DETAILED ACTION
Amendments made February 19, 2026 have been entered.
Claims 1-20 are pending;
Claims 2 and 13-20 have been withdrawn.
Election of Species A3 protein glutaminase/enzymatic deamidation, B1 conjugating with a hydrophilic polysaccharide, and C9 salad dressing or sauce or mayonnaise or gravy in the reply filed on September 30, 2025 is acknowledged.
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 .
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.
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.
Notes: “Functional food” ingredient means that in addition to its nutritional properties, the ingredient contributes a non-nutritional property to the food into which it is added, and in particular contributes towards obtaining the desired final characteristics of the food, such as flavor, texture, color, moisture, workability, etc. See instant specification page 2 lines 1-6.
The rejection of claims 1 and 3-10 under 35 U.S.C. 103 as being unpatentable over Deng et al (WO 2012/084624 A1) in view of Yokoyama et al (US 2017/0044513 A1) and Wong et al (“Deamidated wheat protein-dextran Maillard conjugates: Effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH” Food Hydrocolloids 25 (2011) pages 1424-1432) and Bennett et al (WO 2011/014925 A1) has been withdrawn in light of applicant’s amendments made February 19, 2026. Specifically, the claim amendments now require that the two recited processing steps be at a pH of 5 or above instead of encompassing “about 5”.
Claims 1 and 3-10 are rejected under 35 U.S.C. 103 as being unpatentable over Schafer et al (US 2008/0241320) in view of Yokoyama et al (US 2017/0044513 A1).
Regarding claims 1, 3, 7, and 10, Schafer et al (Schafer) teaches a method of preparing a functional food ingredient comprising plant protein (abstract and paragraph 150), wherein the method comprises:
Providing a mixture or slurry of a plant protein in an aqueous solution;
Reacting the plant protein at a pH of 9.0-13.0 for 0.5-24 hours at a temperature of 25-90C to deamidate the protein; and
Cross-linking which is considered to conjugate the plant protein with a hydrophilic polysaccharide including xanthan gum or pectin, to form the functional food ingredient (paragraphs 68, 70, 84, 90-91, 98, 102, 129, 130, 133, 136, 142-144, and claims 1, 10, 11, 30, and 34).
Regarding the cross-linking, i.e. conjugating as at a pH of 5 or above as recited in claim 1, Schafer is not specific to a general pH range for the process. However, as Schafer teaches that the pH of the mixture is adjusting to a value in the range of from 6.0-9.0 and then the cross-linking is performed (paragraphs 130-133), the claimed limitation is considered at least an obvious suggestion of the prior art. For the process step to be performed at the pH that the mixture is adjusted to would have been encompassed or at least obvious to one of ordinary skill in the art. It is additionally noted that as the cross-linking agents disclosed, such as xanthan gum (paragraph 136) were known to have a pH of about 6-8 in aqueous solutions, the addition of the cross-linking agent would not be expected to take the pH value outside of the claimed range. The position is additionally supported as the protein and xanthan gum product in the examples of Schafer has a pH of 6.8 (see Table 6), which is within the claimed range.
Schafer is silent to the deamidation as with a modification agent including protein glutaminase as recited in claim 1.
Regarding the deamidation as with a modification agent including protein glutaminase as recited in claim 1, preferably wherein the reaction step comprises mixing said plant protein with said glutaminase for about 1-24 hours at a temperature of about 20-70C and pH of about 5-10 as recited in claim 7, as discussed above, Schafer teaches a method of preparing a functional food ingredient comprising plant protein comprising: providing a mixture or slurry of plant protein an in aqueous solution; and reacting the plant protein at a pH of 9.0-13.0 for 0.5-24 hours at a temperature of 25-90C to deamidate the protein.
Yokoyama et al (Yokoyama) teaches that deamidation of protein was known to improve various functional properties of protein including solubility, emulsion stability, foam stability (paragraph 2). Yokoyama teaches techniques for deamidation of protein include chemical and enzymatic techniques, however, all chemical deamidations, including acid and alkaline treatment, have problems, and among the enzymes protein glutaminase is considered to have high practicality (paragraphs 3 and 4). Yokoyama teaches the use of protein deamidase with protein glutaminase at 5-80C and a pH of 2-10 for 10 seconds to 48 hours to deamidate a solution of proteins including soy, wheat, rice, etc. to provide improved functional properties including solubility, dispersibility, emulsion stability, and emulsfiability (paragraphs 172, 174, 175, 177, 181, and 183).
It would have been obvious for the plant protein deamidation of Schafer to be with protein glutaminase to form a deamidated protein at 5-80C and a pH of 2-10 for 10 seconds to 48 hours to provide improved functional properties including solubility, dispersibility, emulsion stability, and emulsfiability while avoiding the problems with chemical deamidation in view of Yokoyama.
Regarding claim 4, Schafer teaches that the rice source, i.e. protein source, used is milled rice with rice bran and optionally non-protein materials removed (claim 1) and thus encompasses or at least makes obvious the plant protein as a protein meal, concentrate, or isolate. Also see paragraphs 145-146 and 183-184.
Regarding claims 5 and 6, Schafer teaches that the protein is a rice protein (abstract and claim 1).
Regarding claim 8, Schafer teaches that the cross-linking, i.e. conjugating step, includes forming a solution to which the cross-linking agent is added and heating at about 30-160C for 2-60 hours (paragraphs 84, 90-91, and 133, and claim 30). Regarding the cross-linking, i.e. conjugating, as at a pH of 5-10 as recited in claim 8, Schafer is not specific to a general pH range for the process. However, as Schafer teaches that the pH of the mixture is adjusting to a value in the range of from 6.0-9.0 and then the cross-linking is performed (paragraphs 130-133), the claimed limitation is considered at least an obvious suggestion of the prior art. For the process step to be performed at the pH that the mixture is adjusted to would have been encompassed or at least obvious to one of ordinary skill in the art. It is additionally noted that as the cross-linking agents disclosed, such as xanthan gum (paragraph 136) were known to have a pH of about 6-8 in aqueous solutions, the addition of the cross-linking agent would not be expected to take the pH value outside of the claimed range. The position is additionally supported as the protein and xanthan gum product in the examples of Schafer has a pH of 6.8 (see Table 6), which is within the claimed range.
Regarding claim 9, Schafer teaches that the preferred protein, i.e. functional food, is obtained by centrifugation and ultra-filtration (paragraph 30) and that in processing, the obtained dispersion can be converted after removal of a solvent into a solid using any conventional technology including drying (paragraphs 31, 65, 66, 95, 97, 148, and 159), and thus the claimed limitations are considered encompassed or at least obvious over the teachings of the prior art in order to form a dried and/or concentrated product.
Response to Arguments
Applicant’s arguments with respect to the prior art rejections have been considered but are moot because the new ground of rejection does not rely on any reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument.
Conclusion
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure. US 2009/0311407 teaches protein-polysaccharide conjugates.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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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KELLY BEKKER
Primary Patent Examiner
Art Unit 1792
/KELLY J BEKKER/Primary Patent Examiner, Art Unit 1792
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