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 the Application
Receipt of the Responses and Amendments after Non-Final Office Action filed 07/08/2026 and 07/09/2026 is acknowledged.
Applicant has overcome the following rejections by virtue of the amendment or cancellation of the claims and/or persuasive remarks: (1) the 35 U.S.C. 102(a)(1) rejections of claims 1-6 over Bishop et al. have been withdrawn; and (2) the 35 U.S.C. 102(a)(1) rejection of claim 7 over Bishop et al. as evidenced by Logie et al. has been withdrawn.
The status of the claims upon entry of the amendments filed on 07/08/2026 and 07/09/2026 stands as follows:
Pending claims: 1-16
Withdrawn claims: None
Previously canceled claims: None
Newly canceled claims: None
Amended claims: 1, 12
New claims: 17-19
Claims currently under consideration: 1-19
Currently rejected claims: 1-19
Allowed claims: None
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.
Claims 1-9 and 12-19 are rejected under 35 U.S.C. 103 as being unpatentable over Bishop et al. (U.S. 5,834,232) in view of During et al. (U.S. 10,383,345 B2).
Regarding claim 1, Bishop et al. discloses a “preparation” (i.e., a composition) comprising at least one high molecular rapeseed protein and transglutaminase (C9, L26-L29, where “rape seed protein” is interpreted as encompassing all proteins that occur in the plant, which would thus include at least one high molecular rapeseed protein).
The statement that the preparation is “for the production of a plant protein-containing food” is considered a statement of intended use that does not structurally limit the claimed preparation, and thus need not be disclosed in the prior art. MPEP 2111.02 II (“During examination, statements in the preamble reciting the purpose or intended use of the claimed invention must be evaluated to determine whether or not the recited purpose or intended use results in a structural difference (or, in the case of process claims, manipulative difference) between the claimed invention and the prior art.”). Nonetheless, Bishop et al. discloses the mixture as forming a plant protein-containing food (C9, L23-L41).
Bishop et al. does not disclose the preparation as comprising low molecular weight rapeseed protein in an amount not more than 30 wt.% of the content of the high molecular weight rapeseed protein, or the high molecular weight rapeseed protein as having a weight average molecular weight of not less than 15,000.
However, During et al. discloses isolation of cruciferin from rapeseed (C2, L31-L33; L50-L52; C3, L35-L38), where cruciferin has a molecular weight of 300 kDa (C8, L22-L25).
It would have been obvious to one having ordinary skill in the art to utilize the purified cruciferin protein product of During et al. in the composition of Bishop et al. Since Bishop et al. discloses broadly that transglutaminase may be added to “rape seed protein” (C9, L23-L29) without providing additional clarification, a skilled practitioner would be motivated to consult During et al. for clarification regarding suitable proteins. Since During et al. discloses cruciferin protein as being suited for use as a functional food product (C5, L4-L9; L25-L26) and Bishop et al. discloses the transglutaminase treatment is useful “to improve the functional properties of proteinaceous foods” (C9, L23-L26), the incorporation of purified cruciferin (which has a weight average molecular weight of not less than 15,000) into the composition of Bishop et al. would be obvious. Such a protein isolate would have a content of a low molecular weight rapeseed protein of not more than 30 wt.%.
As for claims 2-6, the claim limitations are directed to the intended use of the preparation and do not structurally limit the claimed composition. As such, the disclosure of Bishop et al. as modified by During et al. is sufficient to render the claims obvious.
As for claim 7, During et al. discloses the high molecular weight rapeseed protein is rapeseed globulin (C8, L21-L22; C1, L21).
Regarding claim 8, Bishop et al. and During et al. disclose the preparation of claim 1.
The cited prior art does not explicitly disclose the high molecular rapeseed protein as being at a concentration of 50.0-99.9 wt.% of the preparation.
However, Bishop et al. discloses “transglutaminase is added to such foodstuffs as…rape seed protein” (C9, L26-L29), which suggests that the amount of protein may range from 100% to some amount less than 100%. Bishop et al. also discloses: “The ratio of gelatin:transglutaminase will generally be within the range of 1320:1 to 20:1 by weight” (C7, L51-L53), which would be roughly 95.25% protein : 4.75% transglutaminase. MPEP 2144.04 IV C states: “Selection of any order of mixing ingredients is prima facie obvious.” Addition of transglutaminase to the protein at a concentration within the disclosed ratio, prior to the addition of any other ingredients or dilution with water, would result in a mixture having a protein concentration within the claimed range, which renders the range of a high molecular weight rapeseed protein concentration of 50.0 wt.% to 99.9 wt.% obvious.
As for claim 9, Bishop et al. and During et al. disclose the preparation of claim 1.
The cited prior art does not explicitly disclose the transglutaminase concentration as being in an amount of 0.01-1,000 U/g of the preparation.
However, Bishop et al. does teach: “The ratio of gelatin:transglutaminase will generally be within the range of 1320:1 to 20:1 by weight” (C7, L51-L53). Bishop et al. also states: “The concentration of transglutaminase within the solution will typically be from 0.125 mg/ml to 2.0 mg/ml, preferably at least 0.5 mg/ml, although the concentration can be adjusted to provide gels with low melting points or very high or low tensile strength.” (C7, L54-L58).
Although Bishop et al. does not disclose the transglutaminase concentration in terms of units per gram of the mixture, Bishop et al. effectively discloses the transglutaminase as being a result-effective variable subject to optimization depending on the desired characteristics of the resultant gelled product. MPEP 2144.05 II. The disclosed range of 0.125-2.0 mg/ml and the fairly broad range of concentrations relative to the protein of 1320:1 to 20:1 also likely overlap the similarly broad claimed range of 0.01-1,000 U/g of the preparation, even though the concentrations are expressed in different terms, with both ranges thought to essentially include all values ranging from the minimal effective value in terms of enzymatic activity to a maximal concentration that would likely be excessive. For all these reasons, the claimed range of 0.01-1,000 U of transglutaminase per gram of preparation is considered obvious to a skilled practitioner.
Regarding claim 12, Bishop et al. discloses a method for producing a plant protein-containing food comprising combining at least one high molecular weight rapeseed protein and transglutaminase (C9, L26-L29, where “rape seed protein” is interpreted as encompassing all proteins that occur in the plant, which would thus include at least one high molecular rapeseed protein).
Bishop et al. does not explicitly disclose combining foodstuffs recited in the list of suitable foodstuffs (C9, L26-L30) or a content of low molecular weight rapeseed protein in the plant protein-containing food as being an amount not more than 75 wt.% of the content of the high molecular weight rapeseed protein in the plant protein-containing food, or the high molecular weight rapeseed protein as having a weight average molecular weight of not less than 15,000.
However, MPEP 2144.06 I states: “It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art.” Thus, combining foodstuffs in the recited list would be obvious, such that a method comprising adding the high molecular rapeseed protein and transglutaminase to a plant protein-containing composition, such as soy protein, wheat protein, or potato protein (C9, L28-L29), would be obvious.
Also, During et al. discloses isolation of cruciferin from rapeseed (C2, L31-L33; L50-L52; C3, L35-L38), where cruciferin has a molecular weight of 300 kDa (C8, L22-L25).
It would have been obvious to one having ordinary skill in the art to utilize the purified cruciferin protein product of During et al. in the composition of Bishop et al. Since Bishop et al. discloses broadly that transglutaminase may be added to “rape seed protein” (C9, L23-L29) without providing additional clarification, a skilled practitioner would be motivated to consult During et al. for clarification regarding suitable proteins. Since During et al. discloses cruciferin protein as being suited for use as a functional food product (C5, L4-L9; L25-L26) and Bishop et al. discloses the transglutaminase treatment is useful “to improve the functional properties of proteinaceous foods” (C9, L23-L26), the incorporation of purified cruciferin (which has a weight average molecular weight of not less than 15,000) into the composition of Bishop et al. would be obvious. Such a protein isolate would have a content of a low molecular weight rapeseed protein of not more than 75 wt.%.
As for claim 13, Bishop et al. discloses the plant protein-containing food as being a soybean protein-containing food (C9, L28).
As for claim 14, During et al. discloses the high molecular weight rapeseed protein is rapeseed globulin (C8, L21-L22; C1, L21).
As for claim 15, the previous rationale detailed in relation to claim 12 showed that combining the foodstuffs in the list at column 9, lines 27-29, would be obvious, including combining rape seed protein with any of soy protein, wheat protein, or potato protein. Combining proteins in any relative amount would be obvious, especially equal amounts of each, which renders the claimed relative concentration range of 0.0001-5 g high molecular rapeseed protein to 1 g of the remaining plant protein obvious.
As for claim 16, Bishop et al. and During et al. disclose the method of claim 12.
The cited prior art does not explicitly disclose the transglutaminase concentration as being in an amount of 0.01-1,000 U/g of the plant protein in the plant-containing food.
However, Bishop et al. does teach: “The ratio of gelatin:transglutaminase will generally be within the range of 1320:1 to 20:1 by weight” (C7, L51-L53). Bishop et al. also states: “The concentration of transglutaminase within the solution will typically be from 0.125 mg/ml to 2.0 mg/ml, preferably at least 0.5 mg/ml, although the concentration can be adjusted to provide gels with low melting points or very high or low tensile strength.” (C7, L54-L58).
Although Bishop et al. does not disclose the transglutaminase concentration in terms of units per gram of the mixture, Bishop et al. effectively discloses the transglutaminase as being a result-effective variable subject to optimization depending on the desired characteristics of the resultant gelled product. MPEP 2144.05 II. The disclosed range of 0.125-2.0 mg/ml and the fairly broad range of concentrations relative to the protein of 1320:1 to 20:1 also likely overlap the similarly broad claimed range of 0.01-1,000 U/g of the plant protein, even though the concentrations are expressed in different terms, with both ranges thought to essentially include all values ranging from the minimal effective value in terms of enzymatic activity to a maximal concentration that would likely be excessive. For all these reasons, the claimed range of 0.01-1,000 U of transglutaminase per gram of plant protein is considered obvious to a skilled practitioner. The plant protein other than the high molecular rapeseed protein is not required to be at any minimal amount, such that the relative concentration of transglutaminase to the high molecular rapeseed protein may roughly equivalent to the relative concentration of transglutaminase to the plant protein overall.
As for claim 17, During et al. discloses isolation of cruciferin from rapeseed to a purity of at least 99% (C2, L31-L33; L50-L52; C3, L35-L38), which would render the low molecular weight rapeseed protein as comprising not more than 30 wt.% of the content of the high molecular weight rapeseed protein in the plant protein-containing food.
As for claim 18, During et al. discloses isolation of cruciferin from rapeseed to a purity of at least 99% (C2, L31-L33; L50-L52; C3, L35-L38), which renders a purity of 100% obvious. The production of a preparation according to claim 1 that does not contain a low molecular weight rapeseed protein would thus be obvious.
As for claim 19, During et al. discloses isolation of cruciferin from rapeseed to a purity of at least 99% (C2, L31-L33; L50-L52; C3, L35-L38), which renders a purity of 100% obvious. The production of a plant protein-containing food according to claim 12 that does not contain a low molecular weight rapeseed protein would thus be obvious.
Claims 10 and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Bishop et al. (U.S. 5,834,232) in view of During et al. (U.S. 10,383,345 B2) as applied to claim 1, and further in view of Baumer et al. (U.S. 2005/0220979 A1).
Regarding claim 10, Bishop et al. and During et al. disclose the preparation of claim 1.
The cited prior art does not specifically disclose the preparation as further comprising a dietary fiber, a fine powder textured protein, or a texture starch.
However, Baumer et al. discloses a fine powder textured soy protein product ([0021]).
It would have been obvious to one having ordinary skill in the art to combine a fine powder textured protein as taught in Baumer et al. with the composition of Bishop et al. First, Bishop et al. teaches a list of protein-containing food products that may be prepared but does not explicitly disclose combining those foodstuffs (C9, L26-L30). However, MPEP 2144.06 I states: “It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art.” Thus, combining foodstuffs in the recited list would be obvious, such that a mixture comprising high molecular rapeseed protein and a plant protein, such as soy protein, wheat protein, or potato protein (C9, L28-L29), would be obvious. Since Bishop et al. does not provide any details regarding the preparation of such protein products, a skilled practitioner would be motivated to consult Baumer et al. for specific instruction. The teaching in Baumer et al. that a fine soy powder may be used in a variety of food products, including beverages and meat products ([0021]), renders the combination of fine soy powder textured protein as taught in Baumer et al. with the high molecular rapeseed protein product of Bishop et al. obvious to a skilled practitioner.
As for claim 11, Baumer et al. discloses the fine powder textured protein as having an average particle size of not more than 2,500 µm (specifically, 1-5 µm) ([0021]).
Response to Arguments
NOTE: The Remarks filed 07/09/2026 were only regarding the clarifying amendments of new claims 18 and 19. All substantive arguments appeared in the Remarks filed 07/08/2026, which is the document referred to in all subsequent citations herein.
Claim Rejections - 35 U.S.C. § 102(a)(1) of claims 1-6 over Bishop et al.; and claim 7 over Bishop et al. as evidenced by Logie et al.: Applicant has overcome the 35 U.S.C. § 102(a)(1) rejections of claims 1-7 based on amendments to the claims. Accordingly, the 35 U.S.C. § 102(a)(1) rejections have been withdrawn.
However, claims 1-7 are newly rejected under 35 U.S.C. § 103.
Claim Rejections - 35 U.S.C. § 103 of claims 8, 9, 12, 13, 15, and 16 over Bishop et al.; claims 10 and 11 over Bishop et al. and Baumer et al.; and claim 14 over Bishop et al., and Logie et al.: Applicant’s arguments have been fully considered but they are not persuasive.
Applicant first argued that the cited prior art does not disclose that a high molecular weight rapeseed protein would have a superior effect compared to a low molecular weight rapeseed protein (Applicant’s Remarks, p. 7, ¶5). Applicant asserted that a patty-like food had a superior hardness when comprising high molecular weight rapeseed protein compared to low molecular weight rapeseed protein (Applicant’s Remarks, p. 8, ¶1).
However, the claim rejections have been updated to account for the new claim limitations. MPEP 2145 II states: “Mere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention.” That Applicant may have recognized a desirable attribute of high molecular weight rapeseed protein in a certain application does not render the composition nonobvious. Further, the asserted data is much narrower in scope than the present claims. No evidence is apparent that the asserted results would occur over the entire scope of the claims, which undermines the argument. MPEP 716.02(d). Applicant’s arguments are unpersuasive.
The rejections of claims 8, 9, 12, 13, 15, and 16 have been updated and maintained herein.
Conclusion
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.
Claims 1-19 are rejected.
No claims are allowed at this time.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JEFFREY P MORNHINWEG whose telephone number is (571)270-5272. The examiner can normally be reached 8:30AM-5:00PM.
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/JEFFREY P MORNHINWEG/Primary Examiner, Art Unit 1793
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