POLYPEPTIDES

§101 §103 §112

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 divisional of 17/051,454, issued as US Patent No. 12,110,518, which is a 371 of PCT/CN2019/089237. The amendment filed on July 31, 2026 has been entered. Election/Restrictions Applicant's election with traverse of Group I with an election of species of (A) SEQ ID NO: 3 as the GH114 glycosyl hydrolase and (B) SEQ ID NO:62 as the motif in the reply filed on July 31, 2026 is acknowledged. The traversal is on the ground(s) that (1) there would not be a serious burden to examine SEQ ID NO:3, 6, 81, 82, 132, and 136 since these amino acid sequences have a high sequence identify of more than 85% and (2) claim 21 links Groups I and II. This is not found persuasive because (1) SEQ ID NO:3, 6, 81, 82, 132, and 136 are glycosyl hydrolases from different microorganism and each of the glycosyl hydrolases require a different search queries and (2) claim 21 is not a linking claim linking Groups I and II. According to MPEP 809, linking claims and the inventions they link together are usually either all directed to products or all directed to processes. In the instant case, Group I is directed to a product and Group II is directed to a method. Therefore, claim 21 does not link Groups I and II. Instead, the inventions of Group I and II are related as product and process of use, as discussed in the Requirement for Restriction/Election mailed on June 1, 2026. The requirement is still deemed proper and is therefore made FINAL. Claims 25-27 and 33-34 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species (claims 25-27) and invention (claims 33-34), there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on July 31, 2026. Claim Status Claims 21-34 are pending. Claims 25-27 and 33-34 are withdrawn. Claims 21-24 and 28-32 are under examination. Foreign Priority Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d). The certified copy has been filed in parent Application No. 17/051,454, filed on 10/29/2020. Information Disclosure Statement The information disclosure statement (IDS) submitted on October 1, 2024 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Claim Rejections - 35 USC § 112 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. Claim 29 is 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. Claim 29 recites the limitation "wherein the anionic surfactant" in line 1. There is insufficient antecedent basis for this limitation in the claim. Claim 29 depends from claim 21. Claim 21 does not recite an anionic surfactant. Appropriate correction is requested. 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 21-24 and 28-32 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. It is noted that MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' In this case, the claims have been broadly interpreted as a cleaning composition comprising a genus of GH114 glycosyl hydrolase having at least 80-95% sequence identity to SEQ ID NO:3, having alpha-1,4-polygalactosaminidase activity, and having the properties recited in claims 31-32. MPEP 2163 I. states that to “satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. MPEP 2163. II.A.3.(a) sates that “Possession may be shown in many ways. For example, possession may be shown by describing an actual reduction to practice of the claimed invention. Possession may also be shown by a clear depiction of the invention in detailed drawings or in structural chemical formulas which permit a person skilled in the art to clearly recognize that inventor had possession of the claimed invention. An adequate written description of the invention may be shown by any description of sufficient, relevant, identifying characteristics so long as a person skilled in the art would recognize that the inventor had possession of the claimed invention. According to MPEP 2163.II.A.3.(a).ii), “Satisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’" The recitation of “GH114 glycosyl hydrolase”, “alpha-1,4-polygalactosaminidase activity”, and having the properties recited in claims 31-32 fails to provide a sufficient description of the genus of the polypeptides as it merely describes the functional features of the genus without providing any definition of the structural features of the species within the genus. The specification does not specifically define any of the species that fall within the genus. The specification does not define any structural features commonly possessed by members of the genus that distinguish them from others. One skilled in the art therefore cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus. At the time the application was effectively filed, the prior art does not teach a GH114 glycosyl hydrolase having the amino acid sequence of SEQ ID NO:3 and having alpha-1,4-polygalactosaminidase activity. The claimed genus of GH114 glycosyl hydrolase having at least 80-95% sequence identity to SEQ ID NO:3, having alpha-1,4-polygalactosaminidase activity, and having the properties recited in claims 31-32 were not known in the art. Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-1449) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-1449) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”. The specification is limited to a cleaning composition comprising of specific GH114 glycosyl hydrolases, such as the GH114 glycosyl hydrolase having the amino acid sequence of SEQ ID NO:3, which comprises the motif of SEQ ID NO:62. While MPEP 2163 acknowledges that in certain situations “one species adequately supports a genus,” it also acknowledges that “[f]or inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus.” In view of the widely variant species encompassed by the genus, the limited description of GH114 glycosyl hydrolases are not enough and does not constitute a representative number of species to describe the whole genus. Therefore, the specification fails to describe a representative species of the claimed genus. Further, with the aid of a computer, one of skill in the art could identify all polypeptides having 80-95% sequence identity with SEQ ID NO:3. However, there is no teaching regarding which 5-20% of the amino acids of SEQ ID NO:3 can be modified and result in polypeptide having alpha-1,4-polygalactosaminidase activity and having the properties recited in claims 31-32. An important consideration is that structure is not necessarily a reliable indicator of function. In the instant case, there is no disclosure relating similarity of structure to conservation of function. Conservation of structure is not necessarily a surrogate for conservation of function. Given this lack of description of the representative species encompassed by the genus of the claims, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants were in possession of the inventions of claims 21-24 and 28-32. Claims 21-24 and 28-32 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a cleaning composition comprising of specific GH114 glycosyl hydrolases, such as the GH114 glycosyl hydrolase having the amino acid sequence of SEQ ID NO:3, which comprises the motif of SEQ ID NO:62, does not reasonably provide enablement for a cleaning composition comprising any GH114 glycosyl hydrolase having at least 80-95% sequence identity to SEQ ID NO:3, having alpha-1,4-polygalactosaminidase activity, and having the properties recited in claims 31-32. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims. Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). They include (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims. The breadth of the claims. It is noted that MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.' In this case, the claims have been broadly interpreted as a cleaning composition comprising any GH114 glycosyl hydrolase having at least 80-95% sequence identity to SEQ ID NO:3, having alpha-1,4-polygalactosaminidase activity, and having the properties recited in claims 31-32. The claims are not commensurate with the enablement provided by the disclosure with regard to the extremely large number of polypeptides having alpha-1,4-polygalactosaminidase activity and having the properties recited in claims 31-32. In the instant case, the specification is limited to a cleaning composition comprising of a specific GH114 glycosyl hydrolases, such as the GH114 glycosyl hydrolase having the amino acid sequence of SEQ ID NO:3. The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While enzyme isolation techniques, recombinant and mutagenesis techniques were known in the art at the time of the invention, e.g. mutagenesis, and it is routine in the art to screen for variants comprising multiple substitutions or multiple modifications as encompassed by the instant claims, the specific amino acid positions within the protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions. In the absence of: (a) rational and predictable scheme for making any polypeptide having at least 80-95% sequence identity to SEQ ID NO:3 and having alpha-1,4-polygalactosaminidase activity and having the properties recited in claims 31-32, or (b) a correlation between structure and function of having alpha-1,4-polygalactosaminidase activity and having the properties recited in claims 31-32, the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. One of skill in the art would have to test these infinite possible polypeptides to determine which polypeptides have alpha-1,4-polygalactosaminidase activity and have the properties recited in claims 31-32. While enablement is not precluded by the necessity for routine screening, if a large amount of screening is required, as is the case herein, the specification must provide a reasonable amount of guidance which respect to the direction in which the experimentation should proceed so that a reasonable number of species can be selected for testing. In view of the fact that such guidance has not been provided in the instant specification, it would require undue experimentation to enable the full scope of the claims. The state of prior art, the relative skill of those in the art, and predictability or unpredictability of the art. Since the amino acid sequence of the mutant determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. In the instant case, neither the specification or the art provide a correlation between structure and activity such that one of skill in the art can envision the structure of any polypeptides having deoxyribose-phosphate aldolase activity or predict said function of a polypeptide from its primary structure. In addition, the art does not provide any teaching or guidance as to (1) which amino acids within the polypeptide of SEQ ID NO:3 that can be modified and which ones are conserved such that one of skill in the art can make the recited polypeptides having alpha-1,4-polygalactosaminidase activity and having the properties recited in claims 31-32, (2) which segments of the polypeptide of SEQ ID NO:3 are essential for having alpha-1,4-polygalactosaminidase activity and having the properties recited in claims 31-32, and (3) the general tolerance of the polypeptide of SEQ ID NO:3 to structural modifications and the extent of such tolerance. The art clearly teaches that changes in a protein's amino acid sequence to obtain the desired activity without any guidance/knowledge as to which amino acids in a protein are required for that activity is highly unpredictable. At the time of the invention there was a high level of unpredictability associated with altering a polypeptide sequence with an expectation that the polypeptide will maintain the desired activity. For example, Studer (Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes. Biochem. J. (2013) 449, 581–594. – form PTO-892) teach that (1) protein engineers are frequently surprised by the range of effects caused by single mutations that they hoped would change only one specific and simple property in enzymes, (2) the often surprising results obtained by experiments where single mutations are made reveal how little is known about the rules of protein stability, and (3) the difficulties in designing de novo stable proteins with specific functions. At the time the application was effectively filed, the prior art does not teach a GH114 glycosyl hydrolase having the amino acid sequence of SEQ ID NO:3and having alpha-1,4-polygalactosaminidase activity. The claimed scope of GH114 glycosyl hydrolase having at least 80-95% sequence identity to SEQ ID NO:3, having alpha-1,4-polygalactosaminidase activity, and having the properties recited in claims 31-32 were not known in the art. Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-1449) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-1449) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”. The amount of direction or guidance presented and the existence of working examples. The specification is limited to a cleaning composition comprising of a specific GH114 glycosyl hydrolases, such as the GH114 glycosyl hydrolase having the amino acid sequence of SEQ ID NO:3. However, the specification fails to provide any information as to (1) specific substrates associated with any polypeptide having 80-95% sequence identity to SEQ ID NO:3 or (2) structural elements required in a polypeptide having alpha-1,4-polygalactosaminidase activity and having the properties recited in claims 31-32. Thus, in view of the overly broad scope of the claims, the lack of guidance and working examples provided in the specification, the high level of unpredictability of the prior art in regard to structural changes and their effect on function and the lack of knowledge about a correlation between structure and function, an undue experimentation would be necessary one having ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of polypeptides having the desired biological characteristics recited in the claims are unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). Claim Rejections - 35 USC § 103 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness. This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claims 21-23 and 28-30 are rejected under 35 U.S.C. 103 as being unpatentable over A0A2N3WSQ5 (UniProtKB/TrEMBL Database. April 25, 2018 – form PTO-892) and Lant (US 2018/0155802 – form PTO-1449) Regarding claims 21-23, A0A2N3WSQ5 discloses a GH114 glycosyl hydrolase having 92.6% sequence identity to SEQ ID NO:3 of the instant application, having alpha-1,4-polygalactosaminidase activity and having the motif of SEQ ID NO:62 (see pages 1-2 and see the sequence alignment below, wherein the motif is underlined). A0A2N3WSQ5 does not disclose a cleaning composition comprising the above GH114 glycosyl hydrolase. However, a cleaning composition comprising of GH114 glycosyl hydrolases were known in the art. Regarding claim 21 and 28-30, Lant discloses a cleaning composition to clean textiles, wherein the composition comprises (a) at least 0.01 ppm of GH114 glycosyl hydrolase having alpha-1,4-polygalactosaminidase activity ([0005], (b) an anionic surfactant of sulfates and sulfonates ([0095]-[0108]), and (c) a nonionic surfactant ([0109]-[0110]). Therefore, combining the teachings of A0A2N3WSQ5 and Lant, it would have been obvious to one having ordinary skill in the art at the time the claimed invention was effectively filed to make a cleaning composition comprising the GH114 glycosyl hydrolase of A0A2N3WSQ5. One of ordinary skill in the art would have been motivated to do so in order to use the GH114 glycosyl hydrolase of A0A2N3WSQ5 in a cleaning composition to clean textiles. One of ordinary skill in the art would have had a reasonable expectation of success since Lant discloses a cleaning composition comprising GH114 glycosyl hydrolase having alpha-1,4-polygalactosaminidase activity and anionic/nonionic surfactants and A0A2N3WSQ5 discloses a GH114 glycosyl hydrolase having alpha-1,4-polygalactosaminidase activity. The rationale to support that the claim would have been obvious is that all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination yielded nothing more than predictable results to one of ordinary skill in the art. Therefore, the above references render claims 21-23 and 28-30 prima facie obvious. 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 21-24 and 31-32 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Claim interpretation MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' Claims 21-24 and 31-32 are directed to a cleaning composition comprising (a) GH114 glycosyl hydrolase having at least 80-100% sequence identity to SEQ ID NO:3 and (b) a cleaning component. The specification discloses that the GH114 glycosyl hydrolase having the amino acid sequence of SEQ ID NO:3 was obtained from Amycolatopsis circi (Table 2 at page 201). A0A2N3WSQ5 (UniProtKB/TrEMBL Database. April 25, 2018 – form PTO-892) discloses an Amycolatopsis echigonensis GH114 glycosyl hydrolase having 92.6% sequence identity to SEQ ID NO:3 of the instant application and having alpha-1,4-polygalactosaminidase activity. The cleaning component comprised in the cleaning composition has been broadly interpreted as any component, such as water. Therefore, the cleaning composition comprises (a) an Amycolatopsis circi GH114 glycosyl hydrolase, a natured based product, or Amycolatopsis echigonensis GH114 glycosyl hydrolase, a natured based product and (b) any component, such as water, a nature based product. Step 1: This part of the eligibility analysis evaluates whether the claim falls within any statutory category (see MPEP 2106.03). Since the claims are directed to a protease mutant, the claims are directed to a composition of matter, which is one of the statutory categories of invention. (Step 1: YES) Step 2A Prong 1: This part of the eligibility analysis evaluates whether the claim recites a judicial exception (see MPEP 2106.04). The GH114 glycosyl hydrolase comprised in the claimed composition is not considered to have markedly different characteristics from what occurs in nature, Amycolatopsis circi GH114 glycosyl hydrolase or Amycolatopsis echigonensis GH114 glycosyl hydrolase, as discussed above, and is considered to be a law of nature exception. Further, there is no indication in the specification that placing the GH114 glycosyl hydrolase in a generic cleaning composition results in the GH114 glycosyl hydrolase having any characteristics (structural, functional, or otherwise) that are different from the naturally occurring Amycolatopsis circi GH114 glycosyl hydrolase or Amycolatopsis echigonensis GH114 glycosyl hydrolase. Because there is no difference in characteristics (structural, functional, or otherwise) between the claimed GH114 glycosyl hydrolase and the naturally occurring Amycolatopsis circi GH114 glycosyl hydrolase or Amycolatopsis echigonensis GH114 glycosyl hydrolase, the claimed composition comprising GH114 glycosyl hydrolase is directed to a judicial exception. Step 2A Prong 2: This part of the eligibility analysis evaluates whether the claim as a whole integrates the recited judicial exception into a practical application (see MPEP 2106.04(d)). This evaluation is performed by (a) identifying whether there are any additional recited elements in the claim beyond the judicial exception and (b) evaluating those additional elements individually and in combination to determine whether the claim as a whole integrates the exception into a practical application. There are no additional elements recited in the claim beyond the judicial exception. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claimed GH114 glycosyl hydrolase is found naturally occurring in nature (Amycolatopsis circi GH114 glycosyl hydrolase or Amycolatopsis echigonensis GH114 glycosyl hydrolase). The claims recite a generic cleaning composition comprising the naturally occurring GH114 glycosyl hydrolase and a generic component, such as water. The addition of an intended use does not impart any added benefit to the claimed GH114 glycosyl hydrolase or integrate the claimed GH114 glycosyl hydrolase into a practical application. (Step2 A: YES) Step 2B: This part of the eligibility analysis evaluates whether the claim as a whole amounts to significantly more than the recited exception, i.e., whether any additional element, or combination of additional elements, adds an inventive concept to the claim (see MPEP § 2106.05). The claim only recites the laws of nature and do not include any additional elements that could add significantly more to the judicial exceptions. (Step 2B: NO) As such, the claims do not qualify as eligible subject matter. Conclusion Claims 21-34 are pending. Claims 25-27 and 33-34 are withdrawn. Claims 21-24 and 28-32 are rejected. Any inquiry concerning this communication or earlier communications from the examiner should be directed to YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 7:00am - 5:00pm. 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, Robert Mondesi can be reached on 408-918-7584. 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. /YONG D PAK/Primary Examiner, Art Unit 1652 Sequence alignment of the GH114 glycosyl hydrolase of SEQ ID NO:3 of the instant application (“Qy”) and the GH114 glycosyl hydrolase of A0A2N3WSQ5 (“Db”) A0A2N3WSQ5_9PSEU ID A0A2N3WSQ5_9PSEU Unreviewed; 280 AA. AC A0A2N3WSQ5; A0A8E1VUP4; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 10-JUN-2026, entry version 18. DE SubName: Full=Glycosyl hydrolase family 114 {ECO:0000313|EMBL:PKV96880.1}; GN ORFNames=ATK30_7844 {ECO:0000313|EMBL:PKV96880.1}; OS Amycolatopsis echigonensis. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Amycolatopsis. OX NCBI_TaxID=2576905 {ECO:0000313|EMBL:PKV96880.1, ECO:0000313|Proteomes:UP000233750}; RN [1] {ECO:0000313|EMBL:PKV96880.1, ECO:0000313|Proteomes:UP000233750} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45165 {ECO:0000313|EMBL:PKV96880.1, RC ECO:0000313|Proteomes:UP000233750}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 Actinobacteria strains."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PKV96880.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PJMY01000003; PKV96880.1; -; Genomic_DNA. DR RefSeq; WP_101439677.1; NZ_PJMY01000003.1. DR OrthoDB; 319933at2; -. DR Proteomes; UP000233750; Unassembled WGS sequence. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR017853; GH. DR InterPro; IPR004352; GH114_TIM-barrel. DR PANTHER; PTHR35273; ALPHA-1,4 POLYGALACTOSAMINIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G07890)-RELATED; 1. DR PANTHER; PTHR35273:SF2; ALPHA-GALACTOSIDASE; 1. DR Pfam; PF03537; Glyco_hydro_114; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Hydrolase {ECO:0000313|EMBL:PKV96880.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000233750}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..280 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5047735009" FT DOMAIN 56..268 FT /note="Glycoside-hydrolase family GH114 TIM-barrel" FT /evidence="ECO:0000259|Pfam:PF03537" SQ SEQUENCE 280 AA; 29921 MW; 5512A61B35CDF425 CRC64; Query Match 92.6%; Score 1216; Length 280; Best Local Similarity 92.3%; Matches 227; Conservative 6; Mismatches 13; Indels 0; Gaps 0; Qy 1 APLPSPHSQVKDVPLPTPHAGFDYQIGGPYQPPAGVQVVSRDHSAPAAAGLYNICYVNAF 60 |||||||||| ||||| |||||||||||||||||||||||||||||||:||||||||||| Db 35 APLPSPHSQVADVPLPAPHAGFDYQIGGPYQPPAGVQVVSRDHSAPAASGLYNICYVNAF 94 Qy 61 QAQPGAEKEWGDLVLRDGDGKVVMDPDWNEALLDLRTADKRSRIADKVGTWIDECAGKGY 120 | ||||||||||||||| || ||||||||||||| |||||||||||||| |||||||||| Db 95 QVQPGAEKEWGDLVLRDDDGTVVMDPDWNEALLDSRTADKRSRIADKVGAWIDECAGKGY 154 Qy 121 QAVEPDNYDSFTRSQGLLSARNAQDLVKLLSQRAHGKGLAIGQKNTSELASSRADNGLDF 180 ||:||||||||||||||||||||||||||||:|||||||||||||||||||||| ||||| Db 155 QAIEPDNYDSFTRSQGLLSARNAQDLVKLLSERAHGKGLAIGQKNTSELASSRAANGLDF 214 Qy 181 AVAEECGDQDNCAEYTQYFGNRVIVIEYTEDGLRNACDKWGAALSVVRRDRDVTPKGDSA 240 ||||||| ||||||||:|||:||||||||||||| || ||| ||||||||||||||||| Db 215 AVAEECGQQDNCAEYTRYFGDRVIVIEYTEDGLRTACAKWGNTLSVVRRDRDVTPKGDSA 274 Qy 241 YVRETC 246 ||||:| Db 275 YVRESC 280