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 .
DETAILED ACTION
This application is a US national phase of PCT/EP2021/058998, filed April 7, 2021, that has foreign priority application EP20168634.2, filed April 8, 2020.
Applicant’s amendment filed November 26, 2025 is acknowledged. Claims 1-40 are canceled, and claims 41-62 are newly added, wherein claims 52 and 62 are withdrawn as being directed to a previously non-elected invention.
Currently claims 41-51 and 53-61 are under examination.
Claim Rejections - 35 USC § 112
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 41-49, 51, 53-59 and 61 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 claims contain 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.
Claims 41 and 53 recite a glycoside hydrolase, comprising (a) one or more catalytic domains from a polypeptide having glycoside hydrolase activity; (b) one or more linkers; and (c) one or more variants of claim comprising a substitution at the recited positions in claims 41/53 with at least 80%/85% sequence identity to SEQ ID NO: 173’. Claims 49 and 59 recite specific linker sequences. Claims 50 and 60 recites glycoside hydrolase variants comprising specific catalytic domain SEQ ID NO: 5 having recited mutations, specific linker SEQ ID NO: 30, and specific carbohydrate binding module (CBM) variants. Claims 51 and 61 recite a detergent composition comprising the glycoside hydrolase of claims 41 and 53, respectively.
The Specification defines ‘catalytic domains having glycoside hydrolase activity’ as the region of an enzyme containing the catalytic machinery of the enzyme and the glycoside hydrolase enzyme catalyzes the hydrolysis of a glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety, which may contain one or more catalytic domains, such as from the families GH5, GH6, GH7, GH8, GH9, GH12, GH44, GH45, GH48, GH51, GH124, with family GH45 being particularly preferred. The Specification defines the ‘linker’ as linking the catalytic domain and CBM, and the proline-rich linker comprises one or more Pro-Pro, Pro-Xaa (or Xaa-Pro), Xaa-Pro-Xaa or Xaa-Xaa-Pro (or Pro-Xaa-Xaa) units in repetition, and can be at least 25%-90% proline. To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116.
In analyzing whether the written description requirement is met for genus claims, it is first determined whether a representative number of species have been described by their complete structure. In the instant case, the specification merely gives working examples of glycoside hydrolase variants comprising a catalytic domain, linker, and CBM according to SEQ ID NO’s: 1-2, as well as variants comprising catalytic domain SEQ ID NO: 5 (with specified mutations), CBM SEQ ID NO: 173 (with specified mutations), and 58 linkers from SEQ ID NO’s: 30-97, and are the only species whose complete structure is disclosed. While the genus encompasses a large number of variants that have the same activity as glycoside hydrolase variants comprising catalytic domains having glycoside hydrolase activity and linkers in kind and the genus encompasses a large number of variants that have a different structure, the specification does not describe the complete structure of a representative number of species of the large genus of glycoside hydrolase variants comprising catalytic domains having glycoside hydrolase activity and linkers or functional equivalents thereof.
Next, then, it is determined whether a representative number of species have been sufficiently described by other relevant identifying characteristics (i.e., other than nucleotide sequence or amino acid sequence), specific features and functional attributes that would distinguish different members of the claimed genus. In the instant case, the only other identifying characteristic of a linker can be considered as a variant of the linker of the parent molecule, having stabilizing point mutations, including mutations to proline, and the glycoside hydrolase variants have an improved property relative to a reference enzyme/parent enzyme (such as residual activity), as well as improved stability/shelf life in detergents comprising proteases. Such broad limitations cannot be an identifying characteristic for the claimed diverse genus of glycoside hydrolase variants comprising a catalytic domain having glycoside hydrolase activity, linker, and CBM variant, since by Applicant’s definition of variant or functional equivalent thereof all members of the claimed genus will have that characteristic. Further, no other identifying characteristics of the catalytic domains having glycoside hydrolase activity and linkers are disclosed, only the variants comprising SEQ ID NO: 5 (with specified mutations) and the 58 linkers from SEQ ID NO’s: 30-97, though no degree of the variation of these variants were disclosed (such as percent identity to the respective parent enzymes).
The inventions of claims 42-49, 51, 54-59, and 61 require the use of the inventions of claims 41 and 53, and therefore are likewise rejected under 35 U.S.C. 112, first paragraph, as failing to comply with the written description requirement.
In conclusion, Applicant’s disclosure of the species of glycoside hydrolase comprising a catalytic domain having glycoside hydrolase activity, one or more linkers, and one or more CBM variants of claims 41 and 53 of the claimed broad genus is not deemed sufficient to reasonably convey to one skilled in the art that Applicant was in possession of the claimed broad genus at the time the application was filed. Thus, it is concluded that the written description requirement is not satisfied for the claimed genus.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 47 and 58 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Both claims 47 and 58 repeat the same limitation of claims 46 and 57, respectively, from which they depend, and fail to further limit the amino acid substitution of the claims upon which they depend.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 41-51 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a naturally occurring product without significantly more.
The Supreme Court has required analysis based on a 3-part test for subject matter eligibility.
Step 1: Is the claim to a process, machine, manufacture, or composition of matter?
Step 2A (The Judicial Exceptions): Prong 1: Is the claim directed to a law of nature, a natural phenomenon (product of nature), or an abstract idea?
Step 2A (The Judicial Exceptions): Prong 2: Does the claim recite additional elements that integrate the judicial exception into a practical application?
Step 2B: Does the claim recite additional elements that amount to significantly
more than the judicial exception?
Claims 41-51 recite a glycoside hydrolase comprising one or more catalytic domains, one or more linkers, and one or more variants of a carbohydrate binding module (CBM) comprising a substitution at one or more positions corresponding to positions 18, 21, 27, 29, 34, and 37 wherein the polypeptide has at least 80% sequence identity to SEQ ID NO: 173, which is a statutory category of invention (Step 1: Yes).
The claims recite variants of SEQ ID NO: 173 which is a fungal cellulose binding domain in the enzyme cellulose 1,4-beta-cellobiosidase from Thermochaetoides thermophila (NCBI Accession # CAM98448.1, Vehmaanpera J. Direct Submission, Submitted (13-MAY-2007) to the INSDC. Voutilainen S., Roal Oy, Tykkimaentie 15, POBox 57, Rajamaki 05201, Finland, cited in PTO-892 mailed 7/29/2025).
Because claim 41 recites variants with 80% or more identity to SEQ ID NO: 173, the scope is broad to include any naturally occurring variant, such as the protein sequence, TWF718_002811 from Orbilia javanica (Palmer, KAK6330614, Direct Submission, Submitted (23-OCT-2019) CFMR, USDA Forest Service, 1 Gifford Pinchot Drive, Madison, WI 53726, USA) that comprises a glycoside hydrolase 131 catalytic domain, a linker, and a cellulose binding domain (CBM1), wherein the CBM1 has 82% identity to SEQ ID NO: 173 and comprises substitution T27Q. Thus the claims recite a judicial exception in the form of a product of nature (Step 2A, Prong 1: Yes).
Claim 51 recites detergent compositions comprising the glycoside hydrolase variants. As evidenced by Schnorr et al. (WO 2005/042735 A1, cited in PTO-892 mailed 7/29/2025), it is well-understood and routine in the industry to combine catalytic domains, linkers, and CBMs to be incorporated into detergent compositions (abstract, pg. 8, lines 9-17). The claims do not recite additional elements that integrate it into a practical application, only reciting variants and a generic application of a detergent composition comprising the glycoside hydrolases (Step 2A Prong 2, No). Claims 41-51 do not recite additional elements that amount to significantly more than the judicial exception (Step 2B: No.).
Therefore, claims 41-51 are not patent eligible subject matter.
Claim Rejections - 35 USC § 102
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.
Claims 41 and 45 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Palmer (KAK6330614, Direct Submission, Submitted (23-OCT-2019) CFMR, USDA Forest Service, 1 Gifford Pinchot Drive, Madison, WI 53726, USA).
Palmer teaches a hypothetical protein TWF718_002811 derived from Orbilia javanica that comprises a glycoside hydrolase 131 catalytic domain, a linker, and a cellulose binding domain (CBM1), wherein the CBM1 has 82% identity to SEQ ID NO: 173 and comprises substitution T27Q, which anticipates claims 41 and 45 (See sequence comparison below).
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Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 41-48 and 53-58 are rejected under 35 U.S.C. 103 as being unpatentable over Voutilainen et al. (Biotechnology and Bioengineering, 2008, Vol. 101, No. 3, pgs. 515-528, hereinafter “Voutilainen”) in view of Nishijima, (PhD Dissertation, Shinshu University, 2015, pgs. 1-98, cited in PTO-892 mailed 7/29/2025), and Betts et al. (Ch. 14, Bioinformatics for Geneticists, 2003, John Wiley & Sons, Ltd, pgs. 289-316, cited in PTO-892 mailed 7/29/2025, hereinafter “Betts”).
Regarding claims 41-48, Voutilainen teaches cloning, expression and characterization of novel thermostable family 7 cellobiohydrolases (title). Voutilainen teaches many cellulases have a bimodular organization composed of a catalytic module linked to a carbohydrate binding module (CBM), which helps the enzymatic action on solid substrates (pg. 515, col. 2, para 2). Voutilainen teaches the construction of fusion proteins comprising Thermoascus aurantiacus Cel7A, and the CBM1 from Chaetomium thermophilum, which is 100% identical to SEQ ID NO: 173 (pg. 517, col. 1, para 3, NCBI Accession # CAM98448.1, cited in PTO-892 mailed 7/29/2025). Voutilainen teaches all family-1 CBMs contain 35–36 amino acids and show strong sequence similarity, some residues being fully conserved and some showing conservative substitutions, wherein there are 2 or 3 disulphide bridges that stabilize the structure, and three conserved aromatic amino acid residues (tyrosines, tryptophans, or histidines) on the flat face of the CBM (Y491, Y517, and Y518 in Tr CBM numbering, Fig. 8) shown to be involved in binding to the cellulose surface (pg. 520, col. 1, para 2). Voutilainen teaches Ct Cel7A was the most active enzyme on soluble substrates, the specific activity on being 2- to 11-fold higher than for the other Cel7A enzymes (pg. 524, col.1, para 1).
Voutilainen does not teach a S34Y substitution in the CBM1.
However, Nishijima teaches structure function relations of family 1 CBMs for white-rot fungi (title). Nishijima teaches CBM1 facilitates adsorption on cellulose and enhances its degradation and three aromatic amino acid residues located on the flat surface of CBM1 are essential for the adsorption on cellulose, such as the motifs Y-YY, W-WY, W-YY, Y-WY, and Y-FY (pg. 7, sec. 1.1, pg. 8, sec. 1.3) (which corresponds to AA 32-34 W-YS of SEQ ID NO: 173). Cel6A from Trichoderma reesi can adsorb on cellulose for a longer period than Cel7A because of its higher binding parameters; its motif is W-Y-Y, also the CBM1 from Cel6A has an additional S-S bond, which produces a stable structure and conveys a binding capacity that differs from that of conventional CBM1 (pg. 8, sec. 1.3). Nishijima teaches Irpex lacteus, a kind of white-rot fungus, is known as a strong cellulase and been found to be very efficient in lignocellulose degradation compared with other fungi, and found a xylanase (Xyn10B) comprising regions of CBM1 and the catalytic domain are from Val 21 to Leu 55 and from Leu 88 to Ser 383, respectively (pg. 33, para 1, pg. 41, sec. 3.2.4). Nishijima teaches multiple CBM1’s from I. lacteus, wherein xyn10a and xyn10c comprise the motif YSQC (corresponding to AA 33-36 of SEQ ID NO: 173), whereas Xyn10B has the CBM1 motif YYQC (pg. 46, Table 3-1, See sequence comparison below). Thus, Nishijima discloses the S34Y substitution in their teachings of the YSQC and YYQC motifs when comparing CBM1 variants.
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Nishijima teaches a mutational study wherein the CBM1 from Xyn10B is mutated Y52S (corresponding to S34 of SEQ ID NO: 173), which cellulose absorption decreased significantly compared with the native protein, which suggests that the aromatic residue Tyr 52 plays an important role in defining the binding affinity, thus, CBM Xyn10B contains a unique motif (W-YYY) that facilitates strong cellulose adsorption (pg. 72, para 3, Table 4-2).
Betts teaches conservative amino acid substitutions such as tyrosine (Y), phenylalanine (F), and tryptophan (W), have very hydrophobic side chains and are commonly exchanged/substituted with one another (sec. 14.4.1.2, sec. 14.5.6.1). Betts also discloses asparagine (N) and serine (S) are neutral polar amino acids, and can be substituted by other polar AA’s, such as W or Y (sec. 14.4.2, sec. 14.5.16.1).
Regarding claims 46-48, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to construct a glycoside hydrolase comprising a catalytic domain, linker, and CBM1 as taught by Voutilainen and modify the CBM1 with a S34Y substitution, as taught by Nishijima and Betts, with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to mutate the ‘YSQC’ motif with the motif ‘YYQC’ to enhance cellulose absorption and degradation by a glycoside hydrolase as taught in the mutational studies by Nishijima. Furthermore, mutating only S34Y in the CBM1 from C. thermophilum would be 97.3% identical to SEQ ID NO: 173, which meets the limitations of claims 42-44.
Regarding claims 53-58, Voutilainen teaches cloning, expression and characterization of novel thermostable family 7 cellobiohydrolases (title). Voutilainen teaches many cellulases have a bimodular organization composed of a catalytic module linked to a carbohydrate binding module (CBM), which helps the enzymatic action on solid substrates (pg. 515, col. 2, para 2). Voutilainen teaches the construction of fusion proteins comprising Thermoascus aurantiacus Cel7A and the CBM1 from Chaetomium thermophilum, which is 100% identical to SEQ ID NO: 173 (pg. 517, col. 1, para 3, NCBI Accession # CAM98448.1, cited in PTO-892 mailed 7/29/2025). Voutilainen teaches all family-1 CBMs contain 35–36 amino acids and show strong sequence similarity, some residues being fully conserved and some showing conservative substitutions, wherein there are 2 or 3 disulphide bridges that stabilize the structure, and three conserved aromatic amino acid residues (tyrosines, tryptophans, or histidines) on the flat face of the CBM (Y491, Y517, and Y518 in Tr CBM numbering, Fig. 8) shown to be involved in binding to the cellulose surface (pg. 520, col. 1, para 2). Voutilainen teaches Ct Cel7A was the most active enzyme on soluble substrates, the specific activity on being 2- to 11-fold higher than for the other Cel7A enzymes (pg. 524, col.1, para 1). Voutilainen teaches a Y14W variable substitution in the CBM1 domains between C. thermophilum and A. thermophilum in Figure 8 (pg. 526).
Nishijima also teaches structure function relations of family 1 CBMs for white-rot fungi (title). Nishijima teaches CBM1 facilitates adsorption on cellulose and enhances its degradation. The CBM1 of Xyn10B also has a Y14F and A22S substitution when aligned with SEQ ID NO: 173.
Betts teaches conservative amino acid substitutions such as tyrosine (Y), phenylalanine (F), and tryptophan (W), have very hydrophobic side chains and are commonly exchanged/substituted with one another (sec. 14.4.1.2, sec. 14.5.6.1). Betts also discloses asparagine (N) and serine (S) are neutral polar amino acids, and can be substituted by other polar AA’s (sec. 14.4.2, sec. 14.5.16.1). Thus the Y14W substitution recited in claims 53-58 would be a conservative substitution in the CBM’s taught by Voutilainen and Nishijima, since W & Y are commonly substituted for one another as a well-understood, and routine practice in the art as suggested by Betts. Furthermore, mutating only Y14W in the CBM1 from C. thermophilum would be 97.3% identical to SEQ ID NO: 173, which meets the limitations of claims 53-55.
Therefore it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to construct a glycoside hydrolase comprising a catalytic domain, linker, and CBM1 as taught by Voutilainen and modify the CBM1 with a Y14 substitution taught by Nishijima, and substitute with W for a Y14W substitution as taught by Betts with a reasonable expectation of success. One of ordinary skill in the art before the effective filing date would have made this routine substitution of Y to W at the 14 position based on the CBM1 taught by Nishijima, as this is a common AA substitution in the art.
Claim 49 and 59 are rejected under 35 U.S.C. 103 as being unpatentable over Voutilainen in view of Nishijima, and Betts as applied to claims 41-48 and 53-58 above, and further in view of Cooper et al. (Mol Gen Genet (1993) 241:341-350, cited in PTO-892 mailed 7/29/2025, hereinafter “Cooper”), and Chen et al. (Adv Drug Deliv Rev. 2013 October 15; 65(10): 1357–1369, cited in PTO-892 mailed 7/29/2025, hereinafter “Chen”)..
As described above, Voutilainen and Nishijima teach glycoside hydrolase comprising CBM1 variants and a linker, though neither teach the specific linkers recited in claims 49 and 59.
However, Cooper teaches molecular analysis of the major cellulase CelV, which comprises two functional domains in the enzyme; a catalytic domain linked by a short proline/threonine-rich linker to a cellulose-binding domain (CBD) (abstract). Cooper teaches the linker, a short Pro-Thr box (TPTTPTEPTNP) is present in CelV between amino acids Thr338 and Pro349 (pg. 343, col. 2, para 1).
Although Cooper does not explicitly teach one of the recited linker sequences, only partially teaching SEQ ID NO’s: 17 & 18, many such linkers are known or suggested in the prior art.
Chen teaches in Table 2, proline-rich linkers can have a structure as simple as (XP)n wherein X can be any amino acid residue, wherein Table 3 of Chen gives an example of an AlaPro repeat linker of 10-34 amino acid residues. As such, forming an (XP)n linker of n=5 wherein X can be Ala, Thr, or Serine (i.e. recited SEQ ID NO: 17 or 18 when Thr is selected) as a linker is consistent with the formula (XP)n is a matter of design choice when a genus of linkers with a high proline content are suggested by the prior art for linking a glycoside hydrolase or cellulase enzyme with a CBD/CBM domain (pg. 5, sec. 3.2).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to construct a glycoside hydrolase comprising a catalytic domain, linker, and CBM1 with a modified CBM1 comprising a S34Y substitution as taught by Voutilainen and Nishijima, and modify the linker to be a proline-rich linker such as a Pro-Thr box motif taught by Cooper and Chen with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to design a Pro-Thr box linker to link the CBM1 and catalytic domains to confer stability between the domains of the enzyme, when the spatial separation of the domains is critical to preserve the stability or bioactivity of the fusion proteins, as disclosed by Chen (pg. 6, para 2). Furthermore, it would have been prima facie obvious to one in the art to design any of the recited linkers in claims 49 and 59, as this is a common, routine, and well-understood practice in the art.
Claims 50 and 60 are rejected under 35 U.S.C. 103 as being unpatentable over Voutilainen in view of Nishijima, and Betts as applied to claims 41-48 and 53-58 above, and further in view of Kaasgaard et al. (US11661592B2, PCT priority filing date 4/12/2019, cited in PTO-892 mailed 7/29/2025, hereinafter “Kaasgaard”), Cooper, and Chen.
As discussed in the 103 rejection above, Voutilainen and Nishijima teach glycoside hydrolase comprising a catalytic domain, linker, and CBM1, wherein the CBM1 has substitution S34Y or Y14W. Neither reference teach the specific glycoside hydrolase recited in claims 50 and 60.
However, Kaasgaard teaches variants having endoglucanase activity, and teaches AA 1-212 of SEQ ID NO: 1 has 100% identity to instant SEQ ID NO: 5 (catalytic domain), and recites the same substitutions in claims 50 and 60 (claim 1, See sequence comparison below). SEQ ID NO: 1 also comprises a linker between 213-241, and a CBM between 242-277 that has 76.4% identity to SEQ ID NO: 173, comprising substitutions at Y14 & A22. Kaasgaard teaches substitutions N134D, A146D, and Q169Y conferred increased residual activity ratio to the enzyme during an assay (Table 1).
Cooper teaches molecular analysis of the major cellulase CelV, which comprises two functional domains in the enzyme; a catalytic domain linked by a short proline/threonine-rich linker to a cellulose-binding domain (CBD) (abstract). Cooper teaches the linker, a short Pro-Thr box (TPTTPTEPTNP) is present in CelV between amino acids Thr338 and Pro349 (pg. 343, col. 2, para 1).
Although Cooper does not explicitly teach one of the recited linker sequences, only partially teaching SEQ ID NO’s: 17 & 18, many such linkers are known or suggested in the prior art. Chen teaches in Table 2, proline-rich linkers can have a structure as simple as (XP)n wherein X can be any amino acid residue, wherein Table 3 of Chen gives an example of an AlaPro repeat linker of 10-34 amino acid residues. As such, forming an (XP)n linker of n=5 wherein X can be Ala, Thr, or Serine (i.e. recited SEQ ID NO: 17 or 18 when Thr is selected) as a linker is consistent with the formula (XP)n is a matter of design choice when a genus of linkers with a high proline content are suggested by the prior art for linking a glycoside hydrolase or cellulase enzyme with a CBD/CBM domain (pg. 5, sec. 3.2).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to construct a glycoside hydrolase comprising a catalytic domain, linker, and CBM1 with a modified CBM1 comprising a S34Y substitution as taught by Voutilainen and Nishijima, and modify the linker to be a proline-rich linker such as a Pro-Thr box motif taught by Cooper and Chen, and also modify the glycoside hydrolase catalytic region, wherein the catalytic region is AA 1-212 of SEQ ID NO: 1 with the specified substitutions as taught by Kaasgaard with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to formulate a glycoside hydrolase variant with the catalytic region of SEQ ID NO: 1 and specified substitutions, specifically N134D, A146D, and Q169Y, which would confer increased residual activity ratio to the enzyme as taught by Kaasgaard.
Claims 51 and 61 are rejected under 35 U.S.C. 103 as being unpatentable over Voutilainen in view of Nishijima, and Betts as applied to claims 41-48 and 53-58 above, and further in view of Bott et al. (US 11053488B2, cited in PTO-892 mailed 7/29/2025, hereinafter “Bott”).
As discussed above, Voutilainen and Nishijima teach glycoside hydrolases comprising a catalytic domain, linker, and CBM1 variants. Voutilainen teaches the cellulases are a group of enzymes that can hydrolyze the b-1,4-linkage between the glucose units of the cellulose chain and are important industrial enzymes, which can be used, for example, in the pulp and paper, textile, and detergent industries (pg. 515, col. 2, para 1). Nishijima teaches several commercial enzyme preparations have been applied for quality improvement of detergent, in the paper-making industry, and for bioethanol production from cellulosic biomass (pg. 7, sec. 1.7). Neither reference explicitly teaches the glycoside hydrolase is part of a detergent composition.
However, Bott teaches polypeptides with endoglucanase activity comprising a cellulose binding module (CBM) and a catalytic domain that are separated by a flexible spacer known as a “linker” or “linker peptide”, and teaches the cellulase variant can be a part of a detergent composition (claims 12-13).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to formulate a detergent composition comprising a glycoside hydrolase variant as taught by Bott, and suggested by Voutilainen and Nishijima.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
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Claims 41-49, 53-59, and 61 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-6, 8, 10, and 12 of copending Application No. 18/700134 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are anticipated by the copending claims:
Claims 1, 3-6, 8, and 10 of ‘134 recite a polypeptide having endoglucanase activity comprising a catalytic domain, linker, and CBM. Claims 3, 8, and 10 recite the CBM has at least 80% identity to SEQ ID NO’s: 395-401, which SEQ ID NO’s: 395 & 396 are 100% identical to SEQ ID NO: 173 with a S34H & L37R and A22N & S34H substitutions, respectively, thus anticipating the instant claims. Claims 1 and 4-6 also recites the linker is in the form of (P/X)aG wherein the value of a is in the range 8-16, X is selected from the amino acids G, V, N, F and D, and (P/X)a specifies that each position in the linker is selected from the group consisting of the amino acids G, V, N, F, D and P, and wherein further the linker comprises at least one and not more than five amino acids selected from the group consisting of G, V, N, F and D, which anticipates the specified linkers in instant claims 49 and 59. Claim 12 of ‘134 recites a composition comprising the endoglucanase polypeptide and at least one detergent component, anticipating claims 51 and 61.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 41-51 and 53-61 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10 and 12 of copending Application No. 18/700134 in view of Kaasgaard.
As discussed above, claims 41-49, 53-59, and 61 are anticipated by ‘134. Claims 2 and 7 of ‘134 recite the catalytic domain has 80% identity to SEQ ID NO: 394, which has 97% identity to instant SEQ ID NO: 5, but ‘134 does not recite the specific substitutions in instant claims 50 and 60.
However, Kaasgaard teaches variants having endoglucanase activity, and teaches AA 1-212 of SEQ ID NO: 1 has 100% identity to instant SEQ ID NO: 5, and recites the same substitutions in claim 38 (claim 1). SEQ ID NO: 1 also comprises a linker between 213-241, and a CBM between 242-277 that has 76.4% identity to SEQ ID NO: 173, comprising substitutions at Y14 & A22 (See sequence comparison above in 102 rejection). Kaasgaard teaches substitutions N134D, A146D, and Q169Y conferred increased residual activity ratio to the enzyme during an assay (Table 1).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to formulate an endoglucanase variant comprising the CBM1 according to SEQ ID NO: 395, a proline-rich linker, and a glycoside hydrolase catalytic region according to SEQ ID NO: 394 recited by ‘134, and modify the catalytic region with the specified substitutions taught by Kaasgaard with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to formulate an endoglucanase variant with the catalytic region of SEQ ID NO: 394 and specified substitutions, specifically N134D, A146D, and Q169Y, which would confer increased residual activity ratio to the enzyme as taught by Kaasgaard.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant’s arguments with respect to claims 24-39 have been considered but are moot because the new ground of rejection does not rely on any reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument.
Conclusion
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 nonprovisional extension fee (37 CFR 1.17(a)) 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 mailing date of this final action.
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/JESSICA EDWARDS/
Examiner, Art Unit 1657