DETAILED ACTION
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 05/20/2026 has been entered.
Status of claim rejections
The rejections of record under 35 USC 103 have been maintained in view of Applicant’s arguments in the response filed 05/20/2026.
Examiner’s Note
Please note that the examiner of record has changed. Please address all correspondences following this Office action to Georgiana Reglas, Examiner AU1651.
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.
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).
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.
Accordingly, the claimed invention was prima facie obvious to one of ordinary skill at the time of filing, especially in the absence of evidence to the contrary.
Response to Arguments
Applicant's arguments filed 05/20/2026 have been fully considered but they are not persuasive.
On pg. 8-13 of the remarks, Applicant argues REG is not a recognized result-effective variable, pointing to In re Antonie for support. Applicant argues that REG is not disclosed as a parameter at all and, inter alia, the ratio of endoglucanase to cellobiohydrolase I affects hydrolysis performance and that Scnorr’s discussion of optimizing the enzymes and a polypeptide having cellulolytic enhancing activity refers to optimizing the ratio of cellulases to LPMOs not the ratio of one cellulase to another. Applicant then argues the rejection amounts to impermissible hindsight reconstruction. Applicant further argues the Office’s reliance on Schnorr’s disclosure that “[t]he optimum amounts of the enzymes and a polypeptide having cellulolytic enhancing activity depend on several factors including, but not limited to, the mixture of cellulolytic enzymes and/or hemicellulolytic enzymes, the cellulosic material, the concentration of cellulosic material, the pretreatment(s) of the cellulosic material, temperature, time, pH, and inclusion of a fermenting organism (e.g., for Simultaneous Saccharification and Fermentation)” and that wide range of enzyme amounts to the cellulosic material is generic and does not establish sufficient motivation to reduce the amount of endoglucanase to arrive at a ratio within the claimed invention. Applicant further argues the Office conflates the total enzyme loading amounts in Schnorr and the internal composition ratios of endoglucanase and cellobiohydrolase I. Applicant further argues the Office has not explained why a skilled artisan, starting from Schnorr’s composition with an REG of 0.21, would have had any reason to believe that reducing endoglucanase relative to cellobiohydrolase I would yield an improved composition, especially in view of the understanding that endoglucanase creates the substrate for cellobiohydrolase. Applicant further argues the fact that Schnorr’s examples do not fix the enzyme amounts does not provide or establish motivation to arrive at the claimed REG range by reducing the amount of endoglucanase relative to cellobiohydrolase. Applicant further argues the rational of the Office for optimizing the enzyme amounts to arrive at an REG of the claimed invention echoes the Board’s reliance on Pallas’ teachings in Stepan, 868 F.3d at 1346. Applicant further argues the several factors listed in Schnorr are process conditions and substrate characteristics, not internal enzyme ratios, and the claimed REG range is not merely a trivial adjustment from Schnorr’s 0.21.
In response, the examiner disagrees. First, regarding Applicant’s argument about REG not being recognized as “a result-effective variable”, the examiner notes that MPEP 2144.05(II)(B) states the Supreme Court has clarified that an "obvious to try" line of reasoning may properly support an obviousness rejection. In In re Antonie, 559 F.2d 618, 195 USPQ 6 (CCPA 1977), the CCPA held that a particular parameter must first be recognized as a result-effective variable, i.e., a variable which achieves a recognized result, before the determination of the optimum or workable ranges of said variable might be characterized as routine experimentation, because "obvious to try" is not a valid rationale for an obviousness finding. However, in KSR International Co. v. Teleflex Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007), the Supreme Court held that "obvious to try" was a valid rationale for an obviousness finding, for example, when there is a "design need" or "market demand" and there are a "finite number" of solutions. 550 U.S. at 421, 82 USPQ2d at 1397 ("The same constricted analysis led the Court of Appeals to conclude, in error, that a patent claim cannot be proved obvious merely by showing that the combination of elements was ‘[o]bvious to try.’ ... When there is a design need or market pressure to solve a problem and there are a finite number of identified, predictable solutions, a person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense. In that instance the fact that a combination was obvious to try might show that it was obvious under §103."). Thus, after KSR, the presence of a known result-effective variable would be one, but not the only, motivation for a person of ordinary skill in the art to experiment to reach another workable product or process.
Second, 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.
Moreover, Applicant has not demonstrated that REG ratio is a result-effective variable across the breadth of the claimed range. The specification only demonstrates experiments with REG of 1.00 (Experiment 1 – Table 1), 0.50 (Exp. 2 – Table 1), 0.30 (Exp. 3 – Table 1 and Exp. 1 – Table 5), 0.20 (Exp. 4 – Table 1), 0.23 (Exp. 2 – Table 5), 0.18 (Exp. 1-5 – Table 3), 0.17 (Exp. 3 – Table 5), and 0.10 (Exp. 5 – Table 1). Table 2 discloses the viscosity levels of the five experiments in Table 1. Experiment 3, which had an REG of 0.30 and an endoglucanase amount less than 10% (w/w), resulted in a viscosity of 1094 cP which is not significantly different from the 1063 cP viscosity obtained in Exp. 4 at REG of 0.20. Therefore, the claimed range of REG contains within it REG values that do not confer unexpected results of viscosity. Table 3 demonstrates the effects on glucose yield of varying the w/w% of endoglucanase in the composition while retaining REG of 0.18. Again, the amounts of glucose yield slightly increased in Experiments 2-5 when endoglucanase was below 10% w/w but is not representative of the entire range of REG as claimed, only REG of 0.18. Likewise, the experiments of Tables 5-6 demonstrate a slight increase in glucose concentration when decreasing the weight concentration of endoglucanase below 10% (w/w) and the REG from 0.30 to 0.23 and 0.17. It is noted that the glucose concentration demonstrated in Experiment 3 of Tables 5 and 6, i.e., 42.5 g/L, is lower than the glucose concentrations obtained in Table 4, even when REG was 0.18 and endoglucanase had a weight concentration above 10%. Thus, the results do not appear to be unexpected and furthermore the results have not be demonstrated across the full breadth of the claimed REG for the supposed unexpected reduction in viscosity and increase in glucose yield.
Finally, in response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). As discussed above, 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.
On pg. 13-15 of the remarks, Applicant argues , Applicant argues the prior art teaches away from reducing endoglucanase. Applicant argues that Schnorr discloses “[e]ndoglucanases digest the cellulose polymer at random locations, opening it to attack by cellobiohydrolases,” and “[c]ellobiohydrolases sequentially release molecules of cellobiose from the ends of the cellulose polymer,” providing reason to maintain high amounts of endoglucanase, since lowering the amounts would be expected to starve cellobiohydrolase of substrate and reduce hydrolysis efficiencies. Applicant argues a skilled artisan would have no reason to drastically reduce endoglucanase without some teaching or suggestion that it would be beneficial. Applicant further argues the Office conflates the absence of an explicit prohibition with the presence of a motivation. Applicant further cites Zhou et al. and Billard et al. (given its fullest consideration) to argue that the art recognized the need for high amounts of endoglucanase. Applicant further argues no reference in the record teaches or suggests that reducing total endoglucanase below 10% would be beneficial.
In response, the examiner disagrees. It should be noted that the full range of the REG ratio claimed does not require a drastic reduction in endoglucanase amount as Applicant argues. Only a slight decrease in endoglucanase is required for the composition of Schnorr having an REG of 0.21 to be adjusted to an REG of 0.20. Moreover, the claimed composition is not required to be applied in any process, let alone the hydrolysis of cellulosic materials, since the preamble does not recite an intended use of the composition. Thus, the prior art of Zhou and Billard are not found to be persuasive to overcome the rejection of record.
On pg. 15-18 of the remarks, Applicant argues the claimed range produces unexpected results. Applicant cites In re Papesch to argue that a compound and its properties are inseparable. Applicant further cites Allergan, Inc. v. Sandoz Inc. to argue the unexpected properties of the claimed formulation, even if inherent in that formulation, differ in kind from the prior art, thereby supporting a conclusion of nonobviousness. Applicant further argues the unexpected results is that reducing the amount of endoglucanase improves both viscosity reduction and glucose yield, contrary to the understanding of the art that endoglucanase should be increased to yield better hydrolysis results. Applicant points to Table 2 of the instant specification to show that viscosity drops from 1650 cP in Experiment 1 to 924 cP in Experiment 5 from a starting material viscosity of 8700 cP. Applicant argues this is unexpected in light of the prior art which disclose that endoglucanase is responsible for internal cellulose chain cleavage that drives viscosity reduction, and the skilled artisan would have expected that reducing endoglucanase would have increased viscosity, not reduced it. Applicant then points to Table 4 of the instant specification to show that when endoglucanase is reduced to 6.18% from 10.20% while REG is held constant at 0.18, glucose concentration increases from 45.2 g/L in Experiment 1 to 51.3 g/L in Experiment 5. Applicant further explains that a composition with REG of 0.23 and endoglucanase at 20.6% (w/w) yielded approximately 25% lower glucose concentration than the composition used in Experiment 1. Applicant also explains that a composition with REG of 0.53 and endoglucanase at 40.5% (w/w) yielded 17% lower glucose concentration. Applicant argues the results demonstrate the compositions within the claimed REG range with endoglucanase less than 10% (w/w) produce both lower viscosity and higher glucose yields than compositions outside these parameters, which would have been unexpected in light of the prior art. Applicant argues the specification reveals that the REG and total endoglucanase being less than 10% (w/w) is the key to improved viscosity and glucose yield, contrary to the prior art’s belief that endoglucanase should be increased to maximize hydrolysis and generate chain ends for cellobiohydrolases.
In response, the examiner disagrees. As discussed above, Applicant has not demonstrated that REG ratio is a result-effective variable across the breadth of the claimed range. The specification only demonstrates experiments with REG of 1.00 (Experiment 1 – Table 1), 0.50 (Exp. 2 – Table 1), 0.30 (Exp. 3 – Table 1 and Exp. 1 – Table 5), 0.20 (Exp. 4 – Table 1), 0.23 (Exp. 2 – Table 5), 0.18 (Exp. 1-5 – Table 3), 0.17 (Exp. 3 – Table 5), and 0.10 (Exp. 5 – Table 1). Table 2 discloses the viscosity levels of the five experiments in Table 1. Experiment 3, which had an REG of 0.30 and an endoglucanase amount less than 10% (w/w), resulted in a viscosity of 1094 cP which is not significantly different from the 1063 cP viscosity obtained in Exp. 4 at REG of 0.20. Therefore, the claimed range of REG contains within it REG values that do not confer unexpected results of viscosity. Table 3 demonstrates the effects on glucose yield of varying the w/w% of endoglucanase in the composition while retaining REG of 0.18. Again, the amounts of glucose yield slightly increased in Experiments 2-5 when endoglucanase was below 10% w/w but is not representative of the entire range of REG as claimed, only REG of 0.18. Likewise, the experiments of Tables 5-6 demonstrate a slight increase in glucose concentration when decreasing the weight concentration of endoglucanase below 10% (w/w) and the REG from 0.30 to 0.23 and 0.17. It is noted that the glucose concentration demonstrated in Experiment 3 of Tables 5 and 6, i.e., 42.5 g/L, is lower than the glucose concentrations obtained in Table 4, even when REG was 0.18 and endoglucanase had a weight concentration above 10%. Thus, the results do not appear to be unexpected and furthermore the results have not be demonstrated across the full breadth of the claimed REG for the supposed unexpected reduction in viscosity and increase in glucose yield.
On pg. 18-21 of the remarks, Applicant argues Schnorr does not teach the claimed “recombinant whole fermentation broth”. Applicant argues that Schnorr’s Example 6 uses individually purified monocomponent enzymes, each produced in separate host organisms and then combined. Applicant argues that the endoglucanase recombinantly produced in Aspergillus oryzae is extensively purified and does not read on a whole fermentation broth of the claimed invention that undergoes no or minimal recovery and/or purification. Applicant argues the whole fermentation broth produced by a recombinant filamentous fungus overexpressing beta-glucosidase would contain overexpressed beta-glucosidase, spent cell culture medium, cell debris, other secreted proteins, and metabolites, which are not present in Schnorr’s monocomponent preparation of Example 6. Applicant further argues that Uniprot fails to remedy the deficiencies of Schnorr.
In response, the examiner disagrees. 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 can 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). There is no limit placed on what is to be considered “minimal recovery and/or purification”. In fact, the following descriptions of whole fermentation broth components in paragraphs 1-7 of page 21 are merely exemplary place no further limits on what is to be considered a whole fermentation broth. Furthermore, the alleged deficiencies of Schnorr have been addressed above and will not be repeated here. Schnorr renders obvious the claimed invention (for the reasons set forth above), and 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. Thus, the rejections of record are maintained as set forth above.
Conclusion
NO CLAIMS ALLOWED.
All claims are identical to or patentably indistinct from, or have unity of invention with claims in the application prior to the entry of the submission under 37 CFR 1.114 (that is, restriction (including a lack of unity of invention) would not be proper) and all claims could have been finally rejected on the grounds and art of record in the next Office action if they had been entered in the application prior to entry under 37 CFR 1.114. Accordingly, THIS ACTION IS MADE FINAL even though it is a first action after the filing of a request for continued examination and the submission under 37 CFR 1.114. See MPEP § 706.07(b). 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to GEORGIANA C REGLAS whose telephone number is (571)270-0995. The examiner can normally be reached M-Th: 8:00am-2:00pm.
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/G.C.R./Examiner, Art Unit 1651
/THOMAS J. VISONE/Supervisory Patent Examiner, Art Unit 1672
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