Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
This application is a US national phase of PCT/US2020/065293, filed December 16, 2024, with provisional application 62/948415, filed December 16, 2019.
Applicant’s amendment filed April 24, 2026 is acknowledged. Claims 1-31, 34-35, 40-41 and 46-47 are canceled, claims 32, 36-38, 42-44, and 48-49 are amended, and claims 50-71 and 73-74 are newly added. No claim 72 has been presented.
Currently claims 32-33, 36-39, 42-45, 48-71, and 73-74 are pending.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 32-33, 36-39, 42-45, 48-53, 58-61, 66-69 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The Federal Circuit has clarified the application of the written description requirement to inventions in the field of biotechnology. See University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568,43 USPQ2d l398, 1406 (Fed. Cir. 1997). The Court stated that a written description of an invention requires a precise definition, one that defines the structural features of the chemical genus that distinguishes it from other chemical structures. A definition by function does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. Further, the Court held that to adequately describe a claimed genus, an applicant must describe a representative number of species of the claimed genus, and that one of skill in the art should be able to "visualize or recognize the identity of the members of the genus."
Claims 32, 38, and 44 recite “a thermostable xylanase having at least 85% identity to the polypeptide of SEQ ID NO: 2” and claims 50, 52, 58, 60, 66, and 68 recite the thermostable xylanase has at least 90% or 95% identity to SEQ ID NO: 2. Thus, the claims require a polypeptide having the aforementioned activity with at least 85%, 90% or 95% sequence identity to SEQ ID NO: 2. However, the specification has failed to sufficiently describe the structural features that must be retained by members of the claimed genus as to establish a structure-function relationship with respect to the activity, except for identifying the polypeptide as having the motif YITEMD (SEQ ID NO: 30). For example, SEQ ID NO: 2 is 328 amino acids long. A protein sharing only 85% identity relative to SEQ ID: 2 could have anywhere from 1 to 49 substitutions, deletions or additions in any combination along any length of SEQ ID: 6. Thus, an enormous genus (2048 = 2.8 x 1062) comprising literally more than trillions of sequences is encompassed by the tremendously broad scope of the claims.
However, while the claims are drawn to a genus that comprises literally trillions of sequences, the specification has only adequately described and successfully reduced to practice the full-length of SEQ ID NO’s: 2-4. This is not representative of the extremely large genus of sequences claimed, since only two other variants of SEQ ID NO: 2 is demonstrated to have thermostable xylanase activity. At best, the specification contemplates the use of BLAST to identify functional homologs based on sequence homology. However, this is not sufficient to describe members of the claimed genus because such methods access online databases that are continually being updated as sequencing technology improves. As a result, they are not a static source of information. Thus, one of skill in the art would readily appreciate that relying on a non-patent source that is continuously subject to change as a means to identify members of the claimed genus does not sufficiently meet the written description requirement.
Moreover, Friedberg (Brief. Bioinformatics (2006) 7: 225-242) teaches that homology-based transfer is not reliable for functional annotation even with high alignment percentages (page 227, second column). Friedberg also teaches that identification of functionally significant sub-regions is critical to functional annotation, and that often addition, deletion, or re-shuffling of domains can lead to errors in annotation (page 227, second column, page 228, first paragraph). Furthermore, Friedberg teaches that sequence-based tools are just not sensitive enough to identify functional protein similarity as databases get larger, and diversity of sequences gets larger (page 228, first full paragraph).
Thorton et al. (Nature structural biology, structural genomics supplement, November 2000, pgs. 991-994) teaches that the same protein structure is often seen in apparently different homologous families with different functions. Thorton et al. further describe examples of little correlation between specific enzyme function and overall protein structure (see page 992, right column, at lines 2-10).
Thus, when taken with the teachings of Friedberg and Thorton, one of skill in the art would readily appreciate that sequence homology alone cannot serve as the basis to describe members of the genus that have the recited function.
In the absence of a representative number of examples and any art-recognized structure-function relationship, the specification must at least describe the structural features that are required for the claimed function, in this case to the aforementioned activities. However, as discussed above, the specification fails to describe any substantive structural limitations as to establish a structure-function relationship with respect to the activities. Instead, Applicant merely offers a statement that any polypeptide having the intended activity will work.
Accordingly, the claims as currently written are not adequately described and one of skill in the art would readily appreciate that Applicant was not in possession of the claimed genus at the time of filing.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 32-33, 36-39, 42-45, 48-71 and 73-74 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 32, 38, and 44 recite the limitation “at a pH of above 4.8 to 6.0”. This limitation is indefinite because it does not clearly define the claimed pH range, specifically the phrase “above 4.8 to 6.0” is ambiguous and fails to clearly indicate the lower and upper bounds of the claimed pH. Accordingly, one of ordinary skill in the art would not be able to ascertain the metes and bounds of the claim.
Claims 33, 36-37, 39, 42-43, 45, 48-71, and 73-74 are likewise rejected as being dependent on an indefinite claim.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 57, 65, and 74 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claims 57 recites “The process of claim 56, wherein the xylanase is a GH10 xylanase from Thermatoga containing the motif YITEMD (SEQ ID NO: 30)”, however claim 56 recites “the thermostable xylanase comprises the polypeptide of SEQ ID NO: 2” which inherently is a GH10 xylanase from Thermotoga containing the motif YITEMD (SEQ ID NO: 30), therefore does not further limit the claims. Likewise, claims 65 and 74 are rejected as failing to further limit the subject matter.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 32-33, 36, 38-39, 42, 45, 48, 50-71, and 73-74 are rejected under 35 U.S.C. 103 as being unpatentable over Kang et al. (WO 2017/112540 A1, cited in PTO-892 mailed 1/10/2025, hereinafter “Kang”) in view of Steffens et al. (WO 2012/033926 A1, hereinafter “Steffens”).
Kang teaches processes for producing fermentation products from starch-containing material using an alpha-amylase and a thermostable hemicellulase (abstract). Kang teaches liquefying the starch-containing material such as corn or wheat at a temperature from 70-95⁰C using a hemicellulase enzyme that is preferably a xylanase having a melting point above 82⁰C, saccharifying using a glucoamylase, and fermenting using a fermenting organism to produce ethanol, which meets the limitations in claims 32, 33, 38, 39 (claims 1-3, 12, 15, 19-21, 23). In Example 22, Kang teaches the pH of each corn slurry was adjusted to 5.0 using 40% H2SO4, which falls within the pH range in the claims (pg. 134, lines 6-7). In Example 21, Kang teaches adding thermostable xylanase in the liquefaction of ground corn flour from an industrial corn ethanol plant, and its effect on ethanol yield (pg. 129). The thermostable xylanase is from Talaromyces leycettanus (TI Xyl) and combined with thermostable glucoamylase had a 1.5% increase in ethanol production and up to 18.3% increase of solubilized feruloylated arabinoxylan (SFA) over the method not utilizing the xylanase, thus meeting the limitations of decreasing residual starch in claims 36, 38, 42, and 48 (pg. 130, Tables 26 & 27).
Kang does not teach a thermostable xylanase with at least 85%, 90%, 95%, 99% or 100% sequence identity to instant SEQ ID NO: 2, and containing the motif YITEMD.
However, Steffens teaches methods for treating lignocellulosic material with xylanase enzyme that is stable and active at increased pH and temperatures (abstract). Steffens teaches lignocellulosic material that can be used in the method can include agriculture residues such as corn stover (pg. 9, lines 27-31). Steffens teaches the method can be carried out at a temperature ranging from 10⁰C to 100⁰C, and from pH 6 to pH 12, which overlaps with the ranges recited in the claims (pg. 38, lines 7-20). Steffens teaches the method comprises reacting an enzyme that has an amino acid sequence of SEQ ID NO: 8 (TmXynB), which has 100% sequence identity to the instant SEQ ID NO: 2 (See sequence comparison below), thus meets the limitations in the claims.
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Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to modify the method of producing ethanol from ground corn flour with a combination of an alpha-amylase and a thermostable xylanase as taught by Kang, and substitute with the thermostable xylanase TmXynB that comprises instant SEQ ID NO: 2 taught by Steffens with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to use the thermostable xylanases in breaking down industrial corn mashes and corn stover, thereby reducing residual starch, as taught by Kang and Steffens.
Claims 37, 43-44, and 49 are rejected under 35 U.S.C. 103 as being unpatentable over Kang and Steffens as applied to claims 32-33, 36, 38-39, 42, 45, 48, 50-71, and 73-74 above, and further in view of Zhengqiang et al. (Jrnl of Biosci and Bioeng, 2001, vol. 92, no. 5, pgs. 423-428, cited in PTO-892 mailed 3/4/2026, hereinafter “Zheng”).
Kang teaches the thermostable xylanase from T. leycettanus (TI Xyl) combined with the thermostable glucoamylase had a 1.5% increase in ethanol production and up to 18.3% increase of solubilized feruloylated arabinoxylan (SFA) over the method not utilizing the xylanase (pg. 130, Tables 26 & 27). Steffens teaches xylanases are an enzyme capable of at least hydrolyzing xylan to xylobiose and xylotriose (pg. 10, lines 27-29). Steffens teaches in the enzymatic assay measuring the release of xylose (a short chain oligosaccharide) per minute, TmXynB performed at 136% with aqueous ammonia pretreatment followed by neutralization and an hour activity incubation (pg. 45, Table 5). Neither Kang nor Steffens teach the thermostable xylanases specifically increase short-chain oligosaccharides in the method.
However, Zheng teaches characterization of the same thermostable family 10 endo-xylanase (XynB) from Thermotoga maritima (title), that Steffens teaches. Zheng teaches at 50°C, XynB displayed an optimum pH of 6.14 and at this pH the temperature for optimal enzyme activity was 90°C (abstract). Zheng teaches the xylanase gene (xynB, TM0070, AEO01693) has 100% local similarity to instant SEQ ID NO: 2 and contains the YITEMD motif (See sequence comparison below) (pg. 424, col. 1, para 2). Zheng also teaches XynB exhibited a broad substrate specificity, and was highly active towards p-nitropheny-β-D-xylobioside (pNP-X2) and p-nitropheny-β-D-xyloside (abstract). Zheng teaches the main product in the pNP-X2 reaction was xylobiose (a short chain DP2 oligosaccharide), indicating that hydrolysis of the bond between pNP and xylobiose was the major reaction (pg. 427, col. 2, para 2).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to modify the method of producing ethanol from ground corn flour with a combination of an alpha-amylase and a thermostable xylanase as taught by Kang, and substitute with the thermostable xylanase TmXynB that comprises instant SEQ ID NO: 2 taught by Steffens, to increase the amount of short-chain oligosaccharides xylobiose as taught by Zheng with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to utilize the TmXynB taught by Steffens and Zheng in the method taught by Kang for efficient hydrolysis of starch-containing material, thereby increasing the amount of short-chain oligosaccharides in the liquefact.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual 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/apply/applying-online/eterminal-disclaimer.
Claims 32-33, 36, 38-39, 42, 45, 48, 50-71, and 73-74 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 and 6-26 of U.S. Patent No. 10689630B2 (‘630) (cited in PTO-892 mailed 1/10/2025) in view of Steffens.
Patent claims 1-3 and 6-29 of ‘630 recite a process for producing a fermentation product from starch containing material comprising liquefying using an alpha amylase and GH10 xylanase having a melting point above 80 ⁰C, saccharifying using a glucoamylase enzyme, and fermenting using a fermenting organism, wherein the starch containing material is corn. Claims 1-3 and 6-26 do not recite the thermostable xylanase is at least 85%/90%/95%/99%/100% sequence identity to instant SEQ ID NO: 2, and containing the motif YITEMD.
However, Steffens teaches methods for treating lignocellulosic material with xylanase enzyme that is stable and active at increased pH and temperatures (abstract). Steffens teaches lignocellulosic material that can be used in the method can include agriculture residues such as corn stover (pg. 9, lines 27-31). Steffens teaches the method can be carried out at a temperature ranging from 10⁰C to 100⁰C, and a pH from pH 6 to pH 12, which overlaps the ranges recited in the claims (pg. 38, lines 7-20). Steffens teaches the method comprises reacting an enzyme that has an amino acid sequence of SEQ ID NO: 8 (TmXynB), which has 100% sequence identity to instant SEQ ID NO: 2 (See sequence comparison above), thus meets the limitations in the claims.
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to modify the method of producing ethanol from ground corn flour with a combination of an alpha-amylase and a thermostable xylanase as recited in ‘630, and substitute with the thermostable xylanase TmXynB that comprises instant SEQ ID NO: 2 taught by Steffens with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to use the thermostable xylanases in breaking down industrial corn mashes and corn stover, thereby reducing residual starch, as recited in ‘630 and taught by Steffens.
Claims 32-33, 36-39, 42-45, 48-71, and 73-74 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 and 6-26 of U.S. Patent No. 10689630B2 (‘630) in view of Steffens and Zheng.
As discussed above, instant claims 32-33, 36, 38-39, 42, 45, 48, 50-71, and 73-74 were obvious over claims 1-3 and 6-26 of ‘630 in view of Steffens. ‘630 and Steffens are silent on decreasing the amount of residual starch, and increasing the amount of short-chain oligosaccharides.
However, Zheng teaches characterization of the same thermostable family 10 endo-xylanase (XynB) from Thermotoga maritima (title), that Steffens teaches. Zheng teaches at 50°C, XynB displayed an optimum pH of 6.14 and at this pH the temperature for optimal enzyme activity was 90°C (abstract). Zheng teaches the xylanase gene (xynB, TM0070, AEO01693) has 100% local similarity to instant SEQ ID NO: 2 and contains the YITEMD motif (See sequence comparison below) (pg. 424, col. 1, para 2). Zheng also teaches XynB exhibited a broad substrate specificity, and was highly active towards p-nitropheny-β-D-xylobioside (pNP-X2) and p-nitropheny-β-D-xyloside (abstract). Zheng teaches the main product in the pNP-X2 reaction was xylobiose (a short chain DP2 oligosaccharide), indicating that hydrolysis of the bond between pNP and xylobiose was the major reaction (pg. 427, col. 2, para 2).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to modify the method of producing ethanol from ground corn flour with a combination of an alpha-amylase and a thermostable xylanase as recited in ‘630, and substitute with the thermostable xylanase TmXynB that comprises instant SEQ ID NO: 2 taught by Steffens, to increase the amount of short-chain oligosaccharides xylobiose as taught by Zheng with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to utilize the TmXynB taught by Steffens and Zheng in the method recited in ‘630 for efficient hydrolysis of starch-containing material, thereby increasing the amount of short-chain oligosaccharides in the liquefact.
Response to Arguments
Applicant's arguments filed April 24, 2026 have been fully considered but they are not persuasive.
Regarding Remarks directed to the rejection of claims 32-49 under 35 U.S.C. § 112(a), Applicant argues the newly amended claims requiring a polypeptide with 85% sequence identity to EQ ID NO: 2 are defined by structural features, namely a high percent sequence identity, thus is a structural definition, and that there is a well-established definitive relationship between protein function and % identity. Applicant argues the specification discloses 3 examples of thermostable xylanases with the YITEMD motif, some with as little as 83% identity, thus argues the specification provides clear structural guidance sufficient to support the full genus.
As described above in the modified 112(a) rejection, sequence homology alone does not provide enough structural details for sufficient possession of the claimed genus, since there are trillions of variants claimed. Further, only indicating the sequence contains the motif YITEMD does not provide enough structural details on whether or not this motif is integral in enzyme functionality, and the specification does not disclose the structure-function relationship, only indicating the YITEMD is commonly found in Thermotoga xylanases. Thus the written description rejection is maintained.
Regarding Remarks direct to the rejection of claims 32-49 under 35 U.S.C. § 103, Applicant argues a person of ordinary skill in the art would not have a reasonable expectation of success of substituting the thermostable xylanase in the method taught by Kang with the XynB from T. maritima taught by Zheng. Applicant points to the Winterhalther and Liebl reference filed 4/24/2026, that showed the XynB (with 100% sequence identity to SEQ ID NO: 2) was assayed under conditions relevant to the claimed process, and showed no detectable activity on the starch, only releasing DP2, DP3, and DP1 products which are chemically distinct from the starch-derived DP1-DP6 products of the claimed process. Applicant argues the affidavit submitted by Soong filed 4/24/2026 confirm the effect of XynB on residual starch or DP1-DP6 production during starch liquefaction to be uncertain and unpredictable. Applicant argues as explained in the Soong declaration, even among thermostable GH10 xylanases that are both active on xylan and suitable for high-temperature processing, effects on residual starch reduction and DP1-DP6 production in liquefaction are enzyme-specific and depend on the starch-fiber matrix. Applicant argues that even if prima facie case were established, the unexpected results in Example 7 disclose Tm xylanase liquefaction was significant compared to the control. Applicant also argues the SFA taught in Kang is not equivalent to the DP1-DP6 short chain oligosaccharides in the claimed method, and Zheng’s general characterization of XynB does not teach or suggest dose responsive superiority under the claimed conditions as a real and reproducible advantage for the claimed T. maritima xylanase.
In response to applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, Kang teaches the overall claimed method utilizing a thermostable xylanase with a glucoamylase at the specified pH and temperature parameters to liquify starch-containing material, and Steffens teaches the thermostable xylanase from T. maritima that comprises instant SEQ ID NO: 2 that is efficient in breaking down lignocellulosic material, and releasing short chain oligosaccharides as taught by Zheng. A person of ordinary skill in the art would be motivated to utilize other thermostable xylanases, such as TmXynB, in the method taught by Kang. Furthermore, regarding applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Although Kang is silent on the production of DP1-DP6 short chain oligosaccharides, only measuring SFA oligosaccharides, it is noted that the features upon which applicant relies (i.e. DP1-DP6 short chain oligosaccharides and its relation to dose dependent increase of the enzyme) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Furthermore, the specification discloses the use of wheat arabinoxylan as a substrate for the enzymatic assays of the xylanase, which appropriately broke down into xylo-oligosaccharides, the same assay used in the characterization assay taught by Zheng. Regarding Applicant’s assertion of unexpected results over the prior art, the results were only significant over the control, and Tm xylanase contributed to only 1% less residual starch than the Dt xylanase, which underlines the changeability of these thermostable xylanases in the claimed method, albeit one is slightly more efficient at liquification than the other.
Regarding Remarks directed to the nonstatutory double patenting rejection over US Patent No. 11689630B2, Applicant argues the claims of ‘630 doe not disclose or suggest the features of the newly amended claims, and argue Zheng does not cure these deficiencies.
Applicant's arguments fail to comply with 37 CFR 1.111(b) because they amount to a general allegation that the claims define a patentable invention without specifically pointing out how the language of the claims patentably distinguishes them from the references. Thus the non-statutory double patenting rejection is maintained.
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JESSICA EDWARDS whose telephone number is (571)270-0938. The examiner can normally be reached M-F 8am-5pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Louise Humphrey can be reached at (571) 272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/JESSICA EDWARDS/
Examiner, Art Unit 1657
Prosecution Insights