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 continuation of PCT/JP2021/036011.
The amendment filed on October 14, 2025 has been entered.
Election/Restrictions
Applicant's election with traverse of Group I with a species election of 240F+241Q as the amino acid modifications made in the parent α-amylase in the reply filed on October 14, 2025 is acknowledged. The traversal is on the ground(s) that (1) restriction is only proper if the claims of the restricted groups are independent or patentability distinct and there would be a serious burden according to MPEP 803, (2) the USPTO has the burden of explaining why each group lacks unity with each other group specifically describing special features in each group, and (3) the claims were not found to lack of unity of invention in the November 1, 2021 International Preliminary Report on Patentability. This is not found persuasive. (1) MPEP 1893(d) states that “unity of invention analysis (not an independent and distinct analysis) is applicable in national stage applications submitted under 35 U.S.C. 371”. Further, section of MPEP 803 does not apply to national stage applications submitted under 35 U.S.C. 371. (2) The Requirement for Restriction/Election (lack of unity) mailed on July 14, 2025 discussed why Groups I-II and species lack unity of invention, see pages 4-5. (3) MPEP 1893.03(e) II states that the international preliminary examination report “reflects the IPEA’s non-binding opinion regarding lack of unity of invention, novelty, inventive step and industrial applicability”.
The traversal is on the ground(s) that the non-elected claims depend from, or otherwise include all the limitations of one or more claims of the elected group and Applicant request rejoinder. Applicant’s request is noted.
The requirement is still deemed proper and is therefore made FINAL.
Claims 4 and 6-10 withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species/invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on October 14, 2025.
Status of Claims
Claims 1-2 and 4-15 are pending.
Claims 4 and 6-10 are withdrawn.
Claims 1-2, 5, and 11-15 are under examination.
Claim for Foreign Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on March 30, 2023, October 30, 2023, December 27, 2024, and October 9, 2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Objections
Claim 5 is objected for the recitation of an internal period at line 8 and lacking a period at the end of the claim. See MPEP 608.01(m).
Appropriate correction is required.
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 14 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.
The term “low” in claim 14 is a relative term which renders the claim indefinite. The term “low” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. It is unclear as to how what temperature is considered as “low”. A perusal of the specification did not provide a clear definition for the above term. Without a clear definition in terms of numerical value, those skilled in the art would be unable to ascertain what temperature is a “low” temperature. Clarification 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 1-2, 5, and 11-15 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.
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' The claims have been broadly interpreted as any α-amylase mutant of a parent α-amylase, wherein the parent α-amylase has at least 90% sequence identity to SEQ ID NO:2 and two or more deletions at R178, G179, T180, and G181 and wherein the mutant has H240F+S241Q or amino acid substitutions and any other amino acid modifications. Therefore, the claims are drawn to a genus of polypeptides having unknown structure except having a Phe and Gln at the amino acid positions corresponding to H240 and S241 of SEQ ID NO:2 but having α-amylase activity.
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 “α-amylase” 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.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) 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-892) 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 description of specific α-amylase mutants of SEQ ID NO:2 as described in Tables 4-6. 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 examples of Tables 4-6 described above 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, one of skill in the art could identify mutants of SEQ ID NO:2. However, there is no teaching regarding which amino acids can vary from SEQ ID NO:2 (other than those specified in Tables 4-6) and retain α-amylase activity. 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. Since the claimed invention is that of an enzyme, and there is no disclosure of the domains responsible for having α-amylase activity, the absence of information may be persuasive that those of skill in the art would not take the disclosure as generic.
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 1-2, 5, and 11-15.
Claims 1-2, 5, and 11-15 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 specific α-amylase mutants of SEQ ID NO:2 as described in Tables 4-6, does not reasonably provide enablement any polypeptide having unknown structure except having a Phe residue and Gln residue at the amino acid positions corresponding to H240 and S241, respectively, of SEQ ID NO:2 but having α-amylase activity. 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.
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' The claims have been broadly interpreted as any α-amylase mutant of a parent α-amylase, wherein the parent α-amylase has at least 90% sequence identity to SEQ ID NO:2 and two or more deletions at R178, G179, T180, and G181 and wherein the mutant has H240F+S241Q or amino acid substitutions and any other amino acid modifications. Therefore, the claims are drawn to any polypeptide having unknown structure except having a Phe residue and Gln residue at the amino acid positions corresponding to H240 and S241, respectively, of SEQ ID NO:2 but having α-amylase activity.
The claims are not commensurate with the enablement provided by the disclosure with regard to the extremely large number of polypeptides having α-amylase activity. In the instant case, the specification is limited to specific α-amylase mutants of SEQ ID NO:2 as described in Tables 4-6.
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 α-amylase mutants having unknown structure and (b) a correlation between structure and the function of having α-amylase activity, 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 α-amylase activity. 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 provides a correlation between structure and activity such that one of skill in the art can envision the structure of any polypeptides having unknown structure but having α-amylase activity. In addition, the art does not provide any teaching or guidance as to (1) which segments of the polypeptide of SEQ ID NO:2 that are essential for polypeptides having α-amylase activity and (2) the general tolerance of the α-amylase of SEQ ID NO:2 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.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) 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-892) 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 specific α-amylase mutants of SEQ ID NO:2 as described in Tables 4-6. However, the speciation fails to provide any information as to (1) specific substrates associated with any α-amylase mutant of SEQ ID NO:2 or (2) structural elements required in a polypeptide having α-amylase activity.
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 § 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.
Claim(s) 1-2 and 5 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Yuuki (Complete nucleotide sequence of a gene coding for heat- and pH-stable alpha-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying alpha-amylases deduced from the DNA sequences. J Biochem. 1985 Nov;98(5):1147-56 - form PTO-892).
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' MPEP 2113 states that the “patentability of a product does not depend on its method of production.”. In the instant case, the structure of the claimed α-amylase mutant implied is the same whether the α-amylase mutant is obtained from recombinant engineering of a parent α-amylase mutant having at least 90% sequence identity to SEQ ID NO:2 and deletion of R178, G179, T180 and/or G181 or is obtained from any source (including wild type proteins), as long as the resulting product has the structural limitations recited in the claims: having a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 respectively, of SEQ ID NO:2. Therefore, the claims have been broadly interpreted as an α-amylase having a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 of SEQ ID NO:2, respectively, and any other amino acid difference compared to SEQ ID NO:2.
Regarding claims 1-2 and 5, Yuuki discloses α-amylase which has a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 of SEQ ID NO:2, respectively, and other amino acid difference compared to SEQ ID NO:2 (abstract and Fig. 3 at page 1150 and see the sequence alignment below).
Therefore, the reference of Yuuki anticipates claims 1-2 and 5.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-2, 5, and 11-15 are rejected under 35 U.S.C. 103 as being unpatentable over Yuuki (Complete nucleotide sequence of a gene coding for heat- and pH-stable alpha-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying alpha-amylases deduced from the DNA sequences. J Biochem. 1985 Nov;98(5):1147-56 - form PTO-892) and Sone (US Patent No. 5,030,377 – form PTO-892).
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' MPEP 2113 states that the “patentability of a product does not depend on its method of production.”. In the instant case, the structure of the claimed α-amylase mutant implied is the same whether the α-amylase mutant is obtained from recombinant engineering of a parent α-amylase mutant having at least 90% sequence identity to SEQ ID NO:2 and deletion of R178, G179, T180 and/or G181 or is obtained from any source (including wild type proteins), as long as the resulting product has the structural limitations recited in the claims: having a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 respectively, of SEQ ID NO:2. Therefore, the claims have been broadly interpreted as an α-amylase having a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 of SEQ ID NO:2, respectively, and any other amino acid difference compared to SEQ ID NO:2.
Regarding claims 1-2 and 5, Yuuki discloses a Bacillus licheniformis α-amylase which has a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 of SEQ ID NO:2, respectively, and other amino acid difference compared to SEQ ID NO:2 (abstract and Fig. 3 at page 1150 and see the sequence alignment below).
Yuuki does not disclose a cleaning agent composition comprising the Bacillus licheniformis α-amylase. However, use of Bacillus licheniformis α-amylase in a cleaning agent composition was well known in the art as discussed below.
Regarding claims 11-12, Sone discloses a detergent composition, which reads on a clothing cleaning agent composition, comprising a Bacillus licheniformis α-amylase (abstract and Column 2, line 63 through Column 3, line 8).
Regarding claim 13, Sone discloses that the detergent composition is in a powder form (Column 5, lines 50-52).
Regarding claims 14-15, Sone discloses that the detergent composition is used at a temperature of 20°C (Column 8, lines 33-43).
Therefore, in combining the teachings of Yuuki and Sone, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to arrive at a detergent composition comprising the Bacillus licheniformis α-amylase of Yuuki. One of ordinary skill in the art would have been motivated to make a detergent comprising the Bacillus licheniformis α-amylase of Yuuki since use of Bacillus licheniformis α-amylase in a cleaning agent composition was well known in the art. One of ordinary skill in the art would have had a reasonable expectation of success since Sone discloses a detergent composition comprising a Bacillus licheniformis α-amylase.
Therefore, the above references render claims 1-2, 5, and 11-15 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 1-2, 5, and 11-15 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.'' MPEP 2113 states that the “patentability of a product does not depend on its method of production.”. In the instant case, the structure of the claimed α-amylase mutant implied is the same whether the α-amylase mutant is obtained from recombinant engineering of a parent α-amylase mutant having at least 90% sequence identity to SEQ ID NO:2 and deletion of R178, G179, T180 and/or G181 or is obtained from any source (including wild type proteins), as long as the resulting product has the structural limitations recited in the claims: having a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 respectively, of SEQ ID NO:2. Therefore, the claims have been broadly interpreted as an α-amylase having a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 of SEQ ID NO:2, respectively, and any other amino acid difference compared to SEQ ID NO:2.
Yuuki discloses a Bacillus licheniformis α-amylase which has a Tyr residue and a Phe residue at the positions corresponding to F205 and H240 of SEQ ID NO:2, respectively, and other amino acid difference compared to SEQ ID NO:2 (abstract and Fig. 3 at page 1150 and see the sequence alignment below). Bacillus licheniformis α-amylase is a naturally occurring 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 an α-amylase, 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 claimed α-amylase mutant of claims 1-2 and 5 are not considered to have markedly different characteristics from what occurs in nature, Bacillus licheniformis α-amylase as discussed above, and is considered to be a law of nature exception. Regarding claims 11-15, there is no indication in the specification that placing the α-amylase in a generic cleaning agent composition results in the α-amylase having any characteristics (structural, functional, or otherwise) that are different from the naturally occurring Bacillus licheniformis α-amylase. Because there is no difference in characteristics (structural, functional, or otherwise) between the claimed α-amylase and the naturally occurring Bacillus licheniformis α-amylase, the claimed α-amylase mutant and a cleaning agent composition comprising said α-amylase are 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. Regarding claims 1-2 and 5, 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 protease is found naturally occurring in nature (Bacillus sp.). Regarding claims 11-15, the claims recite a generic cleaning agent composition and does not recite any components of the composition other than the α-amylase. The addition of an intended use does not impart any added benefit to the claimed α-amylase or integrate the claimed α-amylase 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.
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 1-2, 5, and 11-15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of copending Application No. 18/722,197 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of the instant application and the claims of the reference application are directed to α-amylase mutants of SEQ ID NO:2. The α-amylase of SEQ ID NO:2 of the instant application is identical to the α-amylase of SEQ ID NO:2 of the reference application.
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' MPEP 2113 states that the “patentability of a product does not depend on its method of production.”. In the instant case, the structure of the claimed α-amylase mutant implied is the same whether the α-amylase mutant is obtained from the parent α-amylase mutant having at least 90% sequence identity to SEQ ID NO:2 and deletion of R178, G179, T180 and/or G181 or is obtained from a parent α-amylase of SEQ ID NO:2, as long as the resulting product has the structural limitations recited in the claims: having a Phe residue and Gln residue at the positions corresponding to H240 and S241 respectively, of SEQ ID NO:2. Therefore, the claims have been broadly interpreted as an α-amylase having a Phe residue and Gln residue at the positions corresponding to H240 and S241 respectively, of SEQ ID NO:, respectively, and any other amino acid difference compared to SEQ ID NO:2.
Regarding claims 1-2, 5, and 11 of the instant application, claims 1-2 of the reference application recites a cleaning composition comprising an α-amylase mutant of SEQ ID NO:2, wherein the α-amylase mutant comprises a H240 + S241Q amino acid mutations. Therefore, claims 1-2, 5, and 11 of the instant application are anticipated by claims 1-2 of the reference application.
Regarding claim 12 of the instant application, claim 8 of the reference application recites that the cleaning composition is a clothing cleaning agent or a dishwashing agent. Therefore, claim 12 of the instant application is anticipated by claim 8 of the reference application.
Regarding claim 13 of the instant application, claim 9 of the reference application recites that the clothing cleaning agent composition or a dishwashing agent composition is a powder or a liquid. Therefore, claim 13 of the instant application is anticipated by claim 9 of the reference application.
Regarding claim 14 of the instant application, claim 10 of the reference application recites that the clothing cleaning agent composition or a dishwashing agent composition is used at a low temperature. Therefore, claim 14 of the instant application is anticipated by claim 10 of the reference application.
Regarding claim 15 of the instant application, claim 11 of the reference application recites that the clothing cleaning agent composition or a dishwashing agent composition is used at a temperature of from 5 to 40°C. Therefore, claim 15 of the instant application is anticipated by claim 11 of the reference application.
Therefore, the conflicting claims are not patentably distinct from each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Claims 1-2 and 4-15 are pending.
Claims 4 and 6-10 are withdrawn.
Claims 1-2, 5, and 11-15 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: 5:30 am - 3:30 pm.
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/YONG D PAK/Primary Examiner, Art Unit 1652
Sequence alignment between the α-amylase of SEQ ID NO:2 of the instant application (“Qy”) and the α-amylase of Yuuki (“Db”)
ALBSL
alpha-amylase (EC 3.2.1.1) precursor [validated] - Bacillus licheniformis
N;Alternate names: 1,4-alpha-D-glucan glucanohydrolase
C;Species: Bacillus licheniformis
C;Date: 30-Jun-1987 #sequence_revision 24-Apr-1998 #text_change 31-Dec-2004
C;Accession: A91997; B24549; A91796; A21663; I39774; I39772; A26151; S53788; A00844
R;Yuuki, T.; Nomura, T.; Tezuka, H.; Tsuboi, A.; Yamagata, H.; Tsukagoshi, N.; Udaka, S.
J. Biochem. 98, 1147-1156, 1985
A;Title: Complete nucleotide sequence of a gene coding for heat- and pH-stable alpha-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying alpha-amylases deduced from the DNA sequences.
A;Reference number: A91997; MUID:86111694; PMID:2418011
A;Accession: A91997
A;Molecule type: DNA
A;Residues: 1-162,'R',164-512 <YUU>
A;Cross-references: UNIPROT:P06278; UNIPROT:Q45283; UNIPARC:UPI0000125AAD; GB:X03236; NID:g39551; PIDN:CAA26981.1; PID:g39552
A;Experimental source: ATCC 27811
R;Gray, G.L.; Mainzer, S.E.; Rey, M.W.; Lamsa, M.H.; Kindle, K.L.; Carmona, C.; Requadt, C.
J. Bacteriol. 166, 635-643, 1986
A;Title: Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis.
A;Reference number: A91817; MUID:86195857; PMID:3009417
A;Accession: B24549
A;Molecule type: DNA
A;Residues: 1-338,'G',340-348,'S',350-512 <GRA>
A;Cross-references: UNIPARC:UPI000002D00E; GB:M13256; NID:g142510; PIDN:AAA22240.1; PID:g142511
A;Experimental source: NCIB 8061
R;Stephens, M.A.; Ortlepp, S.A.; Ollington, J.F.; McConnell, D.J.
J. Bacteriol. 158, 369-372, 1984
A;Title: Nucleotide sequence of the 5' region of the Bacillus licheniformis alpha-amylase gene: comparison with the Bacillus amyloliquefaciens gene.
A;Reference number: A91796; MUID:84185455; PMID:6609154
A;Accession: A91796
A;Molecule type: DNA
A;Residues: 1-104 <STE>
A;Cross-references: UNIPARC:UPI0000141EBA; GB:K01984; NID:g142432; PIDN:AAA22193.1; PID:g142433
R;Sibakov, M.; Palva, I.
Eur. J. Biochem. 145, 567-572, 1984
A;Title: Isolation and the 5'-end nucleotide sequence of Bacillus licheniformis alpha-amylase gene.
A;Reference number: A21663; MUID:85076654; PMID:6334606
A;Accession: A21663
A;Molecule type: DNA
A;Residues: 1-3,'H',5-12,'P',14-47,'R',49-61,'V',63,'D',65-67,'VA',70-71,'S',73-80,'D',82-104,118-121 <SIB>
A;Cross-references: UNIPARC:UPI0000172927
A;Experimental source: chromosomal DNA of ATCC 14580
A;Note: the authors translated the codon CGT for residue 48 as Gly and GAC for residue 64 as His
R;Laoide, B.M.; Chambliss, G.H.; McConnell, D.J.
J. Bacteriol. 171, 2435-2442, 1989
A;Title: Bacillus licheniformis alpha-amylase gene, amyL, is subject to promoter-independent catabolite repression in Bacillus subtilis.
A;Reference number: I39773; MUID:89213924; PMID:2540150
A;Accession: I39774
A;Status: translated from GB/EMBL/DDBJ
A;Molecule type: DNA
A;Residues: 1-29 <LAO>
A;Cross-references: UNIPARC:UPI000016E728; GB:M26412; NID:g341477; PIDN:AAA22237.1; PID:g516590
R;Jorgensen, P.L.; Hansen, C.K.; Poulsen, G.B.; Diderichsen, B.
Gene 96, 37-41, 1990
A;Title: In vivo genetic engineering: homologous recombination as a tool for plasmid construction.
A;Reference number: I39772; MUID:91092499; PMID:2265757
A;Accession: I39772
A;Status: translated from GB/EMBL/DDBJ
A;Molecule type: DNA
A;Residues: 1-32,'I' <JOR>
A;Cross-references: UNIPARC:UPI00000B938E; GB:M62637; NID:g142498; PIDN:AAA22232.1; PID:g142499
R;Kuhn, H.; Fietzek, P.P.; Lampen, J.O.
J. Bacteriol. 149, 372-373, 1982
A;Title: N-terminal amino acid sequence of Bacillus licheniformis alpha-amylase: comparison with Bacillus amyloliquefaciens and Bacillus subtilis enzymes.
A;Reference number: A26151; MUID:82098050; PMID:6172418
A;Accession: A26151
A;Molecule type: protein
A;Residues: 30-37,'E',39-41,'X',43-47 <KUH>
A;Cross-references: UNIPARC:UPI0000172928
R;Machius, M.; Wiegand, G.; Huber, R.
J. Mol. Biol. 246, 545-559, 1995
A;Title: Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution.
A;Reference number: S53788; MUID:95182462; PMID:7877175
A;Accession: S53788
A;Molecule type: protein
A;Residues: 'D',220-227 <MAC>
A;Cross-references: UNIPARC:UPI0000172929
A;Note: sequence represents amino end of an internal fragment created by a single enzymatic cleavage by a protease trace contaminant during purification
R;Machius, M.; Wiegand, G.; Huber, R.
submitted to the Brookhaven Protein Data Bank, July 1995
A;Reference number: A65206; PDB:1BPL
A;Contents: annotation; X-ray crystallography, 2.2 angstroms, residues 32-210;222-511
A;Note: these structural studies suggest 163 is Leu rather than Arg
R;Song, H.K.; Hwang, K.Y.; Chang, C.; Suh, S.W.
submitted to the Brookhaven Protein Data Bank, October 1996
A;Reference number: A66860; PDB:1VJS
A;Contents: annotation; X-ray crystallography, 1.7 angstroms, residues 32-210;222-511
C;Genetics:
A;Gene: amyL
C;Function:
A;Description: catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic bonds
A;Pathway: glycogen/starch degradation
C;Superfamily: alpha-amylase, thermostable type; alpha-amylase core homology
C;Keywords: extracellular protein; glycosidase; heat-stable protein; hydrolase; polysaccharide degradation
F;1-29/Domain: signal sequence #status predicted <SIG>
F;30-512/Product: alpha-amylase #status experimental <MAT>
F;227-360/Domain: alpha-amylase core homology <AMY>
F;133,229,264/Binding site: calcium (Asn, Asp, His) #status experimental
F;260,290,357/Active site: Asp, Glu, Asp #status experimental
Query Match 76.2%; Score 2041; Length 512;
Best Local Similarity 73.7%;
Matches 355; Conservative 57; Mismatches 68; Indels 2; Gaps 1;
Qy 4 NGTMMQYFEWYVPNDGQHWNRLRNDAAYLKSIGVSAIWTPPAYKGTSQNDVGYGAYDLYD 63
|||:|||||||:||||||| ||:||:||| |::|:| ||||||||| |||||||||||
Db 33 NGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWIPPAYKGTSQADVGYGAYDLYD 92
Qy 64 LGEFNQKGTIRTKYGTKAELKSAVSTLKSNGIQVYGDVVMNHKGGADYTENVTAVEVNPS 123
||||:||||:||||||| ||:||: :| | | ||||||:||||||| ||:||||||:|:
Db 93 LGEFHQKGTVRTKYGTKGELQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDPA 152
Qy 124 NRNQETSDEYTIQAWTGFNFPGRGTTHSPFKWQWYHFDGTDWDQSRNASRIFKFRGTGKA 183
:||: | |: |:||| |:|||||:|:| ||| ||||||||||:|| :||:||: |||
Db 153 DRNRVISGEHLIKAWTHFHFPGRGSTYSDFKWHWYHFDGTDWDESRKLNRIYKFQ--GKA 210
Qy 184 WDWEVSSENGNYDYLMYADLDFDHPDVRNEMKNWGVWYANEVGLDGFRLDAVKHIKHSYL 243
||||||:||||||||||||:|:||||| |:| || |||||: ||||||||||||| |:|
Db 211 WDWEVSNENGNYDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSFL 270
Qy 244 GDWVNHVRTKTGKEMFTVAEYWQNDVNAINNYLAKVNYNHSVFDAPLHYNFHYASQSGGN 303
||||||| ||||||||||||||||: |: ||| | |:|||||| |||| || || ||
Db 271 RDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFNHSVFDVPLHYQFHAASTQGGG 330
Qy 304 YDMRNLLNGTVVAAHPTKAVTLVENHDSQPGQSLESVVQPWFKPLAYAFILTRAEGYPSI 363
|||| ||| |||: || |||| |:|||:|||||||| || ||||||||||||| ||| :
Db 331 YDMRKLLNSTVVSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQV 390
Qy 364 FYGDMYGTKGNSSYEIPALKTKIEPLLKARKDYAYGTQHNYMDHWDVIGWTREGDSTKEK 423
||||||||||:| |||||| ||||:||||| |||| ||:| || |::||||||||:
Db 391 FYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQHDYFDHHDIVGWTREGDSSVAN 450
Qy 424 SGLATLVTDGAGGSKWMYVGKQNAGEVWYDITGNRTDKITINTDGWGNFQVNGGSVSVYV 483
|||| |:||| ||:| ||||:||||| |:||||||:: : ||::||| | |||||||:||
Db 451 SGLAALITDGPGGAKRMYVGRQNAGETWHDITGNRSEPVVINSEGWGEFHVNGGSVSIYV 510
Qy 484 QQ 485
|:
Db 511 QR 512