DETAILED ACTION
Applicant’s amendment submitted on 1/20/2026 is acknowledged. Claim 1 is currently amended. Claims 14-15 remain withdrawn pursuant to 37 CFR 1.142(b) as being drawn to a non-elected invention. Claims 1-19 remain pending in the instant application.
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 .
Priority
The instant application is a U.S. National Phase of PCT/EP2020/075137, filed on 9/9/2020, and claims foreign priority to EP19196411.3, filed on 9/10/2019.
Response to Amendment
Applicant’s amendment to claim 1 to require a recombinant whole fermentation broth produced by a recombinant filamentous fungus overcomes the 35 U.S.C. 101 rejection of claims 1-13 and 16-19 previously set forth in the Non-Final Rejection mailed on 10/20/2025. Accordingly, the rejection is withdrawn.
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.
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.
New Rejection Necessitated by Amendment: Claims 1-13 and 16-19 are rejected under 35 U.S.C. 103 as being unpatentable over WO2014/058896A1 to Schnorr et al; of record in IDS filed 3/3/2022, as evidenced by UniProt-P07982-GUN2_HYPJE (published 08/1988; hereinafter UniProt; of record).
Regarding claim 1, Schnorr teaches an enzyme composition comprising 10% of Trichoderma reesei GH5 endoglucanase II, 37% Aspergillus fumigatus Cel7A cellobiohydrolase I, 5% Aspergillus fumigatus GH10 xylanase, and 5% Aspergillus fumigatus β-glucosidase (see Example 6, p.74-76, lines 6-14). Schnorr further teaches using the enzyme composition disclosed above in the presence and absence of lytic polysaccharide monooxygenase GH61 from Taloromyces byssochlamydoides to investigate the composition’s effect in hydrolyzing milled unwashed pretreated corn stover as cellulase-containing substrate (see Example 7, p.76, lines 18-23). Thus, the addition of lytic polysaccharide monooxygenase to the enzyme composition disclosed in Example 6 reduces the amount of endoglucanase to an amount less than 10% (w/w) of the total amount of protein in the composition. The composition of Schnorr has a REG of 0.21 (0.21 = 10/(10+37). While Schnorr teaches an REG outside of the ranges claimed in claim 1 and 16-19, one of ordinary skill in the art would have found it obvious, before the effective filing date of the claimed invention, to arrive at an REG ratio within the claimed ranges by reducing the percentage of Trichoderma reesei GH5 endoglucanase II through routine experimentation. Schnorr discloses the optimum amount of enzymes and a polypeptide having cellulolytic enhancing activity, of which endoglucanase II is a species, depend on several factors and suggests wide ranges of amounts of enzymes and polypeptide (see paragraph bridging p.51-52, p.52, 1st-3rd paragraphs). Thus, one of ordinary skill in the art would have had motivation to optimize the amount of endoglucanase II as disclosed in the example of Schnorr and arrive at concentration rendering an REG within the ranges disclosed in claims 1 and 16-19 because Schnorr suggests the amount of enzyme can be optimized and varied. Schnorr teaches the enzymes of the enzyme composition are recombinantly prepared and specifically teaches the β-glucosidase is recombinantly prepared in the filamentous fungus Aspergillus oryzae (see Example 6). Schnorr further teaches filtered fractions of the fermentation broths used in the preparation of the enzymes of the composition are used in the enzyme composition (see p.75, last paragraph). The instant specification defines a whole fermentation broth as a preparation produced by cellular fermentation that undergoes no or minimal recovery and/or purification and be fractionated, and thus Schnorr reads on a recombinant whole fermentation broth produced by a recombinant filamentous fungus overexpressing a beta-glucosidase as claimed (see Instant Specification – p.21, 1st-2nd paragraphs).
Regarding claim 2, the enzyme composition of Schnorr comprises Trichoderma reesei GH5 endoglucanase II, reading on wherein the endoglucanase comprises a GH5 endoglucanase (see Example 6, p.76, lines 6-14).
Regarding claim 3, Schnorr teaches using the enzyme composition at 50°C, 55°C, 60°C, and 65°C for the hydrolysis of milled unwashed pretreated corn stover (see Example 7, p.76, lines 18-34). This reads on wherein the endoglucanase is a thermostable endoglucanase as defined in the instant specification since the endoglucanase has catalytic activity within the temperature optimum range disclosed (see p.4, lines 18-20).
Regarding claim 4, Schnorr teaches the Trichoderma reesei GH5 endoglucanase II comprising SEQ ID NO: 17, corresponding to the polynucleotide sequence of the gene encoding T. reesei GH5 endoglucanase II, and SEQ ID NO: 18, corresponding to the polypeptide sequence of the T. reesei GH5 endoglucanase II, in the enzyme composition (see Example 6, p.75, lines 12-14). Limitation c) is interpreted to be drawn to polypeptides comprising any fragment of the endoglucanases of limitations a) or b) and further comprising endoglucanase activity. The instant specification discloses that endoglucanases are enzymes belonging to EC 3.2.1.4 and are capable of catalyzing the endohydrolysis of 1,4-β-D-glucosidic linkages in cellulose, lichenin, or cereal β-D-glucans (see p.3, lines 31-34). UniProt provides evidence that the T. reesei GH5 endoglucanase II belongs to EC 3.2.1.4 and catalyzes the endohydrolysis of 1,4-β-D-glucosidic linkages in cellulose, lichenin, or cereal β-D-glucans (see p.1, Catalytic Activity and p.4, Sequence Similarities). SEQ ID NO: 18 of Schnorr comprises multiple fragments of the polypeptide sequence of SEQ ID NO: 2 (see Appendix A for sequence alignment). Therefore, the Trichoderma reesei GH5 endoglucanase II of Schnorr reads on limitation c) of claim 4.
Regarding claim 5, Schnorr teaches the Aspergillus fumigatus Cel7A cellobiohydrolase I in the enzyme composition which is a GH7 cellobiohydrolase (see Example 6, p.74, lines 27-28 and p.76, lines 9-10). Thus, the A. fumigatus Cel7A cellobiohydrolase I of Schnorr reads on claim 5.
Regarding claim 6, Schnorr teaches the Aspergillus fumigatus Cel7A cellobiohydrolase I comprising SEQ ID NO: 13, corresponding to the polynucleotide sequence of the gene encoding the A. fumigatus Cel7A cellobiohydrolase I, and SEQ ID NO: 14, corresponding to the polypeptide sequence of the A. fumigatus Cel7A cellobiohydrolase I, in the enzyme composition (see Example 6, lines 9-10). SEQ ID NO: 14 of Schnorr has 77.2% identity to SEQ ID NO: 4 of the claimed invention, reading on limitation a) of claim 6 (see Appendix B for sequence alignment). SEQ ID NO: 14 of Schnorr is the polypeptide encoded by the polynucleotide of SEQ ID NO: 13 of Schnorr, and thus also reads on limitation b) of claim 6.
Regarding claim 7, Schnorr teaches the enzyme composition comprises 37% Aspergillus fumigatus Cel7A cellobiohydrolase I, which is within the recited range in claim 7 (see Example 6, p.76, lines 9-10).
Regarding claim 8, the RCBH1 of the enzyme composition of Schnorr is 0.88 (0.88 = 37/(37+5), which is within the recited range in claim 8 (see Example 6, p.76, lines 9-14).
Regarding claim 9, Schnorr teaches the enzyme composition comprises 5% Aspergillus fumigatus β-glucosidase, which is within the recited range in claim 9 (see Example 6, p.76, line 12).
Regarding claims 10 and 11, Schnorr teaches the enzyme composition comprises Aspergillus fumigatus Cel6A cellobiohydrolase II and Aspergillus fumigatus beta-xylosidase, reading on claims 10 and 11 (see Example 6, p.76, lines 9-14).
Regarding claim 12, Schnorr teaches the Aspergillus fumigatus beta-xylosidase is a GH3 beta-xylosidase, reading on claim 12 (see Example 6, p.76, lines 1-5).
Regarding claim 13, Schnorr teaches the enzyme composition is a monocomponent composition prepared by filtering the enzymes from a fermentation broth (see Example 6, p.74, lines 29-30, p.75, lines 4-5, 14-15, 19-20, 25-26, and p.76, lines 3-14). Schnorr further teaches the enzyme composition may be a fermentation broth (see p.35, lines 1-2, p.41, lines 11-12, lines 19-20, p.42, lines 8-20, p.51, lines 26-29). Therefore, it would have been obvious to one of ordinary skill in the art, before the effective filing date of the claimed invention, to have prepared a fermentation broth of the enzyme composition of Schnorr as disclosed in the rejection of claim 1, to arrive at the claimed invention, as Schnorr explicitly suggests such a composition.
Therefore, claims 1-13 and 16-19 are prima facie obvious over Schnorr.
Response to Arguments
Applicant's arguments filed 1/20/2026 have been fully considered but they are not persuasive.
In Applicant’s Remarks, see p.8, 1st paragraph-p.9, 1st passage, Applicant argues that Schnorr provides no motivation to specifically reduce the amount of endoglucanase relative to cellobiohydrolase I to the narrow window of REG 0.20 to 0.03. Applicant further argues that Schnorr does not teach that the ratio of EG to CBHI (REG) is a “result-effective variable” that should be minimized to such a low range as claimed. Applicant further argues that a skilled artisan looking at Schnorr would be motivated to maintain or increase endoglucanase levels, not reduce them to the claimed ratio. Applicant argues Schnorr demonstrates this conclusion directly in the 3rd paragraph of p.1 because without sufficient endoglucanase, cellobiohydrolases run out of substrate. This is not found persuasive.
Schnorr discloses the optimum amount of enzymes and a polypeptide having cellulolytic enhancing activity, of which endoglucanase II is a species, depend on several factors and suggests wide ranges of amounts of enzymes and polypeptide (see paragraph bridging p.51-52, p.52, 1st-3rd paragraphs). Thus, one of ordinary skill in the art would have had motivation to optimize the amount of endoglucanase II as disclosed in the example of Schnorr and arrive at a concentration rendering an REG within the ranges disclosed in claims 1 and 16-19 because Schnorr suggests the amount of enzyme can be optimized and varied. Furthermore, Schnorr does not teach against or discourage reducing the amount of endoglucanase. In fact, Schnorr states the optimum amounts of the enzymes and polypeptide having cellulolytic enhancing activity depend on several factors. Thus, Applicant’s argument that Schnorr concludes that endoglucanase levels should be maintained or increased is not an accurate reflection of the disclosure of Schnorr as a whole. While Schnorr does not specifically teach the ratio of EG to CBHI is a result-effective variable, Schnorr does suggest the amount of enzymes are optimizable and depend on several factors, suggesting that enzyme amounts can either be reduced or increased and are not required to be maintained as exemplified.
In Applicant’s Remarks, see p.9, 1st paragraph-paragraph bridging pp.9-10, Applicant argues that a range is not obvious if the variable was not known to be “result-effective” in the prior art. Applicant argues that Schnorr does not identify the REG- ratio or endoglucanase in an amount less than 10% (w/w) as the keys to maximizing glucose yield in a whole fermentation broth overexpressing beta-glucosidase and containing LPMO. Applicant further argues that Schnorr does not identify the interplay between REG and endoglucanase in an amount of less than 10% (w/w) and does not provide a teaching or suggestion that lowering endoglucanase amounts within the claimed parameters would simultaneously reduce viscosity and increase sugar yield. Applicant reiterates that a skilled artisan would seek to increase endoglucanase to hasten and more effectively reduce viscosity. Applicant further argues their disclosure unexpectedly demonstrates viscosity is reduced when REG is reduced, and nothing in Schnorr teaches or suggests this finding. This is not found persuasive.
The claimed invention is directed to a composition and not a method that requires specific results. As discussed in the response above, Schnorr suggests that the enzyme amounts are optimizable depending on several factors. Although, Schnorr does not specifically identify REG, Schnorr does teach endoglucanase in an amount less than 10% (w/w) as set forth in the rejection above. Since the claim does not require maximizing glucose yield or reducing viscosity, it is not relevant that Schnorr teaches or suggests this to obviate the claimed invention. Accordingly, the claimed ratio of endoglucanase to cellobiohydrolase I was obvious in view of the whole disclosure of Schnorr as discussed in the response above. With respect to Applicant’s argument that a skilled artisan would only maintain or increase endoglucanase, this argument has been responded to in the reply above.
In Applicant’s Remarks, see p.10, 1st-last paragraphs, Applicant argues that the office used impermissible hindsight to arrive at the claimed invention since Schnorr only discloses a wide range of enzyme concentrations and optimization therein based on several factors, with no functional direction toward a specific range. Applicant argues the office states that Schnorr already teaches that it has identified the optimum amount of the enzymatic composition, and thus a skilled artisan would be motivated to stick to that amount. Applicant further argues the office contradicts its position by stating that it would have been obvious to one of ordinary skill in the art to optimize the amount of endoglucanase, and therefore uses the Applicant’s own disclosure to arrive at the claimed invention. This is not found persuasive.
The office’s statement has been that Schnorr suggests the optimum amount of enzymes and a polypeptide having cellulolytic enhancing activity, of which endoglucanase II is a species, depend on several factors and suggests wide ranges of amounts of enzymes and polypeptide (see paragraph bridging p.51-52, p.52, 1st-3rd paragraphs). Thus, one of ordinary skill in the art would have had motivation to optimize the amount of endoglucanase II as disclosed in the example of Schnorr and arrive at a concentration rendering an REG within the ranges disclosed in claims 1 and 16-19 because Schnorr suggests the amount of enzyme can be optimized and varied. This is to say that Schnorr is open to optimization of the enzyme amounts and is not bound to an optimized amount as Applicant suggests. Given that Schnorr teaches a wide range of enzyme amounts, it was obvious that the enzyme amounts can be varied and do not have to remain at the amounts exemplified. Therefore, Applicant’s disclosure is not relied upon to arrive at the claimed invention, since the motivations to alter the enzyme amounts are derived directly from the disclosure of Schnorr as a whole.
In Applicant’s Remarks, see p.11, 1st-2nd paragraphs, Applicant argues that the cited UniProt reference fails to remedy the deficiencies of Schnorr. This is not found persuasive because the alleged deficiencies of Schnorr have been addressed in the replies above.
Therefore, claims 1-13 and 16-19 remain rejected over Schnorr as evidenced by UniProt.
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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/J.P.S./Examiner, Art Unit 1651
/MELENIE L GORDON/Supervisory Patent Examiner, Art Unit 1651
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