DETAILED ACTION
Background
The amendment dated July 10, 2026 (amendment) amending claim 1 has been entered. Claims 1-7, 10 and 12-16 as filed with the amendment have been examined. Claims 8-9 and 11 have been canceled.
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 .
Claim Rejections - 35 USC § 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 1-7, 10 and 12-15 are rejected under 35 U.S.C. 103 as being unpatentable over EP1106696 A1 to Yamaguchi et al. (Yamaguchi) in view of US 20220079187 A1 to Stiles et al. (Stiles), both of record.
The Office interprets claim 1, step (b) as reciting an alkaline treatment, without any material removal step. If the alkaline treatment results in precipitating a solid, then the alkaline treatment results in removing a component from a solution phase but not from the sample of plant protein raw material.
Regarding instant claims 1-2, 4 and 16, Yamaguchi at Abstract discloses a new bacterium of the genus Chryseobacterium (claim 4) that produces a deamidase enzyme, wherein at [0072] a method of using the deamidase comprises treating a cereal or bean (“(a) treating a sample comprising a plant protein raw material”…”in an enzyme reaction solution”) comprising soybeans (claim 2) to improve later protein extraction comprising (at [0073]) suspending soybean powder in a dilute alkali solution and then removing insoluble substances (“(b) after completing the enzymatic deamidation in step (a) performing an alkaline treatment by adjusting the pH of the enzyme reaction solution to 9 to 12, thereby separating the enzyme reaction solution into soluble components containing proteins and insoluble components, and subsequently removing the insoluble components” and “(c) recovering the proteins from the separated soluble components”).
Further and regarding instant claims 10, 12 and 14, the deamidase activity disclosed in Yamaguchi at Example 5 for the Chryseobacterium culture indicates activity at (see Table 4 on page 16) at a pH of 8.65 (claims 1 and 16). Further, the Yamaguchi process disclosed at [0073] produces soybean protein concentrate or isolate (claim 14), followed by insolubilizing the protein in an isoelectric point treatment at a pH around 4.5 (“(c) recovering proteins from the separated soluble components” as in claims 10 and 12). The ordinary skilled artisan would at least have found it obvious in Yamaguchi to treat its sample comprising a plant protein raw material at a pH of 7 to 9 as in claim 1 or a pH of 8 to 9 as in claim 16 because Yamaguchi discloses that the deamidase in its cultures at that pH produces a desirable enzyme activity.
Further, and regarding instant claims 5 and 7, Yamaguchi does not disclose its (b) alkaline treatment as being performed at a pH of from 9 to 12 as in claim 1, and does not disclose (d) subjecting recovered proteins to a neutralization process; further, Yamaguchi does not disclose that its Chryseobacterium microorganism is a Chryseobacterium proteolyticum as in claim 5; further, Yamaguchi does not disclose that the concentration of its plant protein raw material in its sample is from 10 to 35 wt% as in claim 7. However, Yamaguchi at [0009] discloses that its deamidase removes amide groups from glutamine and asparagine and thereby creates negatively charged carboxyl groups wherein the protein is solubilized. Further, at [0072] Yamaguchi discloses bean and cereal flours in general as substrates and does not limit the concentration of a plant protein raw material in a deamidase substrate.
Stiles at [0147]-[0155] discloses generally refining or isolating plant proteins from a plant protein raw material, including (at [0156]) soybeans. Further, at [0161] Stiles discloses generally that in refining precipitation pH is the opposite pH for extraction to allow for precipitation. In alkaline treatment for extraction, Stiles discloses at [0158] extraction at a pH of at least 9, at least 10 and at least 11. In addition, at [0172]-[0173] and Example 1 Stiles discloses adding protein glutaminase to deamidate a refined protein wherein the starting refined protein has a pH neutralized to 7.0 adding alkali as NaOH to pea flour in a solid concentration of 20% wt/wt plant protein raw material in water for deamidase treatment. In general, Stiles discloses a pH of a refined protein of from 5 to 7 arrived at by pH adjustment such as with NaOH. In addition, Stiles at [0104] particularly discloses a protein glutaminase from a Chryseobacterium proteolyticum.
Before the effective filing date of the present invention, the ordinary skilled artisan would have found it obvious in view of Stiles for Yamaguchi in its alkaline treatment to subject its plant protein raw material to an alkaline treatment at a pH of from 9 to 12 as in Stiles in claim 1 or at a pH of 10 to 11 as in claim 16, and to neutralize its protein product that is recovered from acidic precipitation to neutralization as in Stiles. In addition, the ordinary skilled artisan in Yamaguchi would have found it obvious in view of Stiles to treat its protein at a raw material concentration of from 10 to 35% (w/w) of the reaction as in Stiles to optimize deamidation and, further, to propagate a Chryseobacterium proteolyticum as in Stiles as its Chryseobacterium to produce deamidase. Both references are drawn to methods of refining or purifying plant proteins in aqueous media using alkali and acid to effect isoelectric protein precipitation from other raw materials and to methods for treating a plant protein raw material with a deamidase from Chryseobacterium. The ordinary skilled artisan working in Yamaguchi would have desired to optimize its method of protein extraction by performing an alkali treatment at pH of 9-11 and from a pH of 10-11 as in Stiles to optimize dissolution of proteins, particularly as Yamaguchi refines a deamidated protein that has additional acid groups that are dissolved at a basic pH. In addition, the ordinary skilled artisan in Yamaguchi would have desired to neutralize its acidic protein concentrate as in Stiles to carboxylate it and render it more easily dispersed or dissolved in liquid when used in a food or beverage. And the ordinary skilled artisan in Yamaguchi would have desired in view of Stiles to treat its plant protein raw material at a pH of from 10 to 35% (w/w) as in Stiles and use a Chryseobacterium proteolyticum as its Chryseobacterium species as in Stiles to optimize its deamidation and to efficiently produce its deamidase for deamidation.
Regarding instant claim 3, Yamaguchi discloses at [0068] that its enzyme is a glutaminase enzyme.
Regarding instant claim 6, Yamaguchi at [0060] discloses an amount of the protein deamidase of 0.1 to 100 units per gram of plant protein raw material.
Regarding instant claim 13, Yamaguchi at [0062] discloses that its plant proteins are used as a tempura powder or as dried.
Regarding instant claim 15, Yamaguchi at [0073] discloses food products such as ham, sausages and baby food.
Response to Arguments
In view of the amendment dated July 10, 2026, the following rejections have been withdrawn as moot:
The rejections of claims 1-7, 10 and 12-16 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite in regard to the claim 1 term (b) “removing components other than proteins from the sample by performing an alkaline treatment”.
The positions taken in the remarks accompanying the amendment dated July 10, 2026 (Reply) have been fully considered but they are not found persuasive for the following reasons:
Regarding the position taken in Reply that the cited portion of Yamaguchi in Example 5 relates to a culture of a deamidase producing bacteria, the Office agrees; however, it is also true that the medium culture in Example 5 of Yamaguchi is tryptone soya which is a plant protein raw material as claimed. Further, the Office considers the claimed treating a sample comprising a plant protein raw material and water to include the deamidated plant protein raw material in a culture containing the bacteria in Example 5 in Yamaguchi.
Regarding the position taken in the Reply that the data show criticality of treating a plant protein raw material with protein deamidase at a pH of 7 to 9 over the art of Yamaguchi, including for the reason that Yamaguchi at [0056] discloses optimum pH for its enzyme activity at a pH of 6 and has no appreciation of the claimed treating at a pH of 7 to 9, respectfully the Office disagrees. Taking the second position first, the Office finds that the optimum pH disclosed in Yamaguchi is only a preferred pH; however, the disclosure of a preferred thing is not a teaching away from the rest of a disclosure and the disclosure of Yamaguchi is not limited to its optimum pH. As it turns out, Yamaguchi at [0060] discloses reaction conditions for its protein deamidase and its substrate of a pH of from 4 to 8, which the claimed pH of 7 to 9 in claim 1 overlaps, and with which the claimed pH of 8 to 9 in claim 16 coincides at a pH of 8. In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art", the Office considers that a prima facie case of obviousness exists. See MPEP 2144.05.I. The ordinary skilled artisan skilled in Yamaguchi would have appreciated and found it obvious to treat its plant protein raw material with a deamidase at the claimed pH because Yamaguchi discloses that the claimed pH provides a desirable deamidated plant protein raw material product.
Regarding the alleged criticality of the claimed treating with a protein deamidase at a pH of 7 to 9, the Office finds that Yamaguchi at [0060] discloses a pH of 4 to 8 which is within the alleged critical range. Yamaguchi cannot be limited to its preferred pH no proper comparison has been made to the art of Yamaguchi. Even if an optimum pH in Yamaguchi is found to be a pH of 6, the Applicants offer only data in Table 2 of the instant specification showing protein yields from a pH in treatment of 7, 8 and 9, all of which are within the claimed range. However, no comparison has been made. And, as Applicants state Yamaguchi boasts of better results at a pH 6. Nevertheless, no comparison to the closest art of Yamaguchi has been made! And, thus no proper showing has been made that the claims are unobvious over the art.
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 ANDREW E MERRIAM whose telephone number is (571)272-0082. The examiner can normally be reached M-H 8:00A-5:30P and alternate Fridays 8:30A-5P.
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/ANDREW E MERRIAM/Examiner, Art Unit 1791
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