Prosecution Insights
Last updated: April 19, 2026
Application No. 18/044,518

TOFU PRODUCTION METHOD

Final Rejection §103
Filed
Mar 08, 2023
Examiner
LI, CHANGQING
Art Unit
1791
Tech Center
1700 — Chemical & Materials Engineering
Assignee
Amano Enzyme Inc.
OA Round
3 (Final)
30%
Grant Probability
At Risk
4-5
OA Rounds
3y 7m
To Grant
64%
With Interview

Examiner Intelligence

Grants only 30% of cases
30%
Career Allow Rate
88 granted / 294 resolved
-35.1% vs TC avg
Strong +34% interview lift
Without
With
+34.1%
Interview Lift
resolved cases with interview
Typical timeline
3y 7m
Avg Prosecution
83 currently pending
Career history
377
Total Applications
across all art units

Statute-Specific Performance

§101
2.5%
-37.5% vs TC avg
§103
49.8%
+9.8% vs TC avg
§102
12.3%
-27.7% vs TC avg
§112
29.0%
-11.0% vs TC avg
Black line = Tech Center average estimate • Based on career data from 294 resolved cases

Office Action

§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 . 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 after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.114 has been timely paid, the finality of the previous Office Action has been withdrawn pursuant to 37 CFR 1.114. Applicant’s submission filed on 02/18/2026 has been entered. Claim status Claims 1 and 3-10 are pending in the application, are previously presented, and are hereby examined on the merits. Examiner Note Any objections and/or rejections that are made in the previous actions and are not repeated below, are hereby withdrawn. Claim Rejections - 35 USC § 103 The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. Claims 1, 3-5 and 7-10 are rejected under 35 U.S.C. 103 as being unpatentable over He US Patent Application Publication No. 2009/0142449 A1 (hereinafter referred to as He) in view of Yamaguchi US Patent Application Publication No. 2002/0009770 A1 (hereinafter referred to as Yamaguchi) and Yasir, “The impact of transglutaminase on soy proteins and tofu texture”, Food Chemistry, 2007, 104, pages 1491-1501 (hereinafter referred to as Yasir). Regarding claims 1, 3 and 10, He teaches a method of making a tofu comprising adding a crosslinking enzyme (e.g., transglutaminase) to soy milk so as to crosslink the protein in the soymilk; and He further teaches the soymilk is coagulated with a coagulant such as magnesium chloride (0008; 0010-0014; 0020). He teaches that the crosslinking enzyme is transglutaminase thus being silent regarding laccase. Yamaguchi teaches that protein materials are crosslinked to have a high molecular weight or gelled structure by the action of a crosslinking enzyme, and mostly such an enzyme is transglutaminase (0002-0003). Yamaguchi further teaches that laccase is an alternative crosslinking enzyme to transglutaminase in increasing the molecular weight and forming gel in a protein material (0007-0008), and the substrate protein for the laccase can be a plant protein derived from beans or cereal in the form of a solution, slurry and paste (0022-0023). Further, Yamaguchi teaches that the laccase can be used in the field of food processing such as fish meat paste, fish cake, sausage, noodle and tofu (0002). Both He and Yamaguchi are directed to crosslinking enzymes and/or tofu. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified He by substituting laccase for transglutaminase as the crosslinking enzyme in making tofu with reasonable expectation of success, for the reason that prior art has established that laccase is a functional equivalent to transglutaminase in crosslinking soybean protein to increase the molecular weight and form a gel in tofu making. Substituting equivalents known for the same purpose is prima facies obvious. See MPEP 2144.06 II. He in view of Yamaguchi as recited above teaches a method of making tofu comprising treating soymilk with a crosslinking enzyme but is silent regarding a boiling step after the crosslinking. In the same filed of endeavor, Yasir teaches a method of making tofu comprising treating soymilk with a cross-linking enzyme (e.g., transglutaminase) followed by boiling, and coagulation (page 1492, section 2.4; page 1493, section 2.6). It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified He by including a boiling step after crosslinking with reasonable expectation of success, for the reason that prior art has established that a boiling step after enzyme crosslinking is suitable in tofu making. Regarding claim 4-5, He teaches a transglutaminase amount of less than 2 U per gram (0008). Yamaguchi teaches that the amount of laccase is 0.5 to 1 x 106 units or narrowly 5 to 1 x 105 units per 1 gram of protein (0024). It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have used the enzyme dosage as disclosed by Yamaguchi so as to ensure that the level of laccase is sufficient to increase the molecular weight or to form a gel. The amount of enzyme as disclosed by Yamaguchi encompasses the ranges as disclosed in claims 4-5. In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. (MPEP 2144.05 I). Regarding claim 7, Yamaguchi teaches a temperature of 5-80 °C or narrowly 20-60 °C for the laccase enzyme to crosslink a protein to increase molecular weight or to form a gel (0024). It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have included the crosslinking temperature as disclosed by Yamaguchi so as to ensure that the laccase could efficiently catalyze the crosslinking of soy protein to increase the molecular weight or to form a gel. The temperature as disclosed by Yamaguchi encompasses or overlaps with the range as disclosed in claim 7. In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. (MPEP 2144.05 I). Regarding claims 8-9, He teaches 50 ml magnesium chloride having a Brix value of 19 is added to 6 L soy milk (Table 1), thus the amount of magnesium chloride by weight of soy milk is 50 x 0.19/6000 =~ 0.16%; further, He teaches 3.96 L magnesium chloride having a Brix value of 17.75 is added to 28 gallon soy milk (0020) thus the amount of magnesium chloride by weight of the soy milk is 3.96 x 0.1775/(28 x 3.78) = ~ 0.66%. Claim 6 is rejected under 35 U.S.C. 103 as being unpatentable over He in view of Yamaguchi and Yasir as applied to claim 1 above, and further in view of Rajakari EP2773753 B1 (cited in the IDS submitted 09/10/2024, hereinafter referred to as Rajakari). Regarding claim 6, Yamaguchi teaches that the laccase can be derived from Trametes (0015), but is silent regarding the species Trametes hirsute. Rajakari teaches that laccase derived from Trametes hirsute is able to catalyze the crosslinking a protein, thus is suitable for use in food processing (0015). Both He and Rajakari are directed to using an enzyme to crosslink a protein in the art of food, and where Yamaguchi teaches that laccase of Trametes origin is suitable for catalyzing the crosslinking of soy protein, Rajakari teaches that a specific laccase of Trametes origin (e.g., laccase derived from Trametes hirsute) is able to catalyze the crosslinking a protein in the food art. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified He in view of Yamaguchi by using laccase derived from Trametes hirsute to crosslink soy protein with reasonable expectation of success, for the reason that prior art has established the suitability of laccase derived from Trametes hirsute in catalyzing the crosslinking a protein for food use. The selection of a known material based on its suitability for its intended use supports a prima facie obviousness determination. See MPEP 2144.07. Claims 1, 3-5 and 7-9 are rejected under 35 U.S.C. 103 as being unpatentable over Yamaguchi US Patent Application Publication No. 2002/0009770 A1 (hereinafter referred to as Yamaguchi) in view of Yasir, “The impact of transglutaminase on soy proteins and tofu texture”, Food Chemistry, 2007, 104, pages 1491-1501 (hereinafter referred to as Yasir). Regarding claims 1 and 3, Yamaguchi teaches that protein materials are crosslinked to have a high molecular weight or gelled structure by the action a crosslinking enzyme, and mostly such an enzyme is transglutaminase (0002-0003). Yamaguchi further teaches that laccase is an alternative crosslinking enzyme to transglutaminase in increasing the molecular weight and forming gel in a protein material (0007-0008), and the substrate protein for the laccase can be a plant protein derived from beans or cereal in the form of a solution, slurry and paste (0023). Further, Yamaguchi teaches that the laccase can be used in the field of food processing such as fish meat paste, fish cake, sausage, noodle and tofu (0002). It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have subjecting a soy milk to the crosslinking step by a laccase to make a tofu, for the reason that it is known that tofu is made of a soymilk, and Yamaguchi teaches that laccase can catalyze the crosslinking of a bean protein in the form of a solution, slurry and paste, and can be used in the field of tofu. Yamaguchi is silent regarding the step of boiling step, the step of coagulation step using a coagulant at a concentration of 0.1% (or 0.5%) or more as recited in claims 3 and 8-9. Yasir in the same field of endeavor teaches a method of making tofu comprising treating soymilk with a crosslinking enzyme (e.g., transglutaminase) followed by boiling, and a coagulation step by a coagulant (e.g., calcium sulfate dihydrate) (page 1492, section 2.4; page 1493, section 2.6). It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Yamaguchi by including the step of boiling the soymilk after crosslinking a soymilk and the step of coagulating the crosslinked soymilk with reasonable expectation of success, for the reason that the aforementioned steps are known to be suitable in making a tofu. Regarding claim 4-5, Yamaguchi teaches that the amount of laccase is 0.5 to 1 x 106 units or narrowly 5 to 1 x 105 units per 1 gram of protein (0024). In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. (MPEP 2144.05 I). Regarding claim 7, Yamaguchi teaches a temperature of 5-80 °C or narrowly 20-60 °C for the laccase enzyme to crosslink a protein to increase molecular weight or to form a gel (0024). In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. (MPEP 2144.05 I). Regarding claims 8-9, Yasir teaches adding 6.7 gram of calcium sulfate dihydrate to 750 ml of soy milk (page 1492, section 2.4), thus the concentration of the coagulant by weight of the soy milk is about 6.7/750 = 0.9%, assuming a density of 1 g/ml for the soy milk. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Yamaguchi by incorporating the amount of coagulant with reasonable expectation of success, for the reason that prior art has established that the aforementioned amount of the coagulant is suitable for coagulating the soymilk into a tofu. Claim 6 is rejected under 35 U.S.C. 103 as being unpatentable over Yamaguchi in view of Yasir as applied to claim 1 above, and further in view of Rajakari EP2773753 B1 (cited in the IDS submitted 09/10/2024, hereinafter referred to as Rajakari). Regarding claim 6, Yamaguchi teaches that the laccase can be derived from Trametes (0015), but is silent regarding the species Trametes hirsute. Rajakari teaches that laccase derived from Trametes hirsute is able to catalyze the crosslinking a protein, thus is suitable for use in food processing (0015). Both Yamaguchi and Rajakari are directed to laccase derived from Trametes. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Yamaguchi by using laccase derived from Trametes hirsute to crosslink soy protein with reasonable expectation of success, for the reason that prior art has established the suitability of laccase derived from Trametes hirsute in catalyzing the crosslinking of a protein for food use. The selection of a known material based on its suitability for its intended use supports a prima facie obviousness determination. See MPEP 2144.07. Claim 10 is rejected under 35 U.S.C. 103 as being unpatentable over Yamaguchi in view of Yasir as applied to claim 1 above, and further in view of He US Patent Application Publication No. 2009/0142449 A1 (hereinafter referred to as He). Regarding claim 10, Yamaguchi in view of Yasir as recited above teaches using calcium sulfate dihydrate to coagulate soymilk to make a tofu thus being silent regarding that the coagulant is magnesium chloride. He teaches that in carrying out the tofu production method, any conventionally known coagulant including magnesium chloride, calcium sulfate, and glucono delta-lactone can be used (0011). Both Yamaguchi and He are directed to tofu. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Yamaguchi by using magnesium chloride to coagulate soy protein to make tofu with reasonable expectation of success, for the reason that prior art has established that magnesium sulfate is suitable for coagulating soy protein to make tofu. Response to Declaration and Arguments The declaration under 37 CFR 1.132 filed 02/18/2026 is insufficient to overcome the rejection of pending claims based upon the references as set forth in the last Office action. Applicant's arguments filed 02/18/2026 have been fully considered but they are not persuasive. Regarding the 35 USC 103 rejection of previously claim 1, applicant asserts unexpected result associated with the step of crosslinking soy protein with laccase followed by boiling. In particular, applicant asserts that as compared to the result of Yasir which uses transglutaminase to crosslink soy protein followed by boiling, substituting laccase for transglutaminase results in a higher degree of improvement in tofu firmness. Further, in response to the examiner’s stance that fracture force used to measured firmness of tofu as in Yasir and firmness measured in the claimed invention are distinct parameters, that there is no evidence that Yasir and the claimed invention are using the same conditions (except the enzyme), the same amount of enzymes, and the same coagulation, applicant argues on pages 4-5 of the Remarks that the claimed invention measures firmness through compressive strength which is synonymous with fracture force, and that the claimed invention used an enzyme dose of 0.0232 mg/ml ( as attested in the Declaration filed concurrently), which is lower than the transglutaminase used by Yasir, making the improvement in firmness by the presently claimed method even more remarkable. The arguments are considered but found unpersuasive for the reason that applicant has not been able to isolate those parameters that could contribute to the firmness of the tofu from the comparison so as to unquestionably prove that the improved firmness is solely because the of enzyme used, even assuming that compressive strength and fracture force are the same parameters. For example, in making the inventive tofu (e.g., Example 4-1) the coagulant being used is magnesium chloride at a concentration of 1% (see also Example 1), however, Yasir uses a different coagulant calcium sulfate at a lower concentration of ~0.8% (Yasir section 2.4). It is known that type of a coagulant has an effect on the textural properties including firmness or hardness of a tofu. See Andrea (Andrea, Tofu Coagulant Buying Guide: Which to get and where to find it [Online], published Oct 4, 2012, [retrieved on 2026-02-26]. Retrieved from the Internet: <URL: https://www.vietworldkitchen.com/blog/2012/10/tofu-coagulant-guide.html>), which evidences that tofu made from magnesium chloride (e.g., nigari) is firmer than that from calcium sulfate (e.g., gypsum). Additionally, the amount of a coagulant could affect the texture of a tofu since the coagulant interacts with the protein molecules to form a network, hence coagulation. Further, where Yasir details the pressing condition (Yasir section 2.4), the claimed invention is silent regarding how the tofu is post-processed. To this end, the firmness of a tofu is reasonably related to the pressing condition, since the step removes moisture to firm up the tofu. Therefore, the Office, again, encourages the applicant to compare the two under the same conditions, i.e., using same amount of enzymes in term of enzyme unit U as opposed to the concentration of the enzyme, using soymilk having the same dry matter and composition, performing crosslinking under the same conditions (e.g., time and temperature), boiling the crosslinked soy protein under the same conditions (e.g., time and temperature), coagulating the crosslinked protein under the same condition (e.g., coagulant, time and temperature), molding the tofu under the same condition (the intensity and duration of firming), and testing the texture by the same parameters and under the same conditions. Doing so would help to exclude the intervening parameters. For the reason set forth above, applicant’s argument regarding depending claims are not persuasive, either. Conclusion All claims are identical to or patentably indistinct from, or have unity of invention with claims in the application prior to the entry of the submission under 37 CFR 1.114 (that is, restriction (including a lack of unity of invention) would not be proper) and all claims could have been finally rejected on the grounds and art of record in the next Office action if they had been entered in the application prior to entry under 37 CFR 1.114. Accordingly, THIS ACTION IS MADE FINAL even though it is a first action after the filing of a request for continued examination and the submission under 37 CFR 1.114. See MPEP § 706.07(b). 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 CHANGQING LI whose telephone number is (571)272-2334. The examiner can normally be reached 9:00-5:00. 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, NIKKI H DEES can be reached at 571-270-3435. 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. /CHANGQING LI/Primary Examiner, Art Unit 1791
Read full office action

Prosecution Timeline

Mar 08, 2023
Application Filed
May 03, 2025
Non-Final Rejection — §103
Sep 05, 2025
Response Filed
Sep 16, 2025
Final Rejection — §103
Feb 18, 2026
Request for Continued Examination
Feb 18, 2026
Response after Non-Final Action
Feb 24, 2026
Response after Non-Final Action
Mar 13, 2026
Final Rejection — §103 (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

4-5
Expected OA Rounds
30%
Grant Probability
64%
With Interview (+34.1%)
3y 7m
Median Time to Grant
High
PTA Risk
Based on 294 resolved cases by this examiner. Grant probability derived from career allow rate.

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