Prosecution Insights
Last updated: April 19, 2026
Application No. 18/251,153

METHOD FOR PRODUCING PLANT PROTEIN-PROCESSED PRODUCT HAVING IMPROVED FOOD TEXTURE

Final Rejection §102§103
Filed
Apr 28, 2023
Examiner
HAWKINS, AMANDA SALATA
Art Unit
1793
Tech Center
1700 — Chemical & Materials Engineering
Assignee
Amano Enzyme Manufacturing (China) Ltd.
OA Round
2 (Final)
0%
Grant Probability
At Risk
3-4
OA Rounds
3y 2m
To Grant
0%
With Interview

Examiner Intelligence

Grants only 0% of cases
0%
Career Allow Rate
0 granted / 13 resolved
-65.0% vs TC avg
Minimal +0% lift
Without
With
+0.0%
Interview Lift
resolved cases with interview
Typical timeline
3y 2m
Avg Prosecution
67 currently pending
Career history
80
Total Applications
across all art units

Statute-Specific Performance

§101
2.7%
-37.3% vs TC avg
§103
46.6%
+6.6% vs TC avg
§102
14.3%
-25.7% vs TC avg
§112
29.1%
-10.9% vs TC avg
Black line = Tech Center average estimate • Based on career data from 13 resolved cases

Office Action

§102 §103
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 . Status of the Application Receipt of the Response and Amendment after Non-Final Office Action filed December 19, 2025 is acknowledged. The status of the claims upon entry of the present amendments stands as follows: Pending claims: 1-7, 10 Withdrawn claims: None Previously canceled claims: 8, 9 Newly canceled claims: None Amended claims: 1 New claims: 10 Claims currently under consideration: 1-7, 10 Currently rejected claims: 1-7, 10 Allowed claims: None Claim Rejections - 35 USC § 102 The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. Claims 1 and 6 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Yamamoto (JP 2011206048A) as evidenced by Motoki (Motoki, Masao, et al. “Glutamine-specific Deamidation of αs1-Casein by Transglutaminase”, Agriculture and Biological Chemistry, Vol. 50(12), p. 3025-3030, published 1986 [accessed online March 17, 2026]). Regarding claim 1, Yamamoto teaches a method of processing foods such as rice (i.e., a plant) using transglutaminase (a known protein deamidase that exhibits an action of decomposing an amide group-containing side chain of a protein without cleaving peptide bonds and crosslinking the protein) and α-glucosidase ([0001]), where α-glucosidase is also known as transglucosidase ([0003]). Although Yukio does not explicitly teach that the rice being treated has protein, it is known in the art that rice naturally contains protein (i.e., a plant protein). Evidence to support that transglutaminase is a protein deamidase is provided by the instant specification. The instant specification says that the protein deamidase can be glutaminase ([0058]), where transglutaminase is understood in the art to be a type of glutaminase. Evidence to support that rice is a plant protein material is also provided by the instant specification. The instant specification states that a plant protein raw material can include plants such as rice ([0014]). Evidence to support that transglutaminase exhibits an action of decomposing an amide group-containing side chain of a protein without cleaving peptide bonds and crosslinking the protein is provided by Motoki. Motoki discloses that deamidated product was not crosslinked even after transglutaminase treatment (p. 3027, col. 1, ¶ 1), and that transglutaminase deamidation was specific to the side chains, and that there was no degradation (i.e., no cleaving) of peptide bonds (p. 3029, col 1, ¶ 2- col 2, ¶ 1). Regarding claim 6, Yamamoto teaches all elements of claim 1 as described above. Yamamoto also teaches that the rice is prepared by adding an amount of water that is 1.5 times the amount of raw rice (i.e., the plant protein raw material; [0038]), which falls within the claimed range of “0.5 parts by weight or more of water per 1 part by weight of plant protein raw material”. Evidence to support that rice is a plant protein material is provided by the instant specification. The instant specification states that a plant protein raw material can include plants such as rice ([0014]). Claim 3 and 4 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Yamamoto (JP 2011206048A) as evidenced by Motoki (Motoki, Masao, et al. “Glutamine-specific Deamidation of αs1-Casein by Transglutaminase”, Agriculture and Biological Chemistry, Vol. 50(12), p. 3025-3030, published 1986 [accessed online March 17, 2026]) and Nutrifox (“Rice, white, short-grain, enriched, uncooked”, Nutrifox, version from May 22, 2022 [accessed online September 8, 2025] https://web.archive.org/web/20220522073956/https://nutrifox.com/nutrition/rice-white-short-grain-enriched-uncooked) Regarding claim 3, Yamamoto teaches all elements of claim 1 as described above. Although Yamamoto does not explicitly teach that protein deamidase is used in an amount of 0.05 U or more per 1 gram of a plant protein, Yamamoto does teach that transglutaminase (i.e., protein deamidase) is present in an amount of 0.05 to 12 U per 1 gram of raw rice ([0013], (9)). Uncooked white rice is known in the art to have 13g protein per 200 grams of rice. Therefore, the process of Yamamoto uses transglutaminase in an amount of 0.769 to 184 U per 1 gram of rice protein, which falls within the claimed range of “0.05 U or more”. Evidence to support that uncooked white rice has 13g protein per 200 grams of rice is provided by Nutrifox (p. 1, serving size of 200 g; p. 2, row 3). Regarding claim 4, Yamamoto teaches all elements of claim 1 as described above. Although Yamamoto does not explicitly teach that transglucosidase is used in an amount of 5 U or more per 1 g of plant protein, Yamamoto does teach that alpha-glucosidase (i.e., transglucosidase) is used in an amount of 15 to 150,000 U per 1 gram of raw rice ([0013], (9)). Uncooked white rice is known in the art to have 13g protein per 200 grams of rice. Therefore, the process of Yamamoto uses transglucosidase in an amount of 230 to 2,300,000 U of transglucosidase per gram of protein, which falls within the claimed range of “5 U or more”. Evidence to support that uncooked white rice has 13g protein per 200 grams of rice is provided by Nutrifox (p. 1, serving size of 200 g; p. 2, row 3). Claim Rejections - 35 USC § 103 The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. Claims 2, 7, and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Yamamoto (JP 2011206048A) as evidenced by Motoki (Motoki, Masao, et al. “Glutamine-specific Deamidation of αs1-Casein by Transglutaminase”, Agriculture and Biological Chemistry, Vol. 50(12), p. 3025-3030, published 1986 [accessed online March 17, 2026]) in view of Triantafyllou (US 2015/0351432 A1). Regarding claim 2, Yamamoto teaches all elements of claim 1 as described above. Yamamoto does not teach wherein the plant protein food and drink is oat milk. However, in the same field of endeavor, Triantafyllou teaches a process for preparing a liquid oat drink by treating it with protein deamidase (Abstract), where oat drinks are also known as oat milk ([0002]). It would have been obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to modify the method taught by Yamamoto with the use of oat milk as the based that is being treated with both protein deamidase and transglucosidase. It would have been obvious because one of ordinary skill in the art could have combined the method of Yamamoto using both protein deamidase and transglucosidase with the method of treating oat milk using protein deamidase and yield the predictable result of a stable oat milk composition. The claim would have been obvious because all 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 function, and the combination yielded nothing more than predictable results to one of ordinary skill in the art, see MPEP §2143(A). Regarding claim 7, Yamamoto teaches all elements of claim 1 as described above. Yamamoto does not teach wherein an α-amylase is used in combination with the protein deamidase and transglucosidase. However, in the same field of endeavor, Triantafyllou teaches that the oat base is provided with one or more amylases and protein deamidase ([0013]), where the amylase can be alpha-amylase ([0026]). It would have been obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to modify the process of Yamamoto with the addition of alpha-amylase as taught by Triantafyllou. One of ordinary skill would be motivated to make this modification because Triantafyllou teaches that amylase helps increase the amount of water-soluble protein in a composition ([0005]) and that a higher protein content of the product is paralleled by increased stability of the product ([0062]). Regarding claim 10, Yamamoto teaches all elements of claim 1 as described above. Yamamoto does not teach wherein the plant protein food and drink material and/or the plant protein food and drink includes oat protein and has fluidity. However, in the same field of endeavor, Triantafyllou teaches a process for making an oat drink treated with protein deamidase (Abstract). Because the product is a drink, it logically follows that it has fluidity. It would have been obvious to one of ordinary skill in the art prior to the effective filing date of the claimed invention to modify the process of Yamamoto with the use of oats as taught by Triantafyllou. It would have been obvious because one of ordinary skill in the art could have combined the method of Yamamoto using both protein deamidase and transglucosidase with the method of treating oat milk using protein deamidase and yield the predictable result of a stable oat milk composition. The claim would have been obvious because all 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 function, and the combination yielded nothing more than predictable results to one of ordinary skill in the art, see MPEP §2143(A). Claim 5 are rejected under 35 U.S.C. 103 as being unpatentable over Yamamoto (JP 2011206048A) as evidenced by Motoki (Motoki, Masao, et al. “Glutamine-specific Deamidation of αs1-Casein by Transglutaminase”, Agriculture and Biological Chemistry, Vol. 50(12), p. 3025-3030, published 1986 [accessed online March 17, 2026]). Regarding claim 5, Yamamoto teaches all elements of claim 1 as described above. Yamamoto also teaches wherein the amount of α-glucosidase (i.e., transglucosidase) is 0.15 to 200,000 U per 1 U of transglutaminase (i.e., protein deamidase) ([0013], (10)), which encompasses the claimed range of “1 U or more per 1 U of protein deamidase”. With respect to the overlapping ranges, MPEP §2114.05 teaches that it would have been obvious to one of ordinary skill in the art before the effective filing date of the invention to have selected the overlapping portion of the ranges disclosed by the reference because selection of overlapping portion of ranges has been held to be a prima facie case of obviousness. Response to Arguments Claim Rejections – 35 U.S.C. §102 of claims 1, 3, 4, and 6 over Yamamoto: Applicant's arguments filed December 19, 2025 have been fully considered but they are not persuasive. Applicant argued that transglutaminases produce protein with crosslinking, and that transglutaminase functions differently than that of other protein deamidase (Remarks, p. 3, ¶ 5- p. 4, ¶ 2). This argument has been considered. However, transglutaminase is capable of exhibiting an action of decomposing an amide group-containing side chain of a protein without cleaving peptide bonds and crosslinking the protein. As described above, evidence to support this assertion is provided by Motoki. Motoki discloses that deamidated product was not crosslinked even after transglutaminase treatment (p. 3027, col. 1, ¶ 1), and that transglutaminase deamidation was specific to the side chains, and that there was no degradation (i.e., no cleaving) of peptide bonds (p. 3029, col 1, ¶ 2- col 2, ¶ 1). Therefore, the transglutaminase of Yamamoto meets the requirement of the protein deamidase of claim 1. Applicant argued that Yamamoto only teaches certain effects in rice foods. However, the Example of the instant specification described a creamy feeling-enhancing effect and a sweetness-reducing effect. Applicant asserted that the texture obtained by the claimed invention is entirely different from that taught by Yamamoto and that these attributes were surprising and unpredictable (Remarks, p. 4, ¶ 3-6). This argument has been considered. In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., the texture obtained) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Because Yamamoto teaches all elements of claim 1, Yamamoto sufficiently anticipates the claimed invention. Furthermore, MPEP ¶716.02(d) states “Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the "objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support." In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range. In re Clemens, 622 F.2d 1029, 1036, 206 USPQ 289, 296 (CCPA 1980)”. The Applicant has failed to provide sufficient data for a showing of unexpected results. Claim Rejections – 35 U.S.C. §103 of claims 2 and 7 over Yamamoto and Triantafyllou: Applicant's arguments filed December 19, 2025 have been fully considered but they are not persuasive. Applicant argued that Triantafyllou only teaches the solubilization of oat milk, and that the texture and taste obtained by the presently claimed methods was completely unpredictable (Remarks, p. 4, ¶ 7). This argument has been considered. In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., the texture obtained) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Furthermore, MPEP §716.02(d) states that “Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the "objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support." In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range. In re Clemens, 622 F.2d 1029, 1036, 206 USPQ 289, 296 (CCPA 1980)” and “To establish unexpected results over a claimed range, applicants should compare a sufficient number of tests both inside and outside the claimed range to show the criticality of the claimed range. In re Hill, 284 F.2d 955, 128 USPQ 197 (CCPA 1960).” Further data would be required for a showing of unexpected results for the claimed invention. The rejections of claims 1-7 have been maintained herein. Conclusion THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a). A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action. Any inquiry concerning this communication or earlier communications from the examiner should be directed to Amanda S Hawkins whose telephone number is (703)756-1530. The examiner can normally be reached Generally available M-Th 8:00a-5:00p, F 8:00-2:00. 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, Emily Le can be reached at (571) 272-0903. 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. /A.S.H./Examiner, Art Unit 1793 /EMILY M LE/Supervisory Patent Examiner, Art Unit 1793
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Prosecution Timeline

Apr 28, 2023
Application Filed
Sep 18, 2025
Non-Final Rejection — §102, §103
Dec 19, 2025
Response Filed
Mar 02, 2026
Final Rejection — §102, §103 (current)

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Prosecution Projections

3-4
Expected OA Rounds
0%
Grant Probability
0%
With Interview (+0.0%)
3y 2m
Median Time to Grant
Moderate
PTA Risk
Based on 13 resolved cases by this examiner. Grant probability derived from career allow rate.

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