DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.
Remarks
The amendments and remarks filed on 05/07/2026 have been entered and considered. The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. The rejections and/or objections presented herein are the only rejections and/or objections currently outstanding. Any previously presented objections or rejections that are not presented in this Office Action are withdrawn.
Claims 27-31 and 37-42 are pending.
Claims 27-29 are amended.
Claims 1-26 and 32-36 are canceled.
Claims 41-42 are withdrawn.
Claims 27-31 and 37-40 have been examined on the merits.
Priority
This application, U.S. Application number 17/778452, is a national stage entry of International Application Number PCT/EP2020/087222, filed on 12/18/2020, which claims for foreign priority under 35 U.S.C. 119(a)-(d) to foreign application EP19218813.4 filed on 12/20/2019.
Rejections - Withdrawn
The rejection of Claims 27, 32, and 40 under 35 U.S.C. 103 is withdrawn
due to the amendment or cancellation of the claims filed on 05/07/2026.
The rejection of Claims 27, 33, and 40 under 35 U.S.C. 103 over Groot in view of Niyonzima et al. and Gjermansen is withdrawn due to the amendment or cancellation of the claims as well as the removal of Pisa et al. (Uniport No. A0A1G8GTV3) from the UniportKB database, as Applicant pointed out in the 05/07/2026 response (pages 8-9).
The rejection of Claims 27, 34, and 40 under 35 U.S.C. 103 over Pisa et al. in view of Niyonzima et al. and Gjermansen is withdrawn due to the amendment or cancellation of the claims as well as the removal of Pisa et al. (Uniport No. A0A433R972) from the UniportKB database, as Applicant pointed out in the 05/07/2026 response (pages 9-10).
Specification
The specification is objected to because two distinct sets of paragraphs 1-40 are recited in the specification. See PGPub US 2022/0411773 of the instant application: the first set of paragraphs 1-40 are disclosed in pages 1-3, and another distinct set of paragraphs 1-40 are recited in pages 30-33 (throughout [0456] – [0529]) of the PGPub throughout paragraphs. For example, see [0498]: “A fusion polypeptide comprising the polypeptide of any one of paragraphs 1-16”; [0500]: “a core comprising the polypeptide of any one of paragraphs 1-16”; and [0527]: “Use according to any of paragraphs 37 to 40 for preventing, reducing or removing … soil during a wash cycle” (Emphasis is added). None of the first set of paragraphs 1-40 in pages 1-3 discloses any subject matter that matches with the second set of paragraphs 1-40 referred by the disclosure of pages 30-33.
Applicant is required to make Appropriate correction without introducing new matter in response to this Office action. This objection is maintained.
Claim Rejections - 35 USC § 101
Claims 27-31 and 37-40 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (a natural phenomenon) without significantly more, as evidenced by De et al. [RSC Adv., 2015, Vol. 5, pages 1-27 (original page number is 65757-65767), of record], and Donio et al. (SpringerPlus 2013, 2:149, pages 1-10, of record).
The base claim 27 is directed to a composition which is one of four categories of patent eligible subject matter (Step 1: Yes).
The base claim 27 is directed to a composition comprising a surfactant and a polypeptide having proteolytic activity. The claimed surfactant and polypeptide are all naturally occurring substances produced by naturally occurring microbes, as evidenced by De et al. (abstract, page 11) and Donio et al. (title, abstract), who teach respectively that natural surfactants/biosurfactants are produced by various microbes including bacteria, yeast, and fungi, and that biosurfactant is produced by a naturally occurring halophilic bacterium; and as evidenced by the specification of the instant application, the claimed polypeptides are obtained from microorganisms of the nature (e.g. in soil or water) (see page 19, lines 12-16).
It is noted that the claim 27 recites a broad limitation of 0.01 – 1000 ppm to define a concentration of the polypeptide, but the instant claims do not recite any limitation to define concentrations or amounts of surfactant in the claimed composition, thus the surfactant can be at any amounts. There is no indication in the specification that any amounts of surfactant combined with a polypeptide as low as 0.01 ppm in the claimed composition has any characteristics (structural or functional) that are different from their naturally occurring counterparts in the natural state. Accordingly, the claim is directed to “products of nature” judicial exception (Step 2A, Prong 1: Yes).
The judicial exception in the claim 27 is not integrated into a practical application because the claim is directed to a product, not a method of use (Step 2A: Prong 2: No).
The claim 27 further recites the limitation to define the composition in the form of liquid, gel, powder, granulate, paste or spray. However, this limitation is at a high level of genericity and the claim appears to recite all the possible forms of the composition (i.e. liquid, solid, semi-liquid, and semi-solid). As such, the claim does not include additional elements that are sufficient to amount to significantly more than the judicial exception (Step 2B: No).
Dependent claims 28-31 and 38-39 further recite the limitations to limit the sequence identity of the clamed polypeptide to the SEQ ID Nos. 21, 3, 6, 9, 12, and/or 18, or describe the sequence of the clamed polypeptide. As indicated above, the specification discloses that the claimed polypeptides are obtained from microorganisms of the nature (e.g. soil, water). There is no indication in the specification that the polypeptide having proteolytic activity in the claimed composition has any characteristics (structural or functional) that are different from their naturally occurring counterparts. Therefore, the limitations recited in the claims are still directed to the “products of nature” judicial exception of the claim 27.
Dependent claim 37 further limits the clamed polypeptide to be a fragment of the polypeptide having the amino acid sequence of SEQ ID Nos. 21, 3, 6, 9, 12, or 18. It is noted that naturally occurring polypeptides having proteolytic activity are present in the form of fragments, because they are generated through naturally occurring events of protein degradation. There is no indication in the specification that the claimed polypeptide in the form of fragment has any characteristics (structural or functional) that are different from their naturally occurring counterparts. Therefore, the limitation recited in the claim is still directed to the “products of nature” judicial exception of the claim 27.
Dependent claim 40 further recites the limitation of “a builder”. However, this limitation is at a high level of genericity because the claim does not define any specific structure of the builder. The specification (page 31, lines 13-17) discloses the builder can be citric acid, citrates, carbonates, bicarbonates, zeolite, and/or silicates, which are all naturally occurring substances. Therefore, the limitation recited in the claim is still directed to the “products of nature” judicial exception of the claim 27.
Therefore, Claims 27-31 and 37-40 are deemed to be patent ineligible.
Claim Rejections - 35 USC § 112, First Paragraph
Claims 27-31 and 40 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(s), at the time the application was filed, had possession of the claimed invention.
The claims 27, 31 and 40 are directed to a composition comprising a polypeptide having proteolytic activity, selected from the group consisting of polypeptides having sequence identities of at least 96%, 95%, 95%, 95%, 95%, and 95%, respectively, to SEQ ID NO: 21, 3, 6, 9, 12, 15 and 18. It is noted that the amino acid sequence lengths of SEQ ID NO: 21, 3, 6, 9, 12, and 18 are in a range from 346 amino acids to 451 amino acids. The claimed at least 95% or 96% sequence identity to SEQ ID NO. 21 (375 AAs), 3 (451 AAs), 6 (349 AAs), 9 (344 AAs), 12 (354 AAs), or 18 (370 AAs) would allow 15 -19 amino acids to be mutated throughout the entire sequence of SEQ ID NO: 21, 3, 6, 9, 12, 15 or 18 for arriving at the claimed polypeptide. The claims 28-30 further limit: the sequence identity to SEQ ID NO: 21 to a level of at least 97%, 98%, or 99%; the sequence identity to SEQ ID NO: 6 to a level of at least 96% or 98% to SEQ ID NO: 6, or the sequence identity to SEQ ID NO: 3 to a level of at least 97%. These further limitations still allow 4-14 amino acids to be mutated throughout the entire sequence of SEQ ID NO: 21, 6, or 3 for arriving at the claimed polypeptide. Overall, the amino acid number allowed to be mutated in the polypeptide sequences of SEQ ID NO: 21, 3, 6, 9, 12, or 18 is ranged from 4 amino acids to 19 amino acids, for arriving at the claimed polypeptides.
Examiner notes that the instant claims do not define any specific positions where the mutations/variations occur; and the claims do not define any specific types of mutations occurring throughout the sequences of SEQ ID NO: 21, 3, 6, 9, 12, or 18. As such, the claimed polypeptide may have up to 19 mutations, including any different substitutions, deletions, insertions, or a combination thereof, at any of positions throughout the 344-452 amino acid sequences of SEQ ID NO: 21, 3, 6, 9, 12, and 18. As known to one of ordinary skill in the art, there are 20 different amino acids, which may be used to mutate/change amino acids at each of 344 - 451 positions throughout SEQ ID NO: 21, 3, 6, 9, 12, and 18. Accordingly, the claimed polypeptide may be derived from a polypeptide of SEQ ID NO: 21, 3, 6, 9, 12, or 18 by any types of up to 19 mutations/variations with any different combination of substitution, deletion, and/or insertion of any amino acids at any of 344-451positions throughout the entire sequences of SEQ ID NO: 21, 3, 6, 9, 12, and 18. Consequently, the scope of the polypeptides that meet the claimed sequence identities to SEQ ID NO: 21, 3, 6, 9, 12, or 18 encompasses an extremely large number of different variants/mutants derived from the proteolytic polypeptide having the sequence set forth in SEQ ID NO: 21, 3, 6, 9, 12, or 18.
The specification provides no information about the structural - proteolytically functional relationship for the polypeptides having the sequence of SEQ ID NOs: 21, 3, 6, 9, 12, or 18 in a range of 346 AAs - 451 AAs. Given the claims do not recite actual structural limitations, an extremely large numbers of variants/mutants of the polypeptide of SEQ ID NOs: 21, 3, 6, 9, 12, and18 must be constructed and screened for identifying those polypeptides having proteolytic activity, encompassed by the scope of the claims. An effective high-throughput process for mutating, cloning and expressing polypeptides as well as screening mutants would be necessary in order to identify mutants/variants having a proteolytic activity among an extremely large pool of polypeptide mutants/variants of SEQ ID NOs: 21, 3, 6, 9, 12, or 18. However, the specification (page 17) only provides general information about mutagenesis of DNA for making amino acid substitution, deletion, and/or insertion mutations, and screening mutants for detecting activity of cloned mutagenized polypeptides. There is no disclosure in the specification about a completely automated high-throughput process for effectively mutagenizing coding-genes, cloning and expressing mutated polypeptides as well as effectively screening mutants for determining their proteolytic activities, thus identifying those mutants having amino acid substitutions, deletions and/or insertions which result in a desired proteolytic activity, from an extremely large pool of mutated polypeptides having up to 19 amino acid mutations throughout the 346 AA - 451 AA polypeptides of SEQ ID NOs: 21, 3, 6, 9, 12, and 18.
In order for the written description provision of 35 USC 112, first paragraph to be satisfied, Applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the 'written description' inquiry, whatever is now claimed. For example, MPEP 2163 states in part,
An adequate written description of a chemical invention also requires a precise definition, such as by structure, formula, chemical name, or physical properties, and not merely a wish or plan for obtaining the chemical invention claimed. See, e.g., Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 927, 69 USPQ2d 1886, 1894-95 (Fed. Cir. 2004) (The patent at issue claimed a method of selectively inhibiting PGHS-2 activity by administering a non-steroidal compound that selectively inhibits activity of the PGHS-2 gene product, however the patent did not disclose any compounds that can be used in the claimed methods. While there was a description of assays for screening compounds to identify those that inhibit the expression or activity of the PGHS-2 gene product, there was no disclosure of which peptides, polynucleotides, and small organic molecules selectively inhibit PGHS-2. The court held that “without such disclosure, the claimed methods cannot be said to have been described.”).
Without additional information, the skilled artisan cannot envision which specific substitutions, deletions and/or insertions of the polypeptide of SEQ ID NO: 21, 3, 6, 9, 12, or 18 would result in the claimed polypeptide having the claimed proteolytic activity.
Therefore, the full breadth of a polypeptide having proteolytic activity and at least 95%, 96%, 97%, 98%, or 99% sequence identity to SEQ ID NO: 21, 3, 6, 9, 12, or 18, encompassed by the claims, do not meet the written description provision of 35 USC 112, first paragraph.
Claim Rejections - 35 USC § 112(d), or 112, Fourth Paragraph
Claim 31 is 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
Claim 31 defines that the polypeptide has at least 96% sequence identity to SEQ ID NO: 21, but it does not recite any limitation to require the polypeptide comprised in the composition is the polypeptide having at least 96% identity to SEQ ID NO: 21. Given that the limitation of having at least 96% identity to SEQ ID NO: 21 is present in the base claim 1, Claim 31 fails to further limit the structures of the composition of Claim 1.
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
Claims 27, 31, and 40 are rejected under 35 U.S.C. 103 as being unpatentable over Lu-3 et al. (Uniport No. A0A368U1V0, 2018, pages 1-2, of record) in view of Niyonzima et al. (Preparative Biochemistry & Biotechnology, 2014, Volume 45, Issue 3, pages 233-258, cited in IDS) and Gjermansen (WO2017064253, 2017, cited in IDS).
Lu-3 et al. teach a serine protease polypeptide in Halomonas montanilacus bacterium isolated from Lake Pengyan at Tibetan, which has sequence identity of 95.3% query match and 94.9% best local similarity to the sequence of SEQ ID NO: 21 in claims 27 and 31. See pages 1-2 for description and sequence of the protease, and also the sequence alignment between the polypeptide of SEQ ID NO:21 and the proteinase of Lu-3 et al. attached below.
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The protease polypeptide taught by Lu-3 et al. differs from the claimed polypeptide composition in that Lu-3 et al. do not teach that the protease polypeptide is comprised in a composition along with a surfactant.
Niyonzima et al. teach that proteases are important commercial enzymes used in detergent industries, as key components in detergent formulations; and the search for detergent-compatible proteases with better properties is a continuous exercise (abstract/lines 1-5). Niyonzima et al. also teach proteases to be used in detergent preparations must have stability in the presence of surfactants and have high activity at alkaline pH and in a broad temperature range (page 240/last para). Niyonzima et al. further teach a process of screening for detergent-compatible proteases, which includes culturing protease-producing microbes under optimized culture conditions, purifying proteases from microbial cultures, and examining effects of factors such as pH, temperatures, and surfactants on activity and stability of the proteases (page 241/paras 1-2, page 246/last para – page 247/para 4).
Gjermansen teaches the use of proteases or polypeptides having protease activity in detergents for cleaning such as dish wash and laundry, and the most commonly used proteases are serine proteases (page 1: lines 12-13 and 19-21). Gjermansen also teaches polynucleotides encoding the polypeptides, expression vectors or nucleic acid constructs for cloning the polynucleotides, and recombinant host cells comprising the polynucleotides in the constructs/vectors for expressing the polypeptides, as well as methods of producing the polypeptides in the host cells (pages: 1/lines 10-12, 2/lines 18-20, 15/lines 26-30, 19/lines 31-34, 22/lines 7-10, claims 14-16); and the techniques used for isolating and cloning polynucleotides for producing polypeptides having proteolytic activity are all known in the art (page 15, lines 3-10). Gjermansen further teaches that detergent compositions comprise proteases and other suitable cleaning/detergent relevant ingredients including surfactants and builders (pages: 26/lines 27-29, 29/lines 15-23, 31/lines 1-11, 48/lines 17-19).
It would have been obvious to one of ordinary skill in the art to combine the serine protease polypeptide taught by Lu-3 et al. with a surfactant for evaluating stability of the protease polypeptide in the presence of surfactant and determining whether the protease polypeptide is a detergent-compatible protease suitable for detergent preparations, thus arriving at a composition comprising the protease and surfactant. This is because Niyonzima et al. teach that proteases are important commercial enzymes and a key component in detergent formulations; the search for detergent-compatible proteases with better properties is a continuous exercise; and proteases to be used in detergent preparations must be tested for ensuring their stability in the presence of surfactants. In addition, Gjermansen teaches that serine proteases are the most commonly used proteases in detergent compositions. Thus, one of ordinary skill in the art would have been motivated to try the serine protease of Lu-3 et al. for identifying a detergent-compatible protease suitable for detergent preparations. Furthermore, the techniques for purifying the protease polypeptide of Lu-3 et al. from bacterial cells as well as cloning and expressing the protease in a host cell are well established in the art, as supported by Niyonzima et al. and Gjermansen. As such, the protease polypeptide of Lu-3 et al. is readily available for being combined with the surfactant for a detergent-compatible protease assay, which provides a reasonable expectation of success at combining the protease of Lu-3 et al. with a surfactant.
Regarding the limitation “0.01 to 1000 ppm” recited in the claim 27, this is an extremely broad concentration range for the claimed proteolytic polypeptide. Gjermansen further teaches that the protease composition of his invention is employed at a concentration of from about 100 ppm, preferably 500 ppm to about 15,000 ppm in a solution (page 49/lines 5-6), which overlaps the claimed range. Given the concentration of Gjermansen is readily adjustable for achieving a better washing performance, the claimed concentration range would have been obvious over Gjermansen in the absence of any showing of unexpected results or criticality..
Regarding the limitation about the sequence identity to SEQ ID NO: 21 in the claims 27 and 31, Lu-3 et al. do not teach the protease has at least 96% sequence identity to SEQ ID NO: 21. However, the sequence identity between the polypeptide of SEQ ID NO: 21 and the proteinase of Lu-3 et al. is close to a level of 96% in view of that there are 95.3% query match and 94.9% best local similarity between the two sequences. Furthermore, the proteinase of Lu-3 et al. has a total of 356 amino acids matched to the 375 AAs-long polypeptide of SEQ ID NO: 21; and among the 19 mismatched amino acids there are 9 conserved mismatches, which are indicated as “:” in the sequence alignment attached above. The conserved mismatches include those between similar amino acids, such as between glutamic acid (E) and glutamine (Q) or aspartic acid (D), between isoleucine (I) and valine (V), as well as between arginine (R) and lysine (K), Specifically, E:D (85), E:Q (135), D:E (153), V:I (223), E:D (226), D:E (276), and R:K (355) (Note: numbers in the parentheses represent locations of 7 mismatched amino acids at the “Qy” sequence, i.e. sequence of SEQ ID NO: 21, in the sequence alignment attached above). As such, It would have been obvious to try replacing the amino acid (e.g. D, Q, E, or K) at each of these mismatched locations with its corresponding similar amino acid (i.e. E, D, or R) in the proteinase of Lu-3 et al. for further evaluating protease stability and identifying proteases more suitable for detergent preparations, thus arriving at the claimed protease polypeptide having at least 96% identity to SEQ ID NO: 21 [Note: (356+7)/375= 96.8% identity], because these amino acids are highly similar to each other and the amino acid replacement facilitates identification of proteases more suitable for detergent preparations. See MPEP 2143 I.E., the rationale “obvious to try” supports a conclusion of obviousness when there is a finite number of identified and predictable solutions in the prior art, and choosing from such a finite number of identified and predictable solutions would have a reasonable expectation of success. Thus, the claims would have been obvious over the combined teachings of Lu-3 et al., Niyonzima et al., and Gjermansen.
Regarding Claim 40, it is a common practice in the art to add builders along with surfactants as cleaning/detergent relevant ingredients to the protease-containing compositions, as supported by Gjermansen. As such, it would have been obvious to further include a builder in the composition containing the protease polypeptide and surfactant suggested by the cite prior art for further evaluating stability of the protease polypeptide and determining whether the protease polypeptide is a detergent-compatible protease suitable for detergent preparations.
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
Response to Arguments
Applicant's arguments about the objection to the specification in the response filed on 05/07/2026 (page 5) have been fully considered, but they are not persuasive. As indicated above, two distinct sets of paragraphs 1-40 are recited in the specification, respectively in pages 1-3 and in pages 30-33. None of disclosure in the first set of paragraphs 1-40 in pages 1-3 matches to that of the second set of paragraphs 1-40 in pages 30-33. As such, the skilled artisan would not consider the paragraphs 1-40 in pages 30-33 refer to the paragraphs 1-40 disclosed in pages 1-3. Therefore, this objection is maintained.
Applicant's arguments about the 101 rejection in the 05/07/2026 response (pages 5-6) have been fully considered but they are not persuasive. In response to Applicant’s arguments about no naturally occurring counterpart to the claimed composition, the surfactant and polypeptide/protease in the claimed composition can co-exist together in the nature because they are both produced by naturally occurring microorganisms, as indicated above. With regard to the limitation about the specific form of the claimed composition recited in the claim 27, this limitation is at a high level of genericity, and the form of the liquid, gel, powder, granulate, paste or spray appears to include all the possible forms of the composition (liquid, solid, semi-liquid, and semi-solid). In addition, naturally occurring counterpart can be present in the form of liquid, solid, semi-liquid, and semi-solid. As such, the claim does not include additional elements that are sufficient to amount to significantly more than the judicial exception, as indicated above. With regard to Applicant’s further arguments based on good wash performance and stain removal of the claimed composition in page 6 of the response, these arguments are based on features not recited in the claims because there is no limitation in the claims to define wash performance and stain removal of the claimed composition. In addition, naturally occurring proteinases has the property of digesting proteins, which could lead to removing a protein stain from a substance. There is no factual evidence to support that stain removal is a feature that distinguishes the claimed composition from its naturally occurring counterpart. With regard to Applicant’s arguments based on the Claim 2/Example 2 of the USPTO’s Guidance and a defined concentration for the polypeptide in pages 5-6 of the response, Examiner reminds Applicant that the instant claims only recites an extremely broad concentration range (0.01 to 1000 ppm) for the polypeptide, but do not recite any limitations to define a concentration of the surfactant in the claimed composition. There is no factual evidence in the specification to support a composition comprising any amount of surfactant combined with a protease polypeptide as low as 0.01 ppm can achieve any significantly different characteristics, such as good wash performance, compared to its naturally occurring counterparts. It is further noted that the subject matter eligibility of Claim 2/Example 2 in the USPTO’s Guidance is not appliable to the instant case, because there is no factual evidence to support the composition encompassed by the instant claims has any property that is markedly different from its naturally occurring counterparts. Therefore, the amended claims are patent ineligible.
Applicant’s arguments about the rejection of claims 27-31 and 40 under 35 U.S.C. 112(a) as failing to comply with the written description requirement in the 05/07/2026 response (pages 6-7) have been fully considered, but they are not persuasive.
In response to Applicant’s arguments in pages 6-7, the Examiner reminds Applicant that the specification of the instant application does not provide any precise definition, such as by structure of the claimed subject matter. The claims 27-31 and 40 only define a level of sequence identity to a known amino acid sequence, but do not define any specific structure of a polypeptide, such as specific amino acids at specific location of the polypeptide. Because the mutations can be any substitution, deletion, and/or insertion of any amino acids and can occur at any locations throughout the entire polypeptide, the claimed polypeptide is widely open to have any structures. Furthermore, the claimed 95% sequence identity is not predictive of protein function (i.e. proteolytic activity), because there is no factual evidence to support that any polypeptide having 95% sequence identity certainly has a proteolytic activity. As indicated above, it is necessary for the specification to provide a structural-functional correlation for proteases of SEQ ID NOs: 21, 3, 6, 9, 12, and 18, so as to show which specific locations, regions, and amino acids throughout their entire amino acid sequence are essential for acquiring the claimed proteolytic activities. However, the specification of the instant application does not provide any information about the structural - proteolytically functional relationship for the polypeptide of SEQ ID NOs: 21, 3, 6, 9, 12, or 18. With regard to Applicant’s arguments based on a working example shows proteinases are useful in detergents (in page 7), it is noted that the proteinases used in the working example are proteinases having 100% sequence identity to SEQ ID NO: 21, 12, 6, or 18, not the claimed polypeptide mutants having less than 100% identity. As such, the disclosure of the example does not provide any written description for claimed polypeptide mutants sharing 95% or more identity to SEQ ID NO: 21, 3, 6, 9, 12, or 18.
Applicant’s arguments about the rejections under 35 U.S.C. 103 over Lu-2 et al., Groot, or Pisa et al. in view of Niyonzima and Gjermansen in the 05/07/2026 response (pages 7-10) have been fully considered, but they are moot, because the rejections have been withdrawn as indicated above.
Regarding the rejection of claims 27, 31, and 40 under 35 U.S.C. 103 over Lu-3 et al. in view of Niyonzima and Gjermansen, Applicant simply asserted in the 05/07/2026 response (page 8) that the cited prior art does not teach/suggest the claimed invention. But Applicant failed to provide any specific arguments or reasons to traverse the rejection. Overall, the conclusion of the obviousness of the claims 27, 31, and 40 has been established for all the reasons indicated above (see pages 11-15 for details).
Conclusion
No claim is in condition for allowance.
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Any inquiry concerning this communication or earlier communications from the examiner should be directed to Qing Xu, Ph.D., whose telephone number is (571) 272-3076. The examiner can normally be reached on Monday-Friday from 9:30 AM to 5:00 PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao, can be reached at (571) 272-0939. Any inquiry of a general nature or relating to the status of this application or proceeding should be directed to the receptionist whose telephone number is (571) 272-1600.
/Qing Xu/
Patent Examiner
Art Unit 1656
Prosecution Insights