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 Application, Amendments, And/Or Claims
The Applicants amendments/remarks received 9/26/2025 are acknowledged. Claims 3-4 are amended; no claims are canceled; no claims are withdrawn; claims 10-11 are new; claims 1-11 are pending and have been examined on the merits.
Information Disclosure Statement
The information disclosure statement submitted on 9/26/2025 has been considered by the examiner. NOTE: The author of NPL cite 1 is Hitomi Kiyotaka; hence, “SEIKAGAKU” has been struck from the reference and Kiyotaka added as the author.
Claim Rejections - 35 USC § 112
The rejection of claims 3-4 under 35 U.S.C. § 112(b), as set forth at pp. 2-3 of the previous Office Action, is withdrawn in view of the amendment of the claims.
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 (i.e., changing from AIA to pre-AIA ) 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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 3 and 5-8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Hou et al., 2016 (NPL cite 11, IDS, 3/8/2023; herein “Hou”) in light of Hou et al., 2015 (cite U, attached PTO-892; herein “Hou#2”).
Hou teaches producing tofu with a method of producing a processed protein comprising a crosslinking step of causing a laccase and a transglutaminase to act on a protein, wherein the crosslinking step comprises the sequential treatment with 4 U laccase per g sugar beet pectin (SBP) and 20 U transglutaminase per g protein (Abst.; pp. 963-964, “Preparation of double-network modified-tofu”) anticipating claims 1, 3 and 7.
Hou#2 is cited as evidence that SBP comprises 5.6% protein (p. 95, “2.1. Materials”); hence, 4 U laccase per g SBP constitutes 71 U laccase per g protein (4 U laccase / 1 g SBP x (1 g SBP / 56 mg SBP protein) x (1000 mg / g) = 71 U laccase / g protein); hence, Hou teaches that the method comprises using laccase in an amount of 71 U laccase / g protein. 20 U transglutaminase per g protein / 71 U laccase per g protein = 0.28 U transglutaminase / U laccase. Hence, Hou anticipates claims 5-6 and 8.
Response to Arguments
Applicant's arguments filed 9/26/2025 have been fully considered but they are not persuasive. Arguments of the Applicant’s Response on p. 3 regarding the rejection under 35 U.S.C. § 112(b) are moot as the rejection has been withdrawn.
Regarding the rejection of claims 1-3 and 5-8 under 35 U.S.C. 102(a)(1) over Hou in light of Hou#2, Applicant argues (pp. 3-4) that “Specifically, in Hou #1, laccase treatment is performed on "beet pectin", followed by transglutaminase treatment on "soy protein". In other words, Hou #1 does not disclose that both laccase and transglutaminase are used for treatment of a protein as specified in present claim 1.” This is incorrect. Hou teaches preparing tofu comprising treating SBP with laccase, followed by addition of soy milk and treatment with transglutaminase (pp. 963-964, “Preparation of double-network modified-tofu”). SBP comprises 5.6% protein (Hou#2; p. 95, “2.1. Materials”); hence, the protein from SBP are treated with both laccase and transglutaminase and the final product of the processed protein is tofu anticipating claims 1 and 3, as set forth in the rejection above. Hou is clear on this point - “The cross-linking between soy protein and the proteinaceous moieties in SBP which was catalysed by MTGase resulted in the interconnections between the SBP and protein network” (p. 965, ¶3).
The soybean protein is only contacted with transglutaminase; hence, Applicant’s argument is persuasive regarding claim 2 but not regarding claims 1, 3 or 5-8.
Applicant further presents an argument based on secondary consideration due to unexpected results (p. 4); however, secondary considerations are only relevant for rejections based on obviousness not for rejections under 35 U.S.C. 102(a)(1) based on anticipation; hence, the argument is moot regarding the rejection under 35 U.S.C. 102(a)(1) over Hou in light of Hou#2 and the rejection is maintained regarding claims 1, 3 and 5-8.
Claim Rejections - 35 USC § 102/103
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 (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 1-2, 5 and 7-10 are rejected under 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Aaltonen et al., US 2014/0220178 (US Patent document cite 3, IDS, 3/8/2023; herein “Aaltonen”).
Aaltonen teaches a method of producing a processed protein (Abst.), wherein the protein can be soybean protein [0036], wherein the method can comprise crosslinking the protein with transglutaminase and laccase used in combination with each other [0041], i.e., wherein in the crosslinking step the laccase and the transglutaminase are simultaneously reacted with the protein, wherein the laccase can be from Trametes hirsuta [0045], wherein the amount of laccase can be 5 U / g protein [0046], wherein the amount of transglutaminase can be 5 U / g protein [0046] anticipating claims 1-2, 5 and 7-10.
It is believed that Aaltonen anticipates claims 1-2, 5 and 7-10; however, if it is determined that Aaltonen is not anticipatory, claims 1-2, 5 and 7-10 are clearly prima facie obvious over paragraphs [0036], [0041], [0045] and [0046] of Aaltonen.
Response to Arguments
Regarding the rejection of claims 1-2, 5 and 7-10 under 35 U.S.C. § 102(a)(1), Applicant argues (p. 4) that “Aaltonen et al. merely discloses transglutaminase and laccase as examples of listed crosslinking enzymes ("transglutaminase, laccase, tyrosinase, peroxidase, sulfhydryl oxidase, glucose oxidase, protein-glutaminase") in paragraph [0028]. Aaltonen et al. does not disclose the specific combination of transglutaminase and laccase to be selected from among these crosslink-forming enzymes and actually used in combination to treat a protein as specified in present claim 1. Therefore, claims 1-11 are not anticipated by Aaltonen et al.” This is unpersuasive as Aaltonen states “These enzymes include transglutaminase, laccase, tyrosinase, peroxidase, sulfhydryl oxidase, glucose oxidase, protein glutaminase, etc. Said enzymes can be used alone or in any combinations with each other.” [0041]. Hence, Aaltonen clearly anticipates methods wherein the crosslinking enzyme comprises transglutaminase and laccase used in combination with each other. Thus, the rejection of claims 1-2, 5 and 7-10 under 35 U.S.C. § 102(a)(1) over Aaltonen is maintained with modification to address claim amendments, new claims and for clarity.
Applicant further argues (p. 5) that there is no teaching regarding specific amounts of laccase and transglutaminase in Aaltonen, quoting [0046] of Aaltonen: “The amount of the protein crosslinking enzyme added to the first raw material liquid ranges from 0.2 to 10U/g protein. In an embodiment, the amount is 1 to 5 U/g protein.” This is unpersuasive of error in the rejection as Aaltonen clearly anticipates methods wherein the amount of enzyme can be between 0.2 U/gprotein and 10 U/ gprotein.
Applicant argues that combining laccase and transglutaminase treatment produces synergy and said synergy is an unexpected result (pp. 4-7).
To successfully argue for secondary consideration based on unexpected results, several considerations are employed as discussed in MPEP 716:
A) Evidence of unexpected results are weighed against evidence supporting prima facie obviousness in making a final determination of the obviousness of the claimed invention.
B) Alleged unexpected results must be commensurate in scope with the claimed invention. Independent claim 1 recites a method of producing a processed protein, comprising a crosslinking step of causing a laccase and a transglutaminase to act on a protein wherein the protein can be any protein, wherein the amount of laccase can be any amount, even a de minimus amount, wherein the amount of transglutaminase can be any amount, even a de minimus amount, wherein the crosslinking step can be at any temperature, wherein the crosslinking step can be for any length of time, including a momentary contacting between the enzymes and the protein composition and wherein the laccase and transglutaminase are not required to be simultaneously present.
The alleged unexpected results are the firmness of the tofu produced wherein the soybean protein is mixed with 50 U laccase per g protein, 02-2 U transglutaminase per g protein and 1 wt% MgCl2 coagulant and incubated at 55 °C for 1 h (specification, Test Example 1, [0054-61]), wherein, according to Applicant, the firmness of the tofu was enhanced by about 37 - 39 N, which amounts to a synergistic effect of ~ 30 N over what would be expected from an additive effect (37-39 N - 8 N (laccase alone)) (Remarks, pp. 5-6).
It is noted that the specification also discloses that the increase in firmness of fermented soy milk (specification, Test Example 2, [0062-64]) was enhanced by 50 U laccase·g-1 alone to 1.25 times that of no enzyme treatment; was enhanced by 20 U transglutaminase·g-1 alone to 1.33 times that of no enzyme treatment; and was enhanced by 50 U laccase·g-1 and 20 U transglutaminase·g-1 to 1.63 times that of no enzyme treatment; hence, the synergistic effect with fermented soy milk appears to be only 0.05 times that of no enzyme treatment as the additive effect would be 1.58 times that of no enzyme treatment. No replicates appear to have been performed as each data point appears to be a single sample; hence, it is completely unclear whether the 0.05-fold increase attributed to synergy is statistically relevant or simply errors in the measurement because no error measurement can be assayed from the assay without replicates; hence, the alleged synergism between laccase and transglutaminase is not established when the method is for producing fermented soy milk and does not comprise adding MgCl2 coagulant to the protein composition.
Hence, the alleged unexpected result has only been demonstrated for methods of producing tofu wherein a soybean protein composition is incubated simultaneously with ≥50 U laccase·g-1, ≥0.02 U transglutaminase and 1 wt% MgCl2 at 55 °C for at least 1 h; hence, there is clearly no demonstration of unexpected results commensurate in scope with claim 1 which encompasses treatment of any protein with a de minimus amount of laccase and a de minimus amount of transglutaminase and no MgCl2 coagulant, wherein the treatment is not required to be simultaneous and can comprise treatment for any amount of time at any temperature. Thus, the unexpected results are not commensurate in scope with the claimed invention and are unpersuasive as a secondary consideration, because the scope of independent claim 1 is much broader than the method which produces the alleged unexpected results and claim 1 does not require method steps which the alleged unexpected results would appear to require including that the composition comprises ≥50 U laccase·g-1, ≥0.02 U transglutaminase and 1 wt% MgCl2 and that the enzymes and coagulant are incubated with the protein composition at 55 °C for at least 1 h. None of the dependent claims limit the method to a scope which is commensurate in scope with the alleged unexpected results. See MPEP 716.02(d).
C) To support an allegation of unexpected results, the claimed composition must be compared to the compositions of the closest prior art to be effective to rebut a prima facie case of obviousness. In re Burckel, 592 F.2d 1175, 201 USPQ 67 (CCPA 1979). There is no comparison to the closest prior art, i.e. to the methods of Hou and the methods of Aaltonen. Hou and Aaltonen each separately anticipate instant claim 1; yet, Applicant has not shown that the methods of Hou and Aaltonen DO NOT produce the alleged unexpected results. Hence, Applicant's allegation of unexpected results is unsupported. See MPEP 716.02(e).
D) Evidence must show results that are unexpected. Hou clearly teaches (Abst.; throughout document) that the tofu prepared using both laccase and transglutaminase, i.e. double-network (DN) tofu, exhibited greater mechanical toughness than the corresponding single-network (SN) tofu, i.e., prepared using only laccase or only transglutaminase; hence, Applicant’s alleged unexpected result would appear to be simply what the prior art suggests. Hence, Applicant’s alleged unexpected results are not unexpected in view of the closest prior art.
Applicant’s arguments are unpersuasive and the rejection of claims 1-2, 5 and 7-10 under 35 U.S.C. 103 over Aaltonen is maintained with modification to address claim amendments, new claims and for clarity.
Claim Rejections - 35 USC § 103
Claims 1-11 are rejected under 35 U.S.C. 103 as being unpatentable over Aaltonen in view of Yamaguchi et al., US 2002/0009770 (US Patent document cite 2, IDS, 3/8/2023; herein “Yamaguchi”).
The discussion of Aaltonen regarding claims 1-2, 5 and 7-10 set forth in the rejection above is incorporated herein.
Aaltonen teaches that the cheese products and cheese milk products produced by the method of Aaltonen can be cheese-like and cheese milk-like products made from the substitution of plant proteins, such as soybean proteins, and other fats for the milk fat and milk proteins (Abst.; [0035-36]) and teaches that the products can be produced by ferments [0075], but does not specifically teach that the products are tofu and/or fermented soy milk; however, a person of ordinary skill in the art at the time of filing would have found it obvious that the products produced by the method of Aaltonen can be tofu and/or fermented soy milk in view of the disclosure of Yamaguchi.
Yamaguchi teaches that tofu and yogurt, a fermented milk product, are produced by a prior art method of protein processing comprising crosslinking of the proteins with transglutaminase [0002-3]. Yamaguchi teaches that these prior art products can be produced by substituting laccase for the transglutaminase wherein the laccase is from the genera Trametes ([0007], [0014-15]). Yamaguchi teaches that several protein crosslinking enzymes can be used in the production of these products, e.g. tofu and yogurt [0006].
Hence, a person of ordinary skill in the art at the time of filing would have found it obvious that the cheese-like product made with soybean protein with the method of Aaltonen would constitute tofu and that the cheese milk-like product made with soybean protein with fermentation with the method of Aaltonen would constitute fermented soy milk; therefore, claims 3-4 are prima facie obvious.
Regarding claims 6 and 11, the amount of laccase and transglutaminase in the method of Aaltonen comprising processing soybean protein simultaneously (used in combination with each other - [0041]) with both transglutaminase and laccase is a result effective variable and a person of ordinary skill in the art would expect the amount of laccase and transglutaminase to have an obvious effect on parameters such as the mechanical and organoleptic properties of the produced products (Aaltonen, Abst.; [0018-24]). Hence, a person of ordinary skill in the art would find it obvious to vary these parameters, i.e., the concentration of laccase and the concentration of transglutaminase, to get the mechanical and organoleptic properties that met the perceived need and would arrive at the claimed concentration of 30 U or more laccase per g protein and 0.02 - 2 U transglutaminase per g protein; therefore, claims 6 and 11 are prima facie obvious. See also MPEP 2144.05 II.A. “Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%)".
Response to Arguments
Regarding the rejection of claims 1-11 under 35 U.S.C. 103 over Aaltonen in view of Yamaguchi, Applicant does not specifically address the rejection or the teachings of Yamaguchi; hence, the rejection is maintained with modification to address claim amendments, new claims and for clarity.
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 1-3 and 5-11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 4-6 of copending Application No. 18/044518 (herein “’518”) in view of Aaltonen.
Claim 1 of ‘518 recites a tofu production method comprising a crosslinking step of causing a laccase to act on soy milk and a boiling step after the crosslinking step; claim 4 of ‘518 recites the tofu production method according to claim 1, wherein the laccase is used in an amount of 5 U or more per 1 g of soybean protein; claim 5 of ‘518 recites the tofu production method according to claim 1, wherein the laccase is used in an amount of 30 U or more per 1 g of soybean protein; claim 6 of ‘518 recites the tofu production method according to claim 1, wherein the laccase is derived from Trametes hirsuta.
The claims of ‘518 don’t specifically recite that the crosslinking step comprises transglutaminase and laccase acting simultaneously; however, a person of ordinary skill in the art at the time of filing would have found it obvious for the crosslinking step to comprise both transglutaminase and laccase acting simultaneously in view of Aaltonen.
Aaltonen teaches a method of producing a processed protein (Abst.), wherein the protein can be soybean protein [0036], wherein the method can comprise crosslinking the protein simultaneously with both transglutaminase and laccase [0041], wherein the laccase can be from Trametes hirsuta [0045], wherein the amount of laccase can be 5 U / g protein [0046], wherein the amount of transglutaminase can be 0.2 - 5 U / g protein [0046].
Hence, a person of ordinary skill in the art at the time of filing would have found it obvious to practice the methods of claims 1 and 4-6 of ‘518 wherein the crosslinking in the production of tofu comprises contacting the soy milk protein simultaneously with 5 U laccase per g protein and 0.2 U transglutaminase per g protein in view of Aaltonen; therefore, instant claims 1-3 and 5-10 are prima facie obvious.
Regarding instant claim 11, claim 5 of ‘518 makes it obvious to use 30 U laccase / g protein and Aaltonen makes it obvious to use 0.2 U transglutaminase per g protein wherein the production of tofu comprises contacting the soy milk protein simultaneously with the laccase and transglutaminase; therefore, instant claim 11 is prima facie obvious.
This is a provisional nonstatutory double patenting rejection.
Claims 1-2, 5 and 7-10 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 3-6 of copending Application No. 18/042510 (herein “’510”) in view of Aaltonen.
Claim 1 of ‘510 recites a method for producing a modified protein, comprising a step of allowing a peptidylprolyl isomerase and a protein modification enzyme to act on a protein; claim 3 of ‘510 recites the production method according to claim 1, wherein the protein modification enzyme is selected from the group consisting of a proteolytic enzyme, a protein side-chain modifying enzyme, and a protein crosslinking enzyme; claim 4 of ‘510 recites the production method according to claim 1, wherein the protein modification enzyme is selected from the group consisting of a protease, a protein deamidase, a transglutaminase, and an oxidoreductase that catalyzes crosslinking of proteins; claim 5 of ‘510 recites the production method according to claim 1, wherein the protein is selected from the group consisting of plant proteins derived from beans, grains, nuts, and seeds; milk proteins, egg proteins, blood proteins, muscle proteins and tendon proteins: and proteins derived from microorganisms, algae, and insects; and claim 6 of ‘510 recites the method according to claim 1, wherein the protein is in a food material, a pharmaceutical material, or an industrial material.
Thus, claims 1 and 3-6 of ‘510 make obvious producing a food material comprising proteins from beans comprising treating the proteins with a transglutaminase, but does not specifically recite that the beans are soybeans or that the proteins are treated simultaneously with laccase and transglutaminase; however, a person of ordinary skill in the art at the time of filing would have found it obvious to use soybeans and to treat the proteins simultaneously with laccase and transglutaminase in view of the disclosure of Aaltonen.
Aaltonen teaches a method of producing a processed protein (Abst.), wherein the protein can be soybean protein [0036], wherein the method can comprise crosslinking the protein simultaneously with both transglutaminase and laccase [0041], wherein the laccase can be from Trametes hirsuta [0045], wherein the amount of laccase can be 5 U / g protein [0046], and wherein the amount of transglutaminase can be 0.2-5 U / g protein [0046].
Hence, a person of ordinary skill in the art at the time of filing would have found it obvious to practice the methods of claims 1 and 3-6 of ‘510 wherein the beans are soybeans and the contacting with enzyme comprises contacting the soybean protein simultaneously with 5 U laccase per g protein and 0.2-5 U transglutaminase per g protein in view of Aaltonen; therefore, instant claims 1-2, 5, and 7-10 are prima facie obvious.
This is a provisional nonstatutory double patenting rejection.
Claims 1-2, 5 and 7-10 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 4, 13, 15 and 17 of copending Application No. 17/906498 (herein “’498”) in view of Aaltonen.
Claim 1 of ‘498 recites a protein crosslinking method comprising allowing a protein improving agent comprising an oxidoreductase and a protein deamidase to act on a protein; claim 2 of ‘498 recites the protein crosslinking method according to claim 1, wherein the oxidoreductase is multicopper oxidase; claim 4 of ‘498 recites the protein crosslinking method according to claim 2, wherein the multicopper oxidase is laccase. Claim 13 of ‘498 recites a method for producing a crosslinked protein, the method comprising the steps of: (1) treating a protein with a protein deamidase; and (2) treating the protein subjected to protein deamidation with an oxidoreductase; claim 15 of ‘498 recites the method of claim 13, wherein the protein is simultaneously treated with the oxidoreductase and the protein deamidase; and claim 17 of ‘498 recites the method of claim 15, wherein the protein is contained within a food or a pharmaceutical product.
Thus, claims 1-2, 4, 13, 15 and 17 of ‘498 make obvious producing a food material comprising treating the proteins with laccase, but does not specifically recite that the protein is soybean protein or that the proteins are treated simultaneously with laccase and transglutaminase; however, a person of ordinary skill in the art at the time of filing would have found it obvious to use soybean protein and to treat the protein simultaneously with laccase and transglutaminase in view of the disclosure of Aaltonen.
Aaltonen teaches a method of producing a processed protein (Abst.), wherein the protein can be soybean protein [0036], wherein the method can comprise crosslinking the protein simultaneously with both transglutaminase and laccase [0041], wherein the laccase can be from Trametes hirsuta [0045], wherein the amount of laccase can be 5 U / g protein [0046], and wherein the amount of transglutaminase can be 0.2-5 U / g protein [0046].
Hence, a person of ordinary skill in the art at the time of filing would have found it obvious to practice the methods of claims 1-2, 4, 13, 15 and 17 of ‘498 wherein the protein is soybean protein and the contacting with enzyme comprises contacting the soybean protein simultaneously with 5 U laccase per g protein and 0.2-5 U transglutaminase per g protein in view of Aaltonen; therefore, instant claims 1-2, 5, and 7-10 are prima facie obvious.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Regarding the double patenting rejections, Applicant (p. 7) argues that “the claims no longer read on the claims in the cited applications and the Applicant respectfully requests that the double patenting rejections be withdrawn.” This is incorrect. The rejections are maintained with modification to address claim amendments, new claims and for clarity.
Conclusion
No claims are allowed.
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.
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/TRENT R CLARKE/ Examiner, Art Unit 1651
/DAVID W BERKE-SCHLESSEL/ Primary Examiner, Art Unit 1651