).
RN [4] {ECO:0000313|EMBL:QCO31627.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang J.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966, ECO:0000256|PROSITE-
CC ProRule:PRU10069};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000256|ARBA:ARBA00007793}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ515703; CAD56665.1; -; Genomic_DNA.
DR EMBL; MH910614; QCO31627.1; -; mRNA.
DR PDB; 1L8F; X-ray; 1.80 A; A=22-228.
DR PDB; 1OA7; X-ray; 2.00 A; A=22-235.
DR PDB; 1OA9; X-ray; 2.00 A; A=22-235.
DR PDBsum; 1L8F; -.
DR PDBsum; 1OA7; -.
DR PDBsum; 1OA9; -.
DR AlphaFoldDB; Q8J0K8; -.
DR SMR; Q8J0K8; -.
DR CAZy; GH45; Glycoside Hydrolase Family 45.
DR BRENDA; 3.2.1.4; 3208.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd22278; DPBB_GH45_endoglucanase; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR052288; GH45_Enzymes.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR39730; ENDOGLUCANASE 1; 1.
DR PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1.
DR Pfam; PF02015; Glyco_hydro_45; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CAD56665.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAD56665.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..235
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044488622"
FT DOMAIN 26..37
FT /note="Glycosyl hydrolases family 45 active site"
FT /evidence="ECO:0000259|PROSITE:PS01140"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069"
FT DISULFID 32..155
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 33..68
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 37..106
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 52..76
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 107..219
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 109..209
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
FT DISULFID 176..187
FT /evidence="ECO:0007829|PDB:1L8F, ECO:0007829|PDB:1OA7"
SQ SEQUENCE 235 AA; 25001 MW; BF9850E83666CD76 CRC64;
Query Match 100.0%; Score 1221; Length 235;
Best Local Similarity 100.0%;
Matches 214; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 ANGQSTRYWDCCKPSCGWRGKGPVNQPVYSCDANFQRIHDFDAVSGCEGGPAFSCADHSP 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 22 ANGQSTRYWDCCKPSCGWRGKGPVNQPVYSCDANFQRIHDFDAVSGCEGGPAFSCADHSP 81
Qy 61 WAINDNLSYGFAATALSGQTEESWCCACYALTFTSGPVAGKTMVVQSTSTGGDLGSNHFD 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 82 WAINDNLSYGFAATALSGQTEESWCCACYALTFTSGPVAGKTMVVQSTSTGGDLGSNHFD 141
Qy 121 LNIPGGGVGLFDGCTPQFGGLPGARYGGISSRQECDSFPEPLKPGCQWRFDWFQNADNPS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 142 LNIPGGGVGLFDGCTPQFGGLPGARYGGISSRQECDSFPEPLKPGCQWRFDWFQNADNPS 201
Qy 181 FTFERVQCPEELVARTGCRRHDDGGFAVFKAPSA 214
||||||||||||||||||||||||||||||||||
Db 202 FTFERVQCPEELVARTGCRRHDDGGFAVFKAPSA 235
Therefore, it would have been obvious to one of ordinary skill in the art of protein chemistry to select the glycosyl hydrolase 45 family cellulase taught by Q8J0K8 and substitute as the enzyme in the fragrance bead comprising an enzyme having cellulase activity taught by the combined teachings of Baeck and Schubert. One of ordinary skill in the art would be motivated to do so as Q8JOK8 teach an enzyme having cellulase activity belonging to the glycoside hydrolase family 45 and has 100% sequence identity with SEQ ID NO: 6 of the current instant application in order to provide a functional enzyme with cellulase activity to the wash liquor. One of ordinary of ordinary skill in the art would have expectations in do so as the combined teachings of Baeck, Schubert and Q8J0K8 provide all the teachings and guidance needed to do so.
Claims 27-28 are rejected under 35 U.S.C. 103 as being unpatentable over Baeck et al. (WIPO International Publication Number: WO 00/18864; published April 6, 2000), hereinafter referred to as Baeck in view of Schubert et al. (WIPO International Publication Number WO 2017/011249 A1; published January 19, 2017), hereinafter referred to as Schubert, as applied to claim 25 above, and further in view of Uniprot Database entry (Q8J0K8_MELAO ; deposited March 1, 2003), hereinafter referred to as Q8J0K8.
Double Patenting
Claims 13, 15, 20, and 21 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 18-19, and 21-28, and 34 of copending Application No. 18/548,506, hereinafter referred to as ‘506. Although the claims at issue are not identical, they are not patentably distinct from each other because: claims 18, 19, 21-28, and 34 of copending ‘506 are drawn to a method of improving the deposition of a fragrance onto a textile from a consumer product composition, the method comprising the step of contacting the textile with a consumer product composition comprising an enzyme having cellulase activity and a fragrance; wherein improving the deposition of the fragrance comprises increasing the deposition of the fragrance on the textile; wherein the enzyme having cellulase activity is selected from glycoside hydrolase family 5 (GH5), glycoside hydrolase family 7 (GH7), glycoside hydrolase family 12 (GH12), glycoside hydrolase family 44 (GH44) and glycoside hydrolase family 45 (GH45); wherein the cellulase has at least 60%, 65%, 70%, 80%, 90%, 95%, 99% sequence identity to SEQ ID NOs: 1-6; and wherein the consumer product composition is a detergent, encompass and anticipate instant application claims 13, 14, 15, and 20-21 drawn to a method for increasing deposition of a fragrance compound to a textile, the method comprising exposing the textile to a wash liquor comprising an enzyme having cellulase activity and one or more fragrance compounds; wherein the enzyme having a cellulase activity is comprised within a cleaning solution; wherein the cleaning composition is a laundry detergent, wherein the enzyme having cellulase activity is selected from the group of glycoside hydrolase family 5 (GH5), glycoside hydrolase family 7 (GH7), glycoside hydrolase family 12 (GH12), glycoside hydrolase family 44 (GH44) and glycoside hydrolase family 45 (GH45); wherein the enzyme having cellulase activity is a polypeptide having at least 60%, 65%, 70%, 80%, 90%, 95%, 99% sequence identity to SEQ ID NOs: 1-6
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claims are allowed.
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/GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652
/ROBERT B MONDESI/ Supervisory Patent Examiner, Art Unit 1652
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