DETAILED ACTION
All objections and rejections raised in prior Office Actions are withdrawn unless restated below.
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 .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 12/08/2025 has been entered.
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 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.
Claim(s) 21, 25, and 27-41 (all pending claims) is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Teter et al. (U.S. 2005/0048619 A1) (see IDS).
Teter et al., abstract, disclose the following:
The present invention relates to variants of a parent glycoside hydrolase, comprising a substitution at one or more positions corresponding to positions 21, 94, 157, 205, 206, 247, 337, 350, 373, 383, 438, 455, 467, and 486 of amino acids 1 to 513 of SEQ ID NO: 2, and optionally further comprising a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2 a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2, wherein the variants have glycoside hydrolase activity. The present invention also relates to nucleotide sequences encoding the variant glycoside hydrolases and to nucleic acid constructs, vectors, and host cells comprising the nucleotide sequences.
“The isolated polypeptides have one or more improved properties compared to the polypeptide of SEQ ID NO: 2, wherein the improved properties are selected from the group consisting of thermal activity, thermostability, pH activity, pH stability, substrate specificity, product specificity, and chemical stability, as described herein.” Teter et al., page [0519].
SEQ ID NO: 2 (positive position numbers) of Teter et al. is identical to recited SEQ ID NO: 2 described as “Trichoderma reesei Cel7A cellobiohydrolase I.” Teter et al., para. [0626].
Fig. 1A/B of the specification evidences that the numbering of recited SEQ ID NO: 1 and SEQ ID NO: 2 (also SEQ ID NO: 2 of Teter) match for about the first 280 positions. Position 373 of SEQ ID NO: 2 of Teter corresponds to position 380 of recited SEQ ID NO: 1 (see boxed residues below):
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“In the present invention, the isolated variants of a parent glycoside hydrolase comprise a substitution at one or more positions corresponding to positions 21, 94, 157, 205, 206, 247, 337, 350, 373, 383, 438, 455, 467, and 486 of amino acids 1 to 513 of SEQ ID NO: 2, and optionally further comprise a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2, wherein the variants, having glycoside hydrolase activity, comprise amino acid sequences which have a degree of identity of at least 70%, preferably at least 75%, more preferably at least 80%, more preferably at least 85%, even more preferably at least 90%, most preferably at least 95%, and even most preferably at least 97% to the amino acid sequence of the parent glycoside hydrolase.” Teter et al., para. [0139].
“Preferably, the parent glycoside hydrolase comprises the amino acid sequence of SEQ ID NO: 2; or an alleleic variant thereof, or a fragment thereof.” Teter et al., para. [0074].
“Table 1 shows the degree of improvement for novel Cel7A cellobiohydrolase I variants as measured by assessing the thermal activity ratio of activity at 64° C. relative to activity at 50° C.” Teter et al., para. [0650]. Table 1 discloses the following species:
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70
680
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39
719
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48
796
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The variant 776-M42 above is a cellobiohydrolase variant identical to SEQ ID NO: 2 of Teter with substitutions S8P and G205R is about 99% (but less than 100%) identical to recited SEQ ID NO: 2 and has the substitution D380N (residue N373 of SEQ ID NO: 2 of Teter), T8P and N205R relative to SEQ ID NO: 1. "[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." MPEP 2113(I). Embodiments of claims 21 and 25 and claims depending therefrom do not require embodiment cellobiohydrolase variants to be made by any particular process or to require manipulation of any particular parent cellobiohydrolase or sequence. For example, an embodiment cellobiohydrolase variant can be made by solid-state peptide synthesis. As such, the claim terminology S8P, N205R and D380N is understood to only require in an embodiment cellobiohydrolase variant that is about 99% (but less than 100%) identical to SEQ ID NO: 2 with the amino acid residues P, R and N being present in positions corresponding to positions 8, 205 and 380 of SEQ ID NO: 1, respectively. Position D380 of SEQ ID NO: 1 corresponds to position N373 of SEQ ID NO: 2 (see alignment in Fig. 1A/B of specification).
Such an embodiment cellobiohydrolase identical to SEQ ID NO: 2 but having residues P and R at positions 8 and 205 (variant 76-M43), respectively, further has a catalytic domain that is over 70% but less than 100% identical to the catalytic domain of SEQ ID NO: 2 as recited in claim 25, and further has a carbohydrate binding module being amino acid residues 461-497 of SEQ ID NO: 2 as set forth in specification, page 5.
Further, it is noted that the variant 776-M42 of Teter can be made starting with the a cellobiohydrolase identical to SEQ ID NO: 1 and substituting under the variant 776-M42 of Teter is produced, although the same is not required by claims 21 and 25 and claims depending therefrom.
As such, Teter et al. describe a cellobiohydrolase variant having at least 99% (but less than 100%) sequence identity to recited SEQ ID NO: 2 with substitutions being 8P, 205R and 380N (according to numbering of SEQ ID NO: 1) having increased thermostability (described 4.6-fold improvement) relative to the parent cellobiohydrolase of SEQ ID NO: 2.
Claims 21, 25, 27-31 and 40-41 are anticipated for this reason.
Regarding claims 32-34, Teter et al., para. [0348], disclose the following:
“The present invention also relates to nucleic acid constructs comprising a nucleotide sequence encoding a glycoside hydrolase variant of the present invention operably linked to one or more control sequences which direct the expression of the coding sequence in a suitable host cell under conditions compatible with the control sequences.” Teter et al., para. [0305].
As such, Teter et al. disclose a cell culture composition (i.e. cultivation medium with host cells) comprising the cellobiohydrolase variant as described from which the cellobiohydrolase variant is recoverable which satisfies the features of claim 32. Further, Teter et al. disclose a both an isolated polynucleotide encoding the cellobiohydrolase variant and operably linked to one or more control sequences that direct the production of the polypeptide in an expression host, and a recombinant expression host comprising such polynucleotide and a method for producing a cellobiohydrolase variant as recited in claim 33. The cultivation and recovery method described in Teter, para. [0348], satisfies the features of claims 34 and 35 including a recombinant host cell.
Regarding claim 36, Teter et al., claim 283, disclose:
A method for obtaining a variant of a parent glycoside hydrolase, comprising:
(a) introducing into the parent glycoside hydrolase a substitution at one or more positions corresponding to positions 21, 94, 157, 205, 206, 247, 337, 350, 373, 383, 438, 455, 467, and 486 of amino acids 1 to 513 of SEQ ID NO: 2, and optionally further introducing a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2, wherein the variant has glycoside hydrolase activity; and
(b) recovering the variant.
Position 373 of SEQ ID NO: 2 corresponds to position 380 of recited SEQ ID NO: 1.
Regarding claim 37, claim 437 of Teter provides: “437. A method for degrading cellulose- and hemicellulose-containing biomass, comprising treating the biomass with an effective amount of a variant of claim 1 and recovering the degraded biomass,” which is considered to be disclosure of performing the same method with any cellobiohydrolase disclosed by Teter consistent with claim 1 of Teter.
Regarding claims 38 and 39, “The glycoside hydrolase variants, polypeptides having glycoside hydrolase activity, and host cells of the present invention may be used in the production of monosaccharides, disaccharides, and polysaccharides as chemical or fermentation feedstocks from biomass for the production of ethanol, plastics, or other products or intermediates.” Teter, para. [0532]. “The glycoside hydrolase variants and polypeptides having glycoside hydrolase activity of the present invention may be used in conjunction with the above-noted enzymes to further degrade the cellulose component of the biomass substrate.” Teter, para. [0540]. “Ethanol can be produced by enzymatic degradation of biomass and conversion of the released saccharides to ethanol.” Teter, para. [0541]. “Once the cellulose is converted to glucose, the glucose is easily fermented by yeast into ethanol.” Teter, para. [0007].
The above disclosure is considered to be an anticipatory disclosure of saccharifying (i.e. released saccharides) a cellulosic material with any cellobiohydrolase as disclosed by Teter, fermenting the saccharified cellulosic material with a fermenting microorganism being yeast and producing ethanol as a fermentation product as to meet the features of claims 38 and 39. Regarding recitation of “recovering the fermentation product from the fermentation” in claim 38, Titer, para. [0541] states: “Ethanol can be produced by enzymatic degradation of biomass and conversion of the released saccharides to ethanol. This kind of ethanol is often referred to as bioethanol or biofuel. It can be used as a fuel additive or extender in blends of from less than 1% and up to 100% (a fuel substitute),” wherein an fuel that is 100% ethanol so produced is necessarily recovered from any fermentation with yeast.
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 21, 25, 27-30, 32-33 and 40-41 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon being a naturally-occurring product without significantly more. The claim(s) recite(s) a variant cellobiohydrolase and isolated polynucleotide encoding the cellobiohydrolase variant that include natural products. This judicial exception is not integrated into a practical application because the claims do not recite any features directed to a practical application as further reviewed below. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception for the reasons further reviewed below.
MPEP 2106(III) directs that claims drawn to 1) a composition of matter (step 1), 2) a law of nature or a natural phenomenon or a product of nature (step 2A) and 3) lacking recitation of additional elements that make the claims directed to significantly more than a judicial exception (step 2B) are ineligible for patenting under 35 U.S.C. 101. See MPEP 2106(III), flow chart. Step 2A has two prongs as set forth in MPEP 2106.04(II)(A).
“If the claim includes a nature-based product that does not exhibit markedly different characteristics from its naturally occurring counterpart in its natural state, then the claim recites a "product of nature" exception, and requires further analysis in Step 2A Prong Two to determine whether the claim as a whole integrates the exception into a practical application.” MPEP 2106.04(c). “It is important to keep in mind that product of nature exceptions include both naturally occurring products and non-naturally occurring products that lack markedly different characteristics from any naturally occurring counterpart.” MPEP 2106.04(b)(II).
“The markedly different characteristics analysis is part of Step 2A Prong One, because the courts use this analysis to identify product of nature exceptions.” MPEP 2106.04(c). “The markedly different characteristics analysis compares the nature-based product limitation to its naturally occurring counterpart in its natural state. Markedly different characteristics can be expressed as the product’s structure, function, and/or other properties, and are evaluated based on what is recited in the claim on a case-by-case basis. If the analysis indicates that a nature-based product limitation does not exhibit markedly different characteristics, then that limitation is a product of nature exception. If the analysis indicates that a nature-based product limitation does have markedly different characteristics, then that limitation is not a product of nature exception.” MPEP 2106.04(c)(II).
Examiners should keep in mind that if the nature-based product limitation is naturally occurring, there is no need to perform the markedly different characteristics analysis because the limitation is by definition directed to a naturally occurring product and thus falls under the product of nature exception.” MPEP 2106.04(c)(I).
Here, the rejected claims are directed towards a composition of matter such that step 1 is yes.
Uniprot, Accession No. S6EXC0, 2024, www.uniprot.org, teaches a natural product cellobiohydrolase (releasing cellobiose from the non-reducing ends of chains, EC 3.2.1.91) from Evansstolkia leycettana with over 70% identity to recited SEQ ID NO: 1 as shown in the following alignment:
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646
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Uniprot S6EXC0 identifies residues 501-537 thereof as CBM that is a carbohydrate binding domain. Residues 26-500 of Uniport S6EXC0 is identified as a” glucanase” or catalytic domain that is not the CBM.
An alignment between 1-443 of recited SEQ ID NO: 1 (catalytic domain) and residues 26-500 of Uniprot S6EXC0 is as follows:
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As shown in the alignment above, the cellobiohydrolase of Uniprot S6EXC0 has substitutions S159P, T430V and T444S relative to SEQ ID NO: 1 and is a cellobiohydrolase variant of SEQ ID NO: 1 having greater than 70% and less than 100% identity to recited SEQ ID NO: 1 and the catalytic domain of SEQ ID NO: 1 that meets the features of claims 21, 25, 27-30 and 40-41.
As discussed above, Uniprot S6EXC0 describes a naturally-ocurring cellobiohydrolase that has all of the features of claims 21, 25, 27-30 and 40-41, wherein claim 32 has an additional feature of a generic composition containing such cellobiohydrolase. Regarding claim 33, the naturally-occurring Evansstolkia leycettana cell has a chromosome (i.e. polynucleotide) operably linked to its native promoter (i.e. a control sequence that can direct production of cellobiohydrolase in an expression host) meeting the features of claim 33.
Since the cellobiohydrolase product recited in the rejected claims is naturally-occurring, for step 2A, prong 1, “there is no need to perform the markedly different characteristics analysis because the limitation is by definition directed to a naturally occurring product and thus falls under the product of nature exception” such that step 2A, prong 1, is satisfied for the rejected claims.
Regarding, step 2A, prong 2, “Prong Two asks does the claim recite additional elements that integrate the judicial exception into a practical application? In Prong Two, examiners evaluate whether the claim as a whole integrates the exception into a practical application of that exception.” MPEP 2106(II)(A)(2). “Examiners evaluate integration into a practical application by: (1) identifying whether there are any additional elements recited in the claim beyond the judicial exception(s); and (2) evaluating those additional elements individually and in combination to determine whether they integrate the exception into a practical application, using one or more of the considerations introduced in subsection I supra, and discussed in more detail in MPEP §§ 2106.04(d)(1), 2106.04(d)(2), 2106.05(a) through (c) and 2106.05(e) through (h).” MPEP 2106.04(d).
Claims 21, 25, 27-30 and 40-41 do not recite any additional elements other than the natural product cellobiohydrolase. Claim 32 recites an additional feature of an enzyme composition having the natural product cellobiohydrolase and claim 33 recites a requirement of an “isolated” polynucleotide encoding the cellobiohydrolase wherein the isolated naturally-ocurring gene sequence and endogenous promoter encoding cellobiohydrolase satisfies the features of claim 33. The recitation of otherwise natural product as being “isolated” or present in a generic composition are not additional elements that integrate the natural product into a practical application. Rather, MPEP 2106.04(b)(I) sets forth that “isolated DNA,” and by extension other “isolated” natural products, are themselves natural phenomena and isolation or similarly isolation by placement in a generic composition are not additional elements that integrate such a natural phenomenon into a practical application. As such, the rejected claims fail to recite additional elements that incorporate the judicial exception into a practical application.
Regarding Step 2B, “Step 2B asks: Does the claim recite additional elements that amount to significantly more than the judicial exception”? MPEP 2106.05(II).
As discussed above, claims 21, 25-30, and 40-41 do not recite any additional elements. The additional elements of a polynucleotide being isolated (claim 33) or the cellobiohydrolase being in a generic composition (claim 32) are not features directed at anything other than the natural phenomenon (i.e. the judicial exception) itself. See MPEP 2106.04(b)(I). As such, Step 2B is answered in the negative and the rejected claims are directed towards a judicial exception.
The claims are directed towards ineligible subject matter for the reasons stated.
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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 21, 25, and 27-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. U.S. 9,701,951 B1 in view of Teter et al. (U.S. 2005/0048619 A1).
U.S. Patent No. U.S. 9,701,951 B1 is previously published as Teter et al. (U.S. 2005/0048619 A1). The rejections above under 35 U.S.C. 102(a)(1) over Teter are incorporated herein by reference.
SEQ ID NO: 2 of the issued patent is the same as recited SEQ ID NO: 2. Patented claims 1-3 directly recite a cellobiohydrolase having SEQ ID NO: 2 and a substitution at position 157 being K157R (same position numbering as in recited SEQ ID NO: 1), and patented claim 10 directly recites the substitution 205R. Such a cellobiohydrolase variant with 157R and 205R has:
-greater than 99% identity to recited SEQ ID NO: 2;
-amino acids 380N, 4C and 205R (numbering according to SEQ ID NO: 1);
-a catalytic domain having over 70% but less than 100% identity to the catalytic domain of SEQ ID NO: 2, and
-a carbohydrate binding module,
Further, Teter as discussed above assert that the substitutions taught therein are expected to increase thermostability relative to the cellobiohydrolase of SEQ ID NO: 2. As such, the patented claims directly anticipate or suggest the features of claim 21, 25, and 27-31.
The reasons why employment of the cellobiohydrolase variant recited in the patented claims (i.e. cellobiohydrolases having a high degree of identity to SEQ ID NO:2) is directly instructed by Teter et al. as to reach the features of the rejected claims are stated above including methods for producing and using such variant cellobiohydrolases as recited in the rejected claims and nucleic acids, vectors, and host cells for production of such cellobiohydrolases, inclusion of such cellobiohydrolases in a laundry detergent/enzyme composition or cell culture composition and processes of degrading a cellulosic material and producing a fermentation product as recited in claims 32-35 and 37-39.
Regarding claims 40 and 41, patented claim 16 directly suggest that a substitution 8P can be combined with any of the other substitutions recited in the patented claims such that an ordinarily skilled artisan at the time of filing would have been motivated to do the same including combined with the substitutions 8P and 205R as directly taught in Table 1 of Teter.
Regarding claim 36, position 373 as recited in patented claims 9 and 10 corresponds to position 380 of recited SEQ ID NO: 1. Teter, claim 283, as discussed above teaches that it is appropriate to produce a cellobiohydrolase variant of recited SEQ ID NO: 2 in a manner meeting all of the features of claim 36.
Claims 21, 25, and 27-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of U.S. Patent No. U.S. 8,383,385 B2 in view of Teter et al. (U.S. 2005/0048619 A1).
U.S. Patent No. U.S. 8,383,385 B1 is previously published as Teter et al. (U.S. 2005/0048619 A1).
The rejections under 35 U.S.C. 102(a)(1) over Teter et al. (U.S. 2005/0048619 A1) stated above are incorporated herein by reference.
SEQ ID NO: 2 of the issued patent is the same as recited SEQ ID NO: 2. Patented claim 1 directly recites a cellobiohydrolase having SEQ ID NO: 2 and a substitution at position 94 being to S, A, R or Q (same position numbering as in recited SEQ ID NO: 1), and patented claim 9 directly recites the substitution 205R. Such a cellobiohydrolase variant with substitution of position 94 and 205R has:
-greater than 99% identity to recited SEQ ID NO: 2;
-amino acids 380N and 205R (numbering according to SEQ ID NO: 1);
-a catalytic domain having over 70% but less than 100% identity to the catalytic domain of SEQ ID NO: 2, and
-a carbohydrate binding module,
Further, Teter as discussed above assert that the substitutions taught therein are expected to increase thermostability relative to the cellobiohydrolase of SEQ ID NO: 2. As such, the patented claims directly anticipate or suggest the features of claim 21, 25, and 27-31.
The reasons why employment of the cellobiohydrolase variant recited in the patented claims (i.e. cellobiohydrolases having a high degree of identity to SEQ ID NO:2) is directly instructed by Teter et al. as to reach the features of the rejected claims are stated above including methods for producing and using such variant cellobiohydrolases as recited in the rejected claims and nucleic acids, vectors, and host cells for production of such cellobiohydrolases, inclusion of such cellobiohydrolases in a laundry detergent/enzyme composition or cell culture composition and processes of degrading a cellulosic material and producing a fermentation product as recited in claims 32-35 and 37-39.
Regarding claims 40 and 41, patented claim 11 directly suggest that a substitution 8P can be combined with any of the other substitutions recited in the patented claims such that an ordinarily skilled artisan at the time of filing would have been motivated to do the same including combined with the substitutions 8P and 205R as directly taught in Table 1 of Teter.
Regarding claim 36, position 373 as recited in patented claim 7 corresponds to position 380 of recited SEQ ID NO: 1. Teter, claim 283, as discussed above teaches that it is appropriate to produce a cellobiohydrolase variant of recited SEQ ID NO: 2 in a manner meeting all of the features of claim 36.
Claims 21, 25, 27-35 and 37-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. U.S. 7,932,073 B2 in view of Teter et al. (U.S. 2005/0048619 A1).
U.S. Patent No. U.S. 7,932,073 B2 is previously published as Teter et al. (U.S. 2005/0048619 A1).
The rejections under 35 U.S.C. 102(a)(1) over Teter et al. (U.S. 2005/0048619 A1) stated above are incorporated herein by reference.
SEQ ID NO: 2 of the issued patent is the same as recited SEQ ID NO: 2. Patented claims 1 and 4 directly recites a cellobiohydrolase having SEQ ID NO: 2 and a substitution at position 94 being to R (same position numbering as in recited SEQ ID NO: 1). Such a cellobiohydrolase variant with substitution 205R has:
-greater than 99% identity to recited SEQ ID NO: 2;
-amino acids 380N and 205R (numbering according to SEQ ID NO: 1);
-a catalytic domain having over 70% but less than 100% identity to the catalytic domain of SEQ ID NO: 2, and
-a carbohydrate binding module,
Further, Teter as discussed above assert that the substitutions taught therein are expected to increase thermostability relative to the cellobiohydrolase of SEQ ID NO: 2. As such, the patented claims directly anticipate or suggest the features of claim 21, 25, and 27-31.
The reasons why employment of the cellobiohydrolase variant recited in the patented claims (i.e. cellobiohydrolases having a high degree of identity to SEQ ID NO:2) is directly instructed by Teter et al. as to reach the features of the rejected claims are stated above including methods for producing and using such variant cellobiohydrolases as recited in the rejected claims and nucleic acids, vectors, and host cells for production of such cellobiohydrolases, inclusion of such cellobiohydrolases in a laundry detergent/enzyme composition or cell culture composition and processes of degrading a cellulosic material and producing a fermentation product as recited in claims 32-35 and 37-39.
Regarding claims 40 and 41, patented claim 7 directly suggest that a substitution 8P can be combined with any of the other substitutions recited in the patented claims such that an ordinarily skilled artisan at the time of filing would have been motivated to do the same including combined with the substitutions 8P and 205R as directly taught in Table 1 of Teter.
Claims 21, 25, and 27-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-45 of U.S. Patent No. U.S. 11,965,189 in view of Teter et al. (U.S. 2005/0048619 A1).
The current application claims divisional priority to U.S. Patent No. 11,965,189. The rejected claims do not maintain consonance with any requirement for restriction issued during the prosecution of U.S. Patent No. 11,965,189.
Patented claim 1 recites a cellobiohydrolase having SEQ ID NO: 1 with a substitution at position 119 wherein the full-length of SEQ ID NO: 1 necessarily and inherently has a catalytic domain and a carbohydrate binding module. Patented claim 2 states that that the substitutions is V119P and N113D, and patented claim 4 indicates a further alteration G4C. Patented claim 43 recites a method anticipating the features of claim 36 and further recite production of a cellobiohydrolase with increased thermostability relative to SEQ ID NO: 1 and further meeting all of the features of claim 21 including specific substitution V119P in patented claim 44. For these reasons the features of claims 21-31 and 36 are anticipated by the patented claims.
Regarding claims 32-35 and 37-39, Teter as discussed above teach that it is appropriate to form an enzyme composition containing a cellobiohydrolase, to produce an isolated polynucleotide encoding a desirably cellobiohydrolase operably linked to a control sequence for expression in an expression host, produce a recombinant host cell containing such an isolated nucleic acid, produce a desirable cellobiohydrolase in a manner including all of the features of claim 35 and to employ a desirable cellobiohydrolase in a manner that meets all of the method features of claims 37-39. As far as the patented claims recited cellobiohydrolase variants that are desirable including increased thermostability as recited in patented claim 1, an ordinarily skilled artisan at the time of filing or invention would have been motivated to employ embodiment cellobiohydrolases meeting the limitations of patented claim 1 and pending claim 21 in a manner to meet the features of claims 32-35 and 37-39 as taught by Teter as discussed above.
Regarding claims 40 and 41, patented claim 2 directly recites a further substitution N113D. For claim 41, it would have been obvious at time of filing to include a combination of any of the substitutions directly recited in patented claim 2 including N113D and V199P since the patented claims directly suggest “one or more” such substitutions be present.
Claims 21, 25, 27-30, 32-35 and 37-39 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-34 of U.S. Patent No. 9,376,670 B2 in view of Spodsberg (U.S. 2014/0342410 A1) and Teter et al. (U.S. 2005/0048619 A1).
U.S. Patent No. 9,376,670 B2 is previously published as Spodsberg (U.S. 2014/0342410 A1) and shares the same specification. The rejection under 35 U.S.C. 102(a)(1) over Teter stated above is incorporated herein by reference.
Patented claim 1 recites a nucleic acid encoding a cellobiohydrolase having SEQ ID NO: 2.
SEQ ID NO: 2, amino acid residues 26-532, of the patented claims are identical to recited SEQ ID NO: 5. The specification page 5 expressly define and state that amino acids 472-507 of recited SEQ ID NO: 5 (as contained within SEQ ID NO: 2 of the patented claims) contain a carbohydrate binding module. Further, “In one embodiment the CBM is amino acids 497 to 532 of SEQ ID NO: 2.” Spodsberg, para. [0062]. A cellulose binding domain (CBM) is considered to be a carbohydrate binding domain.
As shown in Fig. 1 of the specification, S17 of SEQ ID NO: 1 aligns with Q17 of recited SEQ ID NO: 5 (Q43 of SEQ ID NO: 2 of the patented claims). Further, position T440 of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position G466 of SEQ ID NO: 2 of Spodsberg (position G441 of recited SEQ ID NO: 5) such that SEQ ID NO: 2 of Spodsberg has the substitution T440G relative to recited SEQ ID NO: 1. Further, position N113D of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position D150 of SEQ ID NO: 2 of Spodsberg (position D114 of recited SEQ ID NO: 5) As such that the patented claims recite a cellobiohydrolase having recited SEQ ID NO: 5 with a substitutions S17Q, N113D and T440G relative to recited SEQ ID NO: 1 including a catalytic domain otherwise identical to the catalytic domain of recited SEQ ID NO: 5 as to anticipate the features of claims 21, 25, 27-30 and 40-41.
Patented claim 1 recites a nucleic acid construct comprising a polynucleotide encoding a polypeptide having cellobiohydrolase activity, wherein the polynucleotide is operably linked to one or more heteroloqous control sequences that direct production of the polypeptide in an expression host, and wherein the polypeptide is selected from:
(a) a polypeptide having at least 90% sequence identity to the sequence of amino acids 26 to 532 of SEQ ID NO: 2.
Patented claim 8 recites a host cell transformed with the construct of claim 1, and claim 9 recites a cultivating the host cell of patented claim 8 to produce the polypeptide and recovering the polypeptide.
Regarding claim 32, Spodsberg, para. [0234], state that the cellobiohydrolases of Spodsberg can be in an composition, which is necessarily an enzyme composition. Regarding claim 33, Spodsberg, para. [0122]-[0124], state that any of the cellobiohydrolases can be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host. Regarding claims 33 and 34, Spodsberg, para. [0160]-[0162], state that any of the cellobiohydrolases be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host and in a host cell. Regarding claim 35, Spodsberg, para. [0175]-[0180], state that the host cell described can be cultivated under conditions suitable for expression of the cellobiohydrolase and recovering the cellobiohydrolase.
Due to Spodsberg et al. teaching that it is appropriate to employ the cellobiohydrolase of SEQ ID NO: 2 of the patented claims in a manner as recited in claims 32-35, at the time of filing an ordinarily skilled artisan would have been motivated to modify embodiments of the patented claims to further meet the features of claims 32-35.
Further regarding claims 32-35 and 37-39, Teter as discussed above teach that it is appropriate to form an enzyme composition containing a cellobiohydrolase, to produce an isolated polynucleotide encoding a desirably cellobiohydrolase operably linked to a control sequence for expression in an expression host, produce a recombinant host cell containing such an isolated nucleic acid, produce a desirable cellobiohydrolase in a manner including all of the features of claim 35 and to employ a desirable cellobiohydrolase in a manner that meets all of the method features of claims 37-39. As far as the patented claims recited cellobiohydrolase variants that are desirable as recited in patented claim 1, an ordinarily skilled artisan at the time of filing or invention would have been motivated to employ embodiment cellobiohydrolases meeting the limitations of patented claim 1 and pending claim 21 in a manner to meet the features of claims 32-35 and 37-39 as taught by Teter as discussed above.
Regarding recitation in claims 21 and 25 of less than 100% sequence identity to “a parent cellobiohydrolase,” recited SEQ ID NO: 1 and recited SEQ ID NO: 5 (SEQ ID NO: 2 of patented claims) share over 70% identity such that embodiment cellobiohydrolases of the patented claims have at least 70% identity to a parent cellobiohydrolase having recited SEQ ID NO: 1 and fragments thereof and catalytic domains, for example, missing two amino acid residues from the C-terminus of recited SEQ ID NO: 1.
Claims 21, 25, 27-30, 32-35, 37-39 and 40-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-25 of U.S. Patent No. 10,280,413 B2 in view of Spodsberg (U.S. 2014/0342410 A1) and Teter et al. (U.S. 2005/0048619 A1).
U.S. Patent No. 10,280,413 B2 is previously published as Spodsberg (U.S. 2014/0342410 A1) and shares the same specification. The rejection under 35 U.S.C. 102(a)(1) over Teter stated above is incorporated herein by reference.
Patented claim 1 recites a process for degrading a cellulosic material by treating such material with and “enzyme composition” having “(a) a polypeptide comprising an amino acid sequence having at least 90% sequence identity to the sequence of amino acids 26 to 532 of SEQ ID NO: 2.”
SEQ ID NO: 2, amino acid residues 26-532, of the patented claims are identical to recited SEQ ID NO: 5. The specification page 5 expressly define and state that amino acids 472-507 of recited SEQ ID NO: 5 (as contained within SEQ ID NO: 2 of the patented claims) contain a carbohydrate binding module. Further, “In one embodiment the CBM is amino acids 497 to 532 of SEQ ID NO: 2.” Spodsberg, para. [0062]. A cellulose binding domain (CBM) is considered to be a carbohydrate binding domain.
As shown in Fig. 1 of the specification, S17 of SEQ ID NO: 1 aligns with Q17 of recited SEQ ID NO: 5 (Q43 of SEQ ID NO: 2 of the patented claims). Further, position T440 of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position G466 of SEQ ID NO: 2 of Spodsberg (position G441 of recited SEQ ID NO: 5) such that SEQ ID NO: 2 of Spodsberg has the substitution T440G relative to recited SEQ ID NO: 1. Further, position N113D of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position D150 of SEQ ID NO: 2 of Spodsberg (position D114 of recited SEQ ID NO: 5) As such that the patented claims recite a cellobiohydrolase having recited SEQ ID NO: 5 with a substitutions S17Q, N113D and T440G relative to recited SEQ ID NO: 1 including a catalytic domain otherwise identical to the catalytic domain of recited SEQ ID NO: 5 as to anticipate the features of claims 21, 25, 27-30 and 40-41.
Patented claim 1 recites a nucleic acid construct comprising a polynucleotide encoding a polypeptide having cellobiohydrolase activity, wherein the polynucleotide is operably linked to one or more heteroloqous control sequences that direct production of the polypeptide in an expression host, and wherein the polypeptide is selected from:
(a) a polypeptide having at least 90% sequence identity to the sequence of amino acids 26 to 532 of SEQ ID NO: 2.
Spodsberg, claim 40, recites a host cell transformed with the construct of claim 1, and claim 41 of Spodsberg recites a cultivating the host cell of patented claim to produce the polypeptide and recovering the polypeptide.
Regarding claim 32, Spodsberg, para. [0234], state that the cellobiohydrolases of Spodsberg can be in an composition, which is necessarily an enzyme composition. Regarding claim 33, Spodsberg, para. [0122]-[0124], state that any of the cellobiohydrolases can be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host. Regarding claims 33 and 34, Spodsberg, para. [0160]-[0162], state that any of the cellobiohydrolases be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host and in a host cell. Regarding claim 35, Spodsberg, para. [0175]-[0180], state that the host cell described can be cultivated under conditions suitable for expression of the cellobiohydrolase and recovering the cellobiohydrolase.
Due to Spodsberg et al. teaching that it is appropriate to employ the cellobiohydrolase of SEQ ID NO: 2 of the patented claims in a manner as recited in claims 32-35, at the time of filing an ordinarily skilled artisan would have been motivated to modify embodiments of the patented claims to further meet the features of claims 32-35.
Further regarding claims 32-35 and 37-39, Teter as discussed above teach that it is appropriate to form an enzyme composition containing a cellobiohydrolase, to produce an isolated polynucleotide encoding a desirably cellobiohydrolase operably linked to a control sequence for expression in an expression host, produce a recombinant host cell containing such an isolated nucleic acid, produce a desirable cellobiohydrolase in a manner including all of the features of claim 35 and to employ a desirable cellobiohydrolase in a manner that meets all of the method features of claims 37-39. As far as the patented claims recited cellobiohydrolase variants that are desirable as recited in patented claim 1, an ordinarily skilled artisan at the time of filing or invention would have been motivated to employ embodiment cellobiohydrolases meeting the limitations of patented claim 1 and pending claim 21 in a manner to meet the features of claims 32-35 and 37-39 as taught by Teter as discussed above.
Regarding recitation in claims 21 and 25 of less than 100% sequence identity to “a parent cellobiohydrolase,” recited SEQ ID NO: 1 and recited SEQ ID NO: 5 (SEQ ID NO: 2 of patented claims) share over 70% identity such that embodiment cellobiohydrolases of the patented claims have at least 70% identity to a parent cellobiohydrolase having recited SEQ ID NO: 1 and fragments thereof and catalytic domains, for example, missing two amino acid residues from the C-terminus of recited SEQ ID NO: 1.
Claims 21, 25, 27-30, 32-35, 37-39 and 40-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-32 of U.S. Patent No. 11,208,641 B2 in view of Spodsberg (U.S. 2014/0342410 A1) and Teter et al. (U.S. 2005/0048619 A1).
U.S. Patent No. 11,208,641 B2 is previously published as Spodsberg (U.S. 2014/0342410 A1) and shares the same specification. The rejection under 35 U.S.C. 102(a)(1) over Teter stated above is incorporated herein by reference.
Patented claim 1 recites a “recombinant microbial host cell transformed with a nucleic acid construct or expression vector comprising a polynucleotide encoding a polypeptide having cellobiohydrolase activity, wherein the polynucleotide is operably linked to one or more control sequences that direct production of the polypeptide in the recombinant host cell, wherein the polypeptide having cellobiohydrolase activity is heterologous to the recombinant microbial host cell, and wherein the polypeptide having cellobiohydrolase activity is selected from the group consisting of:
an amino acid sequence having at least 90% sequence identity to the sequence of amino acids 26 to 532 of SEQ ID NO: 2.”
The patented claims further recite methods for producing the cellobiohydrolase by “(a) cultivating the host cell of claim 1 under conditions conducive for production of the polypeptide; and (b) recovering the polypeptide.”
SEQ ID NO: 2, amino acid residues 26-532, of the patented claims are identical to recited SEQ ID NO: 5. The specification page 5 expressly define and state that amino acids 472-507 of recited SEQ ID NO: 5 (as contained within SEQ ID NO: 2 of the patented claims) contain a carbohydrate binding module. Further, “In one embodiment the CBM is amino acids 497 to 532 of SEQ ID NO: 2.” Spodsberg, para. [0062]. A cellulose binding domain (CBM) is considered to be a carbohydrate binding domain.
As shown in Fig. 1 of the specification, S17 of SEQ ID NO: 1 aligns with Q17 of recited SEQ ID NO: 5 (Q43 of SEQ ID NO: 2 of the patented claims). Further, position T440 of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position G466 of SEQ ID NO: 2 of Spodsberg (position G441 of recited SEQ ID NO: 5) such that SEQ ID NO: 2 of Spodsberg has the substitution T440G relative to recited SEQ ID NO: 1. Further, position N113D of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position D150 of SEQ ID NO: 2 of Spodsberg (position D114 of recited SEQ ID NO: 5) As such that the patented claims recite a cellobiohydrolase having recited SEQ ID NO: 5 with a substitutions S17Q, N113D and T440G relative to recited SEQ ID NO: 1 including a catalytic domain otherwise identical to the catalytic domain of recited SEQ ID NO: 5 as to anticipate the features of claims 21, 25, 27-30 and 40-41.
Patented claim 1 recites a nucleic acid construct comprising a polynucleotide encoding a polypeptide having cellobiohydrolase activity, wherein the polynucleotide is operably linked to one or more heteroloqous control sequences that direct production of the polypeptide in an expression host, and wherein the polypeptide is selected from:
(a) a polypeptide having at least 90% sequence identity to the sequence of amino acids 26 to 532 of SEQ ID NO: 2.
Spodsberg, claim 40, recites a host cell transformed with the construct of claim 1, and claim 41 of Spodsberg recites a cultivating the host cell of patented claim to produce the polypeptide and recovering the polypeptide.
Regarding claim 32, Spodsberg, para. [0234], state that the cellobiohydrolases of Spodsberg can be in an composition, which is necessarily an enzyme composition. Regarding claim 33, Spodsberg, para. [0122]-[0124], state that any of the cellobiohydrolases can be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host. Regarding claims 33 and 34, Spodsberg, para. [0160]-[0162], state that any of the cellobiohydrolases be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host and in a host cell. Regarding claim 35, Spodsberg, para. [0175]-[0180], state that the host cell described can be cultivated under conditions suitable for expression of the cellobiohydrolase and recovering the cellobiohydrolase.
Due to Spodsberg et al. teaching that it is appropriate to employ the cellobiohydrolase of SEQ ID NO: 2 of the patented claims in a manner as recited in claims 32-35, at the time of filing an ordinarily skilled artisan would have been motivated to modify embodiments of the patented claims to further meet the features of claims 32-35.
Further regarding claims 32-35 and 37-39, Teter as discussed above teach that it is appropriate to form an enzyme composition containing a cellobiohydrolase, to produce an isolated polynucleotide encoding a desirably cellobiohydrolase operably linked to a control sequence for expression in an expression host, produce a recombinant host cell containing such an isolated nucleic acid, produce a desirable cellobiohydrolase in a manner including all of the features of claim 35 and to employ a desirable cellobiohydrolase in a manner that meets all of the method features of claims 37-39. As far as the patented claims recited cellobiohydrolase variants that are desirable as recited in patented claim 1, an ordinarily skilled artisan at the time of filing or invention would have been motivated to employ embodiment cellobiohydrolases meeting the limitations of patented claim 1 and pending claim 21 in a manner to meet the features of claims 32-35 and 37-39 as taught by Teter as discussed above.
Regarding recitation in claims 21 and 25 of less than 100% sequence identity to “a parent cellobiohydrolase,” recited SEQ ID NO: 1 and recited SEQ ID NO: 5 (SEQ ID NO: 2 of patented claims) share over 70% identity such that embodiment cellobiohydrolases of the patented claims have at least 70% identity to a parent cellobiohydrolase having recited SEQ ID NO: 1 and fragments thereof and catalytic domains, for example, missing two amino acid residues from the C-terminus of recited SEQ ID NO: 1.
Claims 21 25, 27-30, 31-35, 37-39 and 40-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-29 of U.S. Patent No. 10,676,769 B2 in view of Spodsberg (U.S. 2014/0342410 A1) and Teter et al. (U.S. 2005/0048619 A1).
Patented claim 1 recites a “variant of a parent cellobiohydrolase, comprising deletions at two or more consecutive positions corresponding to positions of the B2-loop, wherein the corresponding positions of the B2-loop are positions 194, 195, 196, 197, 198, 199, 200, and 201 of SEQ ID NO: 2, wherein the variant has cellobiohydrolase activity, and wherein the variant has at least 95%, but less than 100%, sequence identity to the mature polypeptide of the parent cellobiohydrolase.” The parent cellobiohydrolase can be SEQ ID NO: 16 as recited in patented claim 2, which is identical to recited SEQ ID NO: 5.
Patented claim 5 recites increased specific performance of the cellobiohydrolase. At least Example 12 of the specification indicates that such increased performance includes increased thermostability relative to the cellobiohydrolase of recited SEQ ID NO: 5.
SEQ ID NO: 16 (positive position numbers) of the patented claims are identical to recited SEQ ID NO: 5. The specification page 5 expressly define and state that amino acids 472-507 of recited SEQ ID NO: 5 contain a carbohydrate binding module. Further, “In one embodiment the CBM is amino acids 497 to 532 of SEQ ID NO: 2.” Spodsberg, para. [0062]. A cellulose binding domain (CBM) is considered to be a carbohydrate binding domain.
As shown in Fig. 1 of the specification, S17 of SEQ ID NO: 1 aligns with Q17 of recited SEQ ID NO: 5 (SEQ ID NO: 16 of the patented claims). Further, position T440 of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position G441 of recited SEQ ID NO: 5 (SEQ ID NO: 16 of patented claims), such that SEQ ID NO: 16 of patented claims has the substitution T440G relative to recited SEQ ID NO: 1. Further, position N113D of recited SEQ ID NO: 1 (as shown in Fig. 1 of the specification) aligns with position D114 of recited SEQ ID NO: 5 (SEQ ID NO: 16 of patented claims) As such that the patented claims recite a cellobiohydrolase having recited SEQ ID NO: 5 with a substitutions S17Q, N113D and T440G relative to recited SEQ ID NO: 1 including a catalytic domain otherwise identical to the catalytic domain of recited SEQ ID NO: 5 as to anticipate the features of claims 21, 25, 27-30 and 40-41.
Spodsberg teaches a cellobiohydrolase having SEQ ID NO: 2 that is identical to recited SEQ ID NO: 5 and SEQ ID NO: 16 of the patented claims.
Spodsberg, claim 40, recites a host cell transformed with the construct of claim 1, and claim 41 of Spodsberg recites a cultivating the host cell of patented claim to produce the polypeptide and recovering the polypeptide.
Regarding claim 32, Spodsberg, para. [0234], state that the cellobiohydrolases of Spodsberg can be in an composition, which is necessarily an enzyme composition. Regarding claim 33, Spodsberg, para. [0122]-[0124], state that any of the cellobiohydrolases can be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host. Regarding claims 33 and 34, Spodsberg, para. [0160]-[0162], state that any of the cellobiohydrolases be encoded by an isolated polynucleotide operably linked to a control sequence to direct production in an expression host and in a host cell. Regarding claim 35, Spodsberg, para. [0175]-[0180], state that the host cell described can be cultivated under conditions suitable for expression of the cellobiohydrolase and recovering the cellobiohydrolase.
Due to Spodsberg et al. teaching that it is appropriate to employ the cellobiohydrolase of SEQ ID NO: 2 of the patented claims in a manner as recited in claims 32-35, at the time of filing an ordinarily skilled artisan would have been motivated to modify embodiments of the patented claims to further meet the features of claims 32-35.
Further regarding claims 32-35 and 37-39, Teter as discussed above teach that it is appropriate to form an enzyme composition containing a cellobiohydrolase, to produce an isolated polynucleotide encoding a desirably cellobiohydrolase operably linked to a control sequence for expression in an expression host, produce a recombinant host cell containing such an isolated nucleic acid, produce a desirable cellobiohydrolase in a manner including all of the features of claim 35 and to employ a desirable cellobiohydrolase in a manner that meets all of the method features of claims 37-39. As far as the patented claims recited cellobiohydrolase variants that are desirable as recited in patented claim 1, an ordinarily skilled artisan at the time of filing or invention would have been motivated to employ embodiment cellobiohydrolases meeting the limitations of patented claim 1 and pending claim 21 in a manner to meet the features of claims 32-35 and 37-39 as taught by Teter as discussed above.
Regarding recitation in claims 21 and 25 of less than 100% sequence identity to “a parent cellobiohydrolase,” recited SEQ ID NO: 1 and recited SEQ ID NO: 5 (SEQ ID NO: 2 of patented claims) share over 70% identity such that embodiment cellobiohydrolases of the patented claims have at least 70% identity to a parent cellobiohydrolase having recited SEQ ID NO: 1 and fragments thereof and catalytic domains, for example, missing two amino acid residues from the C-terminus of recited SEQ ID NO: 1.
Claims 21, 25, and 27-41 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-40 of U.S. Patent No. 10,557,127 B2 in view of Teter et al. (U.S. 2005/0048619 A1).
Patented claim 1 recites a cellobiohydrolase variant, comprising a substitution at one or more positions corresponding to positions 4, 44, 45, 72, 265, 266, 391, 393 and 394 of SEQ ID NO: 4, wherein the variant has cellobiohydrolase activity, wherein the variant has increased specific performance relative to a cellobiohydrolase without the substitution at one or more positions corresponding to positions 4, 44, 45, 72, 265, 266, 391, 393 and 394 of SEQ ID NO: 4, and wherein the variant has at least 90% sequence identity, but less than 100% sequence identity, to the mature polypeptide of SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, or SEQ ID NO: 52.
Figures 4-5 of the patent shows that the “increased specific performance” is specifically thermostability relative to a cellobiohydrolase identical to SEQ ID NO: 5.
SEQ ID NO: 14 of the patented claims is identical to recited SEQ ID NO: 5 (SEQ ID NO: 14 has an additional 25 N-terminal amino acid residues). The numbering of SEQ ID NO: 4 of the patented claims is the same as recited SEQ ID NO: 1 for at least the first 400 amino acid positions. Patented claim 3 recites one or more of “a substitution at a position corresponding to position 4 of SEQ ID NO: 4, wherein the substitution is with Cys;” and “a substitution at a position corresponding to position 394 of SEQ ID NO: 4, wherein the substitution is with Pro.” That is, the patented claim states substitutions selected from G4C and S394P be present relative to recited SEQ ID NO: 1. Patented claim 5 directly recites fusion with a heterologous carbohydrate binding domain. Regarding claim 27, the specification, page 5, indicates that recited SEQ ID NO: 5 (SEQ ID NO: 14 of patented claims) has a carbohydrate binding domain.
Patented claim 12 recites a method of obtaining a cellobiohydrolase variant by introducing a substitution at one of “positions 4, 44, 45, 72, 265, 266, 391, 393 and 394 of SEQ ID NO: 4.”
A cellobiohydrolase having SEQ ID NO: 14 of the patented claims with substitutions 4C and 394P anticipates the features of claims 21-28. Regarding claim 32, recovering a variant as recited in patented claim 9 will produce an enzyme composition. Further regarding claim 31, the specification, Example 6 (Table 2), evidences that a substitution 394P is inherently expected to increase thermostability. Regarding claims 29 and 30, patented claim 3 directly suggests making more than one of the recited substitution. As such, an ordinarily skilled artisan would have been motivated to follow this suggestion and modify SEQ ID NO: 14 of the patented claims to have an additional substitution 4C in addition to 394P.
Further regarding claims 32-35 and 37-39, Teter as discussed above teach that it is appropriate to form an enzyme composition containing a cellobiohydrolase, to produce an isolated polynucleotide encoding a desirably cellobiohydrolase operably linked to a control sequence for expression in an expression host, produce a recombinant host cell containing such an isolated nucleic acid, produce a desirable cellobiohydrolase in a manner including all of the features of claim 35 and to employ a desirable cellobiohydrolase in a manner that meets all of the method features of claims 37-39. As far as the patented claims recited cellobiohydrolase variants that are desirable as recited in patented claim 1, an ordinarily skilled artisan at the time of filing or invention would have been motivated to employ embodiment cellobiohydrolases meeting the limitations of patented claim 1 and pending claim 21 in a manner to meet the features of claims 32-35 and 37-39 as taught by Teter as discussed above.
Response to arguments
The last remarks filed are dated 11/21/2025. While the amendments address the prior grounds of rejection, the new grounds of rejections of at least the independent claims under 35 U.S.C. 103 and 35 U.S.C. 101 are necessitied by applicant’s amendment. No substantive remarks are made regarding double patenting rejections.
Conclusion
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/TODD M EPSTEIN/Primary Examiner, Art Unit 1652