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 .
Withdrawal of Rejections
The response and amendments filed on 10/31/2025 are acknowledged. Any previously applied minor objections and/or minor rejections (i.e., formal matters), not explicitly restated here for brevity, have been withdrawn necessitated by Applicant’s formality correction and/or amendments. For the purposes of clarity of the record, the reasons for the Examiner’s withdrawal, and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner’s Response to Arguments section.
Briefly, the previous double patenting rejections have been withdrawn necessitated by Applicants arguments.
The following rejections and/or objections are either reiterated or newly applied. They constitute the complete set presently being applied to the instant application.
Priority
The instant application filed on 09/16/2022 is a 371 of PCT/JP2021/010764 filed on 03/17/2021 which claims priority to JP2020-046931 filed on 03/17/2020. However, the certified copy of foreign priority for JP2020-046931 is not in English; therefore, the effective filing date of the instant application is 03/17/2021.
Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C. 119(a)-(d) prior to declaration of an interference, a certified English translation of the foreign application must be submitted in reply to this action. 37 CFR 41.154(b) and 41.202(e).
Failure to provide a certified translation may result in no benefit being accorded for the non-English application.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 08/12/2025 and 02/13/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Rejections - 35 USC § 103, Obviousness
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 1-6 are rejected under 35 U.S.C. 103 as being unpatentable over Juvonen (Film Formation and Surface Properties of Enzymatically Crosslinked Casein Films; 2010 – cited in the IDS filed on 09/16/2022 – previously cited) in view of Myllarinen (US2015/0148283; Date of Publication: May 28, 2015 – previously cited) and Yokoyama (US2017/0044513; Date of Publication: February 16, 2017 – previously cited).
Juvonen’s general disclosure relates to “The improvement of the properties of sodium caseinate barrier films in potential packaging applications was studied by investigating the effects of enzymatic treatment and plasticizer on the film properties” (see, e.g., Juvonen, abstract). Moreover, Juvonen discloses “oxidoreductases Trametes hirsuta laccase (ThL) and Trichoderma reesei tyrosinase (TrTyr) were compared with transglutaminase for crosslinking of the sodium caseinate molecules in the films and coatings” (see, e.g., Juvonen, abstract).
Regarding claims 1-3 pertaining to a protein crosslinking method and oxidoreductase, Juvonen teaches crosslinking sodium caseinate to form caseinate films through use of the oxidoreductase Trametes hirsute laccase (ThL), which is a multicopper oxidase (see, e.g., Juvonen, Materials, pg. 2206).
However, Juvonen does not teach: a protein deamidase to act on a protein (claim 1); or wherein the protein deamidase is an enzyme that acts on a glutamine residue in a protein (claim 5); or wherein the protein deamidase is protein glutaminase (claim 6).
Myllarinen’s general disclosure relates to a process for producing a casein protein product through treatment with a crosslinking enzyme (see, e.g., Myllarinen, abstract). Moreover, Myllarinen teaches the use of protein glutaminase for crosslinking milk protein (see, e.g., Myllarinen, [0059]). Additionally, Myllarinen teaches that protein glutaminase can be “derived from fungi and bacteria, such as, fungus Trametes hirsute, catalyze the crosslinking between carbohydrates and proteins (oxidation of aromatic compounds and cysteine) with applications in food processing for reduction of allergenicity, for example” (see, e.g., Myllarinen, [0061]).
Regarding claims 1 and 5-6 pertaining to the protein deamidase, Myllarinen teaches that amino acids of animal- and plant-based proteins may be crosslinked by protein glutaminase (see, e.g., Myllarinen, [0003]), wherein protein glutaminase catalyzes the deamidation of protein bound glutamine, and glutamine is converted to glutamic acid (see, e.g., Myllarinen, [0061]).
Yokoyama’s general disclosure relates to “a novel protein deamidase having an activity of directly acting on a side chain amide group of an asparagine residue in a protein to form a side chain carboxyl group and release ammonia” (see, e.g., Yokoyama, abstract). Additionally, Yokoyama teaches the use of a novel protein asparaginase to crosslink proteins so the asparaginase does not compete with transglutaminase, and therefore combinatory use of them provides both the effect of deamidation and the effect of crosslinking (see, e.g., Yokoyama, [0206]).
Regarding claims 1 and 5-6 pertaining to the protein deamidase, Yokoyama teaches “protein glutaminase is the only enzyme that can catalyze deamidation reaction of a high molecular protein without accompanying any side reaction” and “protein glutaminase has high practicality as an enzyme having a high deamidation ability for a high molecular weight protein” (see, e.g., Yokoyama, [0004]).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to crosslink proteins through use of laccase, as taught by Juvonen, and glutaminase, as taught by Myllarinen and Yokoyama. One would have been motivated to do so because Myllarinen teaches that the “protein glutaminase catalyzes the deamination of protein bound glutamine, and glutamine is converted to glutamic acid” (see, e.g., Myllarinen, [0061]) and that amino acids of animal- and plant-based proteins may be crosslinked by protein glutaminase (see, e.g., Myllarinen, [0003]). Moreover, Yokoyama teaches that “protein glutaminase is the only enzyme that can catalyze deamidation reaction of a high molecular protein without accompanying any side reaction” and “protein glutaminase has high practicality as an enzyme having a high deamidation ability for a high molecular weight protein” (see, e.g., Yokoyama, [0004]). Furthermore, it would have been obvious to combine protein glutaminase with laccase, as taught by Juvonen, because Juvonen teaches that laccase has a high redox potential and can efficiently crosslink proteins in the presence of low-molecular-weight phenolic compounds as bridging agents (see, e.g., Juvonen, Introduction, pg. 2206). Additionally, Juvonen teaches that laccase has the ability to crosslink sodium caseinate, similar to glutaminase, as taught by Myllarinen (see, e.g., Juvonen, Conclusions, pg. 2210-2211 & Myllarinen, abstract, [0061]). Therefore, based on the teachings of Juvonen, Myllarinen, and Yokoyama, it would have been obvious to produce a crosslinked protein through use of laccase and glutaminase. One would have expected success because Juvonen, Myllarinen, and Yokoyama all teach methods of enzymatically crosslinking sodium caseinate.
Claims 13-17 are rejected under 35 U.S.C. 103 as being unpatentable over Soeda (JP2000/060431; Date of Publication: February 29, 2000 – cited in the IDS filed on 09/16/2022 previously cited) in view of Myllarinen (US2015/0148283; Date of Publication: May 28, 2015 – previously cited) and Yokoyama (US2017/0044513; Date of Publication: February 16, 2017 – previously cited).
Soeda’s general disclosure relates to “various protein-modified foods such as food materials and processed foods containing a novel enzyme-treated protein”, wherein transglutaminase and an oxidoreductase are used for the modification or treatment of a protein (see, e.g., Soeda, English Translation, [0001]). Moreover, Soeda teaches the treatment of foods with transglutaminase and an oxidoreductase in order to enhance the color, tone, and taste of the food (see, e.g., Soeda, abstract).
Regarding claims 13-15 pertaining to the production of a crosslinked protein, Soeda teaches a protein-containing food product treated with transglutaminase and an oxidoreductase enzyme, wherein the treatments with the two enzymes may be performed simultaneously or separately (see, e.g., Soeda, English Translation, [0018]). Furthermore, in regards to treating the protein-containing food product, Soeda teaches “either one may be treated in advance and the treatments may be sequentially performed, or the treatments may be alternately repeated” (see, e.g., Soeda, English Translation, [0018]).
Regarding claims 16 and 17 pertaining to the protein, Soeda teaches that the protein is contained within food material or processed food (see, e.g., Soeda, English Translation, [0018]).
However, Soeda does not teach: treating a protein with a protein deamidase (claims 13-15).
Myllarinen’s general disclosure is discussed above as it pertains to producing a casein protein product through treatment with a crosslinking enzyme.
Regarding claims 13-15 pertaining to treatment with a protein deamidase, Myllarinen teaches that amino acids of animal- and plant-based proteins may be crosslinked by protein glutaminase (see, e.g., Myllarinen, [0003]), wherein protein glutaminase catalyzes the deamidation of protein bound glutamine, and glutamine is converted to glutamic acid (see, e.g., Myllarinen, [0061]).
Yokoyama’s general disclosure relates to “a novel protein deamidase having an activity of directly acting on a side chain amide group of an asparagine residue in a protein to form a side chain carboxyl group and release ammonia” (see, e.g., Yokoyama, abstract). Additionally, Yokoyama teaches the use of a novel protein asparaginase to crosslink proteins so the asparaginase does not compete with transglutaminase, and therefore combinatory use of them provides both the effect of deamidation and the effect of crosslinking (see, e.g., Yokoyama, [0206]).
Regarding claims 1 and 5-6 pertaining to the protein deamidase, Yokoyama teaches “protein glutaminase is the only enzyme that can catalyze deamidation reaction of a high molecular protein without accompanying any side reaction” and “protein glutaminase has high practicality as an enzyme having a high deamidation ability for a high molecular weight protein” (see, e.g., Yokoyama, [0004]).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce a crosslinked protein with an oxidoreductase and transglutaminase, as taught by Soeda, wherein the transglutaminase is substituted for glutaminase, as taught by Myllarinen. One would have been motivated to do so because Myllarinen teaches that the “protein glutaminase catalyzes the deamination of protein bound glutamine, and glutamine is converted to glutamic acid” (see, e.g., Myllarinen, [0061]) and that amino acids of animal- and plant-based proteins may be crosslinked by protein glutaminase (see, e.g., Myllarinen, [0003]). Moreover, Yokoyama teaches that “protein glutaminase is the only enzyme that can catalyze deamidation reaction of a high molecular protein without accompanying any side reaction” and “protein glutaminase has high practicality as an enzyme having a high deamidation ability for a high molecular weight protein” (see, e.g., Yokoyama, [0004]). Furthermore, it would have been obvious to use an oxidoreductase, as taught by Soeda, along with a glutaminase, as taught by Myllarinen and Yokoyama, because Soeda teaches that the oxidoreductase promotes the function and modification effect exhibited by the transglutaminase; therefore, one of ordinary skill in the art would have a reasonable expectation of success that the oxidoreductase would also promote the function and modification effect exhibited by glutaminase. Therefore, based on the teachings of Soeda, Myllarinen, and Yokoyama, it would have been obvious to produce a crosslinked protein using an oxidoreductase and glutaminase. One would have expected success because Soeda, Myllarinen, and Yokoyama all teach methods of crosslinking protein using enzymes.
Examiner’s Response to Arguments
Applicant's arguments filed 10/31/2025 have been fully considered but they are not persuasive.
Applicant’s arguments regarding the combined teachings of Juvonen, Myllarinen, and Yokoyama not being obvious to the ordinary artisan and that laccase should have been substituted with protein glutaminase (remarks, page 3), this argument is not persuasive because the Broadest Reasonable Interpretation (BRI) (see, e.g., MPEP 2111) of independent claim 1 is contacting a protein with an oxidoreductase and a protein deamidase. Based on the BRI of the instantly claimed invention, laccase should not be substituted for protein glutaminase, but instead be combined with protein glutaminase. Juvonen teaches crosslinking sodium caseinate to form caseinate films through use of the oxidoreductase Trametes hirsute laccase (ThL), which is a multicopper oxidase (see, e.g., Juvonen, Materials, pg. 2206). Myllarinen teaches a process for producing a casein protein product through treatment with a crosslinking enzyme (see, e.g., Myllarinen, abstract). Moreover, Myllarinen teaches the use of protein glutaminase for crosslinking milk protein (see, e.g., Myllarinen, [0059]). Myllarinen teaches that amino acids of animal- and plant-based proteins may be crosslinked by protein glutaminase (see, e.g., Myllarinen, [0003]). Additionally, Myllarinen teaches that protein glutaminase can be “derived from fungi and bacteria, such as, fungus Trametes hirsute, catalyze the crosslinking between carbohydrates and proteins (oxidation of aromatic compounds and cysteine) with applications in food processing for reduction of allergenicity, for example” (see, e.g., Myllarinen, [0061]). Yokoyama was cited as motivation for using a protein glutaminase, wherein Yokoyama teaches “protein glutaminase is the only enzyme that can catalyze deamidation reaction of a high molecular protein without accompanying any side reaction” and “protein glutaminase has high practicality as an enzyme having a high deamidation ability for a high molecular weight protein” (see, e.g., Yokoyama, [0004]). Therefore, based on the teachings of Juvonen, Myllarinen, and Yokoyama, one would have been motivated to combine laccase, as taught by Juvonen, and the protein glutaminase, as taught by Myllarinen and Yokoyama because both of these enzymes exhibit the ability to crosslink protein (see, e.g., Juvonen, Materials, pg. 2206) (see, e.g., Myllarinen, [0003]). Therefore, based on the BRI of the instantly claimed invention, the combined teachings of Juvonen, Myllarinen, and Yokoyama teach contacting a protein with an oxidoreductase (i.e., multicopper oxidase; laccase) and a protein deamidase (i.e., protein glutaminase).
Regarding Applicant’s arguments regarding an ordinary artisan considering it disadvantageous to add low-molecular weight phenolic compounds to promote crosslinking by laccase (remarks, page 3), this argument is not persuasive for multiple reasons:
First, Applicant states that it would have been disadvantageous to add low-molecular weight phenolic compounds as bridging agents to promote crosslinking by laccase, as taught by Juvonen (see, e.g., Juvonen, Introduction, pg. 2206); however, Applicant does not explain why this would be disadvantageous, nor does Applicant provide any evidence as to addition of low-molecular weight phenolic compounds being disadvantageous. MPEP 716.01(c)(II) states that “Arguments presented by the applicant cannot take the place of evidence in the record.” In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965) and In re De Blauwe, 736 F.2d 699, 705, 222 USPQ 191, 196 (Fed. Cir. 1984). Applicant does not provide a persuasive argument that adding a low-molecular weight phenolic compounds as bridging agents to promote crosslinking by laccase is disadvantageous.
Second, for independent claim 1, Applicant uses the transitional phrase “comprising”, which is “inclusive or open-ended and does not exclude additional, unrecited elements or method steps” (see, e.g., MPEP 2111.03). Therefore, low-molecular weight phenolic compounds can be added to promote crosslinking by laccase, as taught by Juvonen, and this can read on the instantly claimed invention. Juvonen teaches that laccase has a high redox potential and can efficiently crosslink proteins in the presence of low-molecular-weight phenolic compounds as bridging agents (see, e.g., Juvonen, Introduction, pg. 2206), which is motivation for including low-molecular-weight phenolic compounds for protein crosslinking.
Regarding Applicant’s argument that there are unexpected results when combining oxidoreductases and protein glutaminase for crosslinking (remarks, page 4), this argument is not persuasive because these results are not commensurate in scope with the claimed invention:
In “Test Example 1”, Applicant is measuring the promotion of protein crosslinking by using laccase in combination with protein glutaminase. However, Applicant is also relying on the addition of egg-derived albumin in an amount of 5% by weight, 50 mM potassium phosphate buffer solution (see, e.g., instant specification, pg. 17, [0037]). Moreover, Applicant is relying on mixing the egg-derived albumin, the potassium phosphate buffer solution, 100 U of laccase, and 500 mU of protein glutaminase, and then allowing the mixture to react at 40oC for 24 hours with being shaken at 160 rpm (see, e.g., instant specification, pg. 17, [0037]). Furthermore, Applicant is relying on fractioning part of the reaction liquid and subjecting it to 2 to 25% polyacrylamide electrophoresis (see, e.g., instant specification, pg. 17, [0037]).
In “Test Example 2”, Applicant is measuring the promotion of protein crosslinking by using laccase in combination with protein glutaminase. However, Applicant is also relying on the addition of LYZAMINE-S (pea protein) in an amount of 5% by weight and 50 mM potassium sodium phosphate buffer (see, e.g., instant specification, pg. 18, [0039]). Moreover, Applicant is relying on mixing LYZAMINE-S, potassium sodium phosphate buffer, 100 U of laccase, and 500 mU of protein glutaminase, and then allowing the mixture to react at 40oC for 24 hours with being shaken at 160 rpm (see, e.g., instant specification, pg. 18, [0039]). Furthermore, Applicant is relying on fractioning part of the reaction liquid and subjecting it to 2 to 25% polyacrylamide electrophoresis (see, e.g., instant specification, pg. 18, [0039]).
Test Examples 1-2 are provided above as examples of the invention not being commensurate in scope with the claimed invention; however, Test Examples 3-12 are also applicable to this argument.
Furthermore, along the same lines, Applicant’s argument that there is no basis provided by Juvonen, Myllarinen, and Yokoyama that a dramatic promotion of crosslinking would be observed by using an oxidoreductase in combination with a protein glutaminase (remarks, page 4), this argument is not persuasive because, as discussed above, Juvonen teaches crosslinking sodium caseinate to form caseinate films through use of the oxidoreductase Trametes hirsute laccase (ThL), which is a multicopper oxidase (see, e.g., Juvonen, Materials, pg. 2206). Myllarinen teaches a process for producing a casein protein product through treatment with a crosslinking enzyme (see, e.g., Myllarinen, abstract). Moreover, Myllarinen teaches the use of protein glutaminase for crosslinking milk protein (see, e.g., Myllarinen, [0059]). Myllarinen teaches that amino acids of animal- and plant-based proteins may be crosslinked by protein glutaminase (see, e.g., Myllarinen, [0003]). Additionally, Myllarinen teaches that protein glutaminase can be “derived from fungi and bacteria, such as, fungus Trametes hirsute, catalyze the crosslinking between carbohydrates and proteins (oxidation of aromatic compounds and cysteine) with applications in food processing for reduction of allergenicity, for example” (see, e.g., Myllarinen, [0061]). Therefore, Juvonen and Myllarinen both teach that laccase and protein glutaminase both have the same activity of crosslinking proteins. One of ordinary skill in the art would readily assume that combining two enzymes that both have the same ability to crosslink proteins would have additive and/or even synergistic effects. Furthermore, Applicant’s arguments of unexpected effects, such as “dramatic promotion of crosslinking”, must be supported by evidence when the art clearly teaches that both laccase and protein glutaminase are useful for the same purpose (see, e.g., MPEP 716.02(a)).
Regarding Applicant’s argument that the disclosure of Myllarinen is erroneous (remarks, page 4), this argument is not persuasive because MPEP 2121.01(II) states “"Even if a reference discloses an inoperative device, it is prior art for all that it teaches." Beckman Instruments v. LKB Produkter AB, 892 F.2d 1547, 1551, 13 USPQ2d 1301, 1304 (Fed. Cir. 1989). Therefore, "a non-enabling reference may qualify as prior art for the purpose of determining obviousness under 35 U.S.C. 103." Symbol Techs. Inc. v. Opticon Inc., 935 F.2d 1569, 1578, 19 USPQ2d 1241, 1247 (Fed. Cir. 1991).” Furthermore, MPEP 2121 states that the prior art is presumed to be operable/enabling and “the burden is on applicant to rebut the presumption of operability. In re Sasse, 629 F.2d 675, 207 USPQ 107 (CCPA 1980)”. Applicant has not provided persuasive arguments that Myllarinen is not enabling. Furthermore is the Applicant’s burden to provide evidence, not just arguments, that the prior art is not enabling (see, e.g., MPEP 716.07 & MPEP 2121). Applicant has not provided evidence that the prior art of Myllarinen is erroneous, and merely stating that “it is a well-known technical matter that protein glutaminase has no cross-linking action by itself” is merely a general statement not backed by art or evidence.
Regarding Applicant’s argument pertaining to the teachings of Soeda (remarks, pages 5-7), this argument is not persuasive because the BRI of independent claim 13 is a method of treating a protein with a protein deamidase and an oxidoreductase. The instantly claimed invention does not explicitly claim that the oxidoreductase needs to be added after the protein deamidase. Instead, based on how the claim is worded, the oxidoreductase can be added at the same time as the protein deamidase because the protein just needs to be subjected to protein deamidation, which can happen if the protein deamidase and oxidoreductase are added at the same time. Therefore, based on the BRI of the instantly claimed invention, the prior teachings of Juvonen, Myllarinen, and Yokoyama could also be applied to these claims. However, the teachings of Soeda were set forth to teach the possible alternative limitation that the protein deamidase needs to be added to the protein before the oxidoreductase. Moreover, Soeda teaches wherein a transglutaminase and an oxidoreductase are used for the modification or treatment of a protein (see, e.g., Soeda, English Translation, [0001]). Additionally, Soeda teaches “either one may be treated in advance and the treatments may be sequentially performed, or the treatments may be alternately repeated” (see, e.g., Soeda, English Translation, [0018]). Therefore, Soeda teaches that the two proteins can be added at different times or at the same time. As discussed previously, Soeda was used as prior art to teach that enzyme treatments can be added at various times to proteins. Moreover, Soeda also teaches the dependent limitations that the protein can be contained within a food product (see, e.g., Soeda, abstract). Furthermore, it would have been obvious to substitute transglutaminase, as taught by Soeda, for protein glutaminase, as taught by Myllarinen because Myllarinen teaches that the “protein glutaminase catalyzes the deamination of protein bound glutamine, and glutamine is converted to glutamic acid” (see, e.g., Myllarinen, [0061]) and that amino acids of animal- and plant-based proteins may be crosslinked by protein glutaminase (see, e.g., Myllarinen, [0003]). Therefore, based on these teachings, it would have been obvious to one of ordinary skill in the art to substitute transglutaminase for protein glutaminase in order to crosslink proteins, as taught by Myllarinen, wherein the oxidoreductase can be added at the same time or separate time, as taught by Soeda.
Conclusion
Claims 1-6 and 13-17 are rejected.
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.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 EST.
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/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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