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 .
Claim status
Claims 1-8, 10-13 and 17-20 filed 10/08/2024 are pending in the application and are hereby examined on the merits.
Claim Objections
Claim 1 is objected to because of the following informalities: “providing a protein-containing composition, wherein the proteins of the protein-containing composition comprise” should read “providing the protein-containing composition, wherein the protein of the protein-containing composition comprises”. Claim 11 is objected to for the same reason. Appropriate correction is required.
Claim 4 is objected to because of the following informalities: “wherein the transglutaminase is contacted” should read “wherein the at least one transglutaminase is contacted”. Appropriate correction is required.
Claim 5 is objected to because of the following informalities: “wherein the transglutaminase is allowed” should read “wherein the at least one transglutaminase is allowed”. Appropriate correction is required.
Claim 7 is objected to because of the following informalities: “wherein the proteins of the cross-linked protein-containing composition comprise” should read “wherein the protein of the cross-linked protein-containing composition comprises”. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-6, 11-13 and 17-20 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites a process for treating a protein-containing composition “comprising the steps consisting of” step a) and b). It is not clear whether the process comprises or consists of the steps. Claim 11 is rejected for the same reason. Claims 2-6 depends from claim 1 thus necessarily incorporate the indefinite subject matter therein. Claims 12-13 and 17-20 depend from claim 11 thus necessarily incorporate the indefinite subject matter therein. Appropriate correction is required.
Claim 11 recites “wherein the proteins of the dairy product or the alternative thereof comprise milk proteins” in line 2-3. There is insufficient antecedent basis for the limitation “the proteins”. Claims 12-13 and 17-20 depend from claim 11 thus necessarily incorporate the indefinite subject matter therein. Appropriate correction is required.
Claim Rejections - 35 USC § 102
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.
Claims 1-2, 5, 7 and 10 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Villas-Boas, “The effect of transglutaminase-induced polymerization in the presence of cysteine on b-lactoglobulin antigenicity”, International Dairy Journal 20 (2010) 386–392.(cited in the IDS submitted 10/08/2024, hereinafter referred to as Villas-Boas).
Regarding claims 1-2, 5, 7 and 10, Villas-Boas teaches a process of treating a composition that contains milk protein (e.g., beta-lactoglobulin), the process comprises treating the composition with transglutaminase at a temperature of 50 °C for 180 min in the presence of cysteine to obtain a cross-linked (e.g., polymerized) milk protein-containing composition, wherein the composition is liquid, wherein the milk protein comprises at least 90% beta-lactoglobulin (e.g., a purity of >95%), and wherein the composition comprises at least 2% milk protein (e.g., 7% w/v) (abstract; page 387, 2.1 and 2.2). Villas-Boas teaches that a dimer of the beta-lactoglobulin is formed as a result of polymerization, which has a MW of 36.8 kDa (Fig. 1). Villas-Boas teaches that the polymerization of beta-lactoglobulin reduces the potential allergenicity of the beta-lactoglobulin (Abstract; Conclusion).
Claim Rejections - 35 USC § 103
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.
Claims 4, 6 and 8 are rejected under 35 U.S.C. 103 as being unpatentable over Villas-Boas as applied to claims 1 and 7 above.
Regarding claim 4, Villas-Boas teaches what has been recited above but is silent regarding that the weight ratio of milk protein to transglutaminase is 20:1 to 1000:1. However, Villas-Boas teaches that the transglutaminase is added at a dosage of 25 U per gram of beta-lactoglobulin substrate (page 387, 2.2). Further, the amount of an enzyme (e.g., transglutaminase) in an enzymatic is the general condition known by one of ordinary skill in the art to affect the amount of degree of crosslinking or polymerization of the protein substrate. Therefore, a skilled person would have been motivated to manipulate the amount of enzyme by weight of the protein substrate so as to ensure an optimal polymerization reaction. As such, the ratio as recited in claim 4 is merely an obvious variant of the prior art. Note that claim 4 recites a very broad range for the ratio of milk protein to transglutaminase. Generally, differences in concentration or temperature will not support the patentability of the subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 “Where 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”. (See MPEP 2144.05 II).
Regarding claims 6 and 8, Villas-Boas teaches that the source material of beta-lactoglobulin has a purity of 95% (page 387, 2.1) thus does not explicitly teach that beta-lactoglobulin is the only milk protein in the composition. However, the gist of Villas-Boas is to study the effect of polymerization by the enzyme transglutaminase (TG) on the antigenicity of beta-lactoglobulin only, therefore, a skilled artisan would have been motivated to use a source material that has beta-lactoglobulin only so as to eliminate any noise brought by other milk protein.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Villas-Boas as applied to claim 1 above, and further in view of Nielsen WO 2020/001765 A1 (hereinafter referred to as Nielsen).
Regarding claim 3, Villas-Boas teaches what has been recited above but is silent regarding adding at least one fat component to the composition that contains beta-lactoglobulin.
Nielsen teaches a method of making a heat-treated beverage preparation, the method comprising mixing beta-lactoglobulin with fat, carbohydrate (e.g., sucrose) and calcium followed by homogenization and heat treatment to obtain the heated beverage preparation (page 2, line 10-14; Example 3; Example 14).
Both Villas-Boas and Nielsen are directed to beta-lactoglobulin. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Villas-Boas by mixing the polymerized beta-lactoglobulin with a fat component, carbohydrate and calcium followed by homogenization and heat treatment so as to obtain a heated beverage preparation. One of ordinary skill in the art, before the effective filing date of the claimed invention, would have had a reasonable expectation of success for doing so because prior art has established that a beverage preparation can be made by combing beta-lactoglobulin, fat, carbohydrate and calcium.
Villas-Boas in view of Nielsen differs from claim 3 in that prior art teaches adding fat after cross-linking as opposed to before cross-linking. However, the selection of any order of mixing ingredients is prima facie obvious in the absence of convincing arguments or evidence that the claimed order provides an unexpected result. (See MPEP 2144.04 IV). Further, selection of any order of performing process steps is prima facie obvious in the absence of new or unexpected results. See In re Burhans, 154 F.2d 690, 69 USPQ 330 (CCPA 1946) (See MPEP 2144.04 IV). In the instant case, it does not appear that adding fat before cross-linking would result in a different product from adding fat after cross-linking since the transglutaminase does not digest fat.
Claims 11-13, 17-18 and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Nielsen WO 2020/001765 A1 (hereinafter referred to as Nielsen) in view of Villas-Boas, “The effect of transglutaminase-induced polymerization in the presence of cysteine on b-lactoglobulin antigenicity”, International Dairy Journal 20 (2010) 386–392.(cited in the IDS submitted 10/08/2024, hereinafter referred to as Villas-Boas).
Regarding claims 11-13, 17-18 and 20, Nielsen teaches a method of producing a heat-treated beverage preparation, the method comprising mixing beta-lactoglobulin solution with fat, carbohydrate (e.g., sucrose) and calcium followed by homogenization and heat treatment to obtain the heated beverage preparation (page 2, line 10-14; Example 3; Example 14). Nielsen teaches that beta-lactoglobulin is from mammal species, e.g., in native, unfolded and/or glycosylated forms and includes the naturally occurring genetic variants (page 4, line 4-6). Nielsen teaches that at least 85% (for example, at least 92%, at least 96% and most preferably approx., 100%) of the protein in the beverage preparation is beta-lactoglobulin (page 15, line 1-10). Nielsen teaches that starch (e.g., modified or resistant), guar gum, konjac flour, etc. can also be incorporated in the beverage preparation (page 29, line 11-18), thus reading on the texturizing agent as recited in claim 12.
Nielsen is silent regarding the step of treating the beta-lactoglobulin with transglutaminase to obtain cross-linked beta-lactoglobulin.
Villas-Boas teaches a process of treating a composition that contains milk protein (e.g., beta-lactoglobulin), the process comprises treating the composition with transglutaminase at a temperature of 50 °C for 180 min in the presence of cysteine to obtain a cross-linked (e.g., polymerized) milk protein-containing composition, wherein the composition is liquid, and wherein the milk protein comprises at least 90% beta-lactoglobulin (e.g., a purity of >95%) (abstract; page 387, 2.1 and 2.2). Villas-Boas teaches that a dimer of the beta-lactoglobulin is formed as a result of treatment with transglutaminase, which has a MW of 36.8 kDa (Fig. 1). Villas-Boas teaches that the polymerization of beta-lactoglobulin reduces the potential allergenicity of the beta-lactoglobulin (Abstract; Conclusion).
Both Nielsen and Villas-Boas are directed to beta-lactoglobulin. It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Nielsen by subjecting the beta-lactoglobulin of Nielsen to the polymerization step as disclosed by Villas-Boas so as to reduce the potential allergenicity of the beta-lactoglobulin.
Claim 19 is rejected under 35 U.S.C. 103 as being unpatentable over Nielsen in view of Villas-Boas as applied to claim 11 above, and further in view of Geistlinger US Patent Application Publication No. 2022/0211061 A1 (hereinafter referred to as Geistlinger).
Regarding claim 19, Nielsen teaches that the beta-lactoglobulin is from mammal species thus being silent regarding recombinant beta-lactoglobulin. What Nielsen teaches is that naturally occurring genetic variants of beta-lactoglobulin can be used (page 4, line 4-6).
Geistlinger teaches a recombinant beta-lactoglobulin that is at least 80% identical to bovine beta-lactoglobulin, and such a recombinant beta-lactoglobulin can be advantageously used in a food or a beverage since it is more soluble and less allergenic than its native form (0006; 0014-0020; 0047; 0089; 0111; 0121).
It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to have modified Nielsen by at least partially substituting the recombinant beta-lactoglobulin as disclosed by Geistlinger for the beta-lactoglobulin of Nielsen with reasonable expectation of success, for the reason that Geistlinger teaches a recombinant beta-lactoglobulin that is at least 80% identical to bovine beta-lactoglobulin, and such a recombinant beta-lactoglobulin can be advantageously used in a food or a beverage since it is more soluble and less allergenic than native form.
Conclusion
Pertinent art
The prior art made of record and not relied upon is considered pertinent to applicant’s disclosure
Tanimoto "Enzymatic modification of proteins: effect of transglutaminase cross-linking on some of physical properties of beta-lactoglobulin", J. Agric. Food Chem. 1988, 36, 281-285, which teaches cross-linking beta-lactoglobulin with transglutaminase in the presence of DTT.
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/CHANGQING LI/Primary Examiner, Art Unit 1791
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