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 § 102
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 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.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 41 and 48 are rejected under 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over EP 0467482 (Klarenbeek) (cited on IDS filed 07/23/2024).
Klarenbeek discloses a milk protein isolate (MPI) with low calcium content of below 0.4wt% (page 2, lines 40-42; page 3, lines 33-35). The protein content may be more than 90% (page 3, lines 38-39; page 4, lines 3-4) and the composition is subjected to hydrolysis up to a degree of 3.3% (0.7-3.3%). This degree of hydrolysis indicates a high degree of breakage of the proteins into smaller peptides in a manner similar to that illustrated in the instant specification (0.1-1.4%). Thus, it is reasonably expected that the MPI of Klarenbeek comprises less than 79 wt% of peptides having an MW of greater than about 20kDa.
Regarding claim 48, Klarenbeek discloses the MPI in the form of a powder (table on page 4, Example 1).
Claim(s) 42-47 and 49 are rejected under 35 U.S.C. 103 as obvious over EP 0467482 (Klarenbeek) (cited on IDS filed 07/23/2024) in view of US 2014/0179609 (Henle) and EP 1973429 (Blanton) (both cited on IDS filed 07/23/2024).
Klarenbeek discloses a milk protein isolate (MPI) with low calcium content of below 0.4wt% (page 2, lines 40-42; page 3, lines 33-35). The protein content may be more than 90% (page 3, lines 38-39; page 4, lines 3-4) and the composition is subjected to hydrolysis up to a degree of 3.3% (0.7-3.3%). Klarenbeek does not expressly disclose the MW distribution but does disclose a similar hydrolysis degree as that of applicant.
Table 4 of Henle discloses the progression of hydrolyzation of the whey protein and depending upon the length of time of hydrolyzing, the molecular weight (peptide sizes) change. For instance, after 10 minutes, no more than 67.5wt% is above 4kDa and 30.8 wt% is in the range of 24-66 kDa. This is seen to meet the limitation of 20-79wt% is above 20kDa since only 30.8wt% is above 24kDa after 10 minutes. The amounts progressively decrease with the increase in time.
Regarding claim 43, Table 4 shows that the range of 4-24 kDa varies from 8.2-37.5wt% depending upon the amount of time allowed for hydrolyzing the proteins.
Regarding claim 44, after 10 minutes, 31.6wt% of the proteins are 4kDa or less.
Regarding claim 45, after 10 minutes, after 10 minutes, 11.7wt% are 1-4kDa.
Regarding claim 46, after 10 minutes, 7.2wt% have less than 0.175kDa and 12.7wt% from 0.175-1 kDa for a total of 19.9wt%.
Regarding claims 47 and 49, claims 43-46 as discussed above address the amounts claimed.
Note that the instant ranges of kDa use the phrase “about” and have overlap at 20kDa, 5kDa and 1kDa. The ranges of Henle also have overlap at 24, 4, 1 and 0.75 kDa. Henle discloses that as the hydrolyzation time lapses, generally in increase in the smaller MW and decrease in the larger MW is seen. The general amounts disclosed by Henle and the overlap in the ranges are seen to obviate the instant ranges. Further, Blanton discloses that the size of the protein hydrolysates affects taste. Specifically, Blanton explains the protein hydrolysates may have an average weight of about 2000 to about 10,000 Daltons. The protein hydrolysates may have about 67% or less of the proteins having a weight below 6000 Daltons. Embodiments also include protein hydrolysates may have an average weight of about 2000 to about 5000 Daltons. In general, smaller protein hydrolysates tend to have larger Q-values, indicating a higher probability of having a bitter taste. The greater the percentage of the hydrolysate products having smaller molecular weights (e.g., less than about 2000 Daltons) the greater the chance a consumer will notice a bitter taste. As the molecular weight profile data below shows, hydrolysate products with about 45% or less of protein hydrolysates weighing less than 2000 Daltons, have little or no detectable bitterness [0038]. One of ordinary skill in the art would have found it obvious to alter and optimize the MW profile of Klarenbeek by altering the extent of hydrolyzation of the proteins depending upon the desired taste of the product as indicated by Henle and Blanton.
Claim(s) 61 and 62 are rejected under 35 U.S.C. 103 as obvious over EP 0467482 (Klarenbeek) (cited on IDS filed 07/23/2024) in view of WO 03/007730 (Edens).
Klarenbeek discloses hydrolysis using protease enzymes such as one originating from Aspergillis saitoi in order to split the proteins (example 2). Edens discloses hydrolysis of milk proteins and explains that the enzymatic hydrolysis of the whey fraction, the casein fraction or the protein fraction, as present in whole milk, is hydrolyzed with the use of endoproteases only i.e. without the use of any exoproteases. Depending on the pH optimum of the proline-specific endoprotease, the hydrolysis can be carried out in combination with or separate from the other endoprotease. The hydrolysis can be carried out under constant pH or uncontrolled pH conditions. Preferably the hydrolysis is carried out in two steps, firstly the proteins are incubated under neutral or alkaline conditions with an endoprotease with a preference for cleaving proteins at the carboxyterminal side of bulky, hydrophobic amino acid residues. During this hydrolysis the pH drops to acidic values (i.e. below pH 7) and only then the second endoprotease is added, preferably a proline-specific endoprotease, more preferably a proline specific endoprotease obtained from Aspergillus (pages 8-9). Thus, Edens discloses that endoproteases (i.e. endopeptidases) may be used to hydrolyze whey and casein fractions in milk concentrates (page 6) and that endoproteases that have an optimal operation of pH 4-10 (page 7) may be used. This pH range overlaps the claimed range. It would have been obvious to one of ordinary skill in the art to use known endoproteases for hydrolysis of whey and casein at their optimal pHs in the hydrolysis of Klarenbeek to achieve the desired degree of hydrolysis.
Response to Arguments
Applicant’s arguments filed 07/09/2026 regarding the 103 rejections over Havea in view of Tomita and Henle in view of Tomita have been fully considered and are persuasive. These rejections are withdrawn. Applicant’s amendments have overcome the 112(b) rejections of record and the rejections are withdrawn.
Applicant's arguments filed 07/09/2026 regarding the 102/103 rejection over Klarenbeek and 103 rejections over Klarenbeek in view of Henle and Blanton have been fully considered but they are not persuasive.
Applicant argues that the Office action provides no clear basis or technical reasoning that would support a conclusion that Klarenbeek necessarily possesses the claimed molecular weight profile, specifically less than about 79% by weight of peptides have a molecular weight of greater than about 20kDa and takes issue with the terminology “reasonable expectation”. The basis of the rejection relies upon the disclosure of the degree of hydrolysis which is understood to mean the degree of breakage of peptide bonds. Klarenbeek discloses a similar degree of hydrolysis as that of the instant specification, thus one of ordinary skill would expect the result of the hydrolysis (degree of peptide bond breakage) to also be similar. Applicant has not provided any reasoning as to why the degree of hydrolysis is not a reasonable basis to conclude that the degree of peptide bond breakage would be within the range claimed since the material used (milk protein concentrate) and degree of hydrolysis are the same as that disclosed. Applicant discloses partial hydrolysis at levels as low as “less than 0.1%” [0047]. Further, the instant specification explains that peptide includes peptide or protein fragments that have been cleaved via hydrolysis from a longer peptide or protein [0089]. Klarenbeek discloses in the table on page 5 degrees of hydrolysis from the addition of protease (protein splitting enzyme) up to 3.3% which is within the range disclosed by applicant. Additionally, Table 10A of the instant specification indicates a degree of hydrolysis of 1-2%. The protease disclosed by Klarenbeek in Example II originates from Aspergillus saitoi and applicant discloses that the proteolytic enzyme may be derived from Aspergillus sp. [0065]. Based upon the similarity in the material used and the process of hydrolysis, one of ordinary skill would expect the proteins of Klarenbeek to have the resulting protein breakage as claimed. Applicant has not explained why one of ordinary skill, based upon these similarities, would not expect a similar outcome of protein size and amount. Applicant notes that the method of measuring the degree of hydrolysis in Klarenbeek is by the TNBS method, but there is no indication that the methods by which the degree of hydrolysis is measured would affect the measurement obtained to such a degree as to negate the measurement itself.
Applicant argues that the 103 is rebutted because the invention achieved unexpected results. Applicant argues that food products made using the claimed MPC and/or MPI provide high protein content while having reduced viscosity, improved sensory properties and negligible to no increase in undesirable flavours relative to control food products. Applicant did not refer to any specific data in support of this allegation. The specific examples of the instant specification appear to refer to MPC/MPIs with protein contents 50wt% and higher which is not commensurate with claim 41. The amounts of calcium (mg/100g total protein dry basis) of the examples are not commensurate with claim 41. As noted in the rejection of claims 42-47 and 49 over Klarenbeek, Henle and Blanton, it is recognized that progression of hydrolyzation of proteins (whey) and depending upon the length of time of hydrolyzing, the MW peptide size changes. An example where only 10 minutes of hydrolyzing (which Klarenbeek can go up to 130 mins) results in no more than 67.5wt% of peptides above 4kDa and Blanton discloses that the size of the hydrolysates affects taste. Applicant did not address this aspect of the 103 rejections which is seen to obviate the claimed MW profiles.
Newly added claims 61 and 62 have necessitated the new grounds of rejection above.
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JENNIFER C MCNEIL whose telephone number is (571)272-1540. The examiner can normally be reached M-F 9-5.
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JENNIFER C. MCNEIL
Primary Examiner
Art Unit 1723
/Jennifer McNeil/Primary Examiner, Art Unit 1723
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