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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on September 30, 2025 has been entered.
Claims 1-16 and 18-24 are pending.
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.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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 1-16 and 18-24 are rejected under 35 U.S.C. 103 as being unpatentable over Hultin et al. (US 7,556,835) in view of O’Brien (“Sanitation and Safety for a Fats and Oils Processing Plant-Chapter 199” – Handbook of Food Science, Technology, and Engineering, Volume 4, Hui, Y.H. Ed. , CRC Taylor & Francis, 2006, pp. 199-1-199-10).
Regarding claims 1, 3-16 and 18-24, Hultin et al. disclose a process for isolating a lipid-free edible protein from animal muscle and the resulting lipid-free edible protein, the method comprising: (a) obtaining a mixture comprising animal muscle and water (i.e. adding water to animal muscle tissue); (b) increasing the pH of the mixture to a level sufficient to solubilize at least 75% of the animal protein in the animal muscle mixture, i.e. pH greater than about 10.0, by adding sodium hydroxide; (c) centrifuging the pH adjusted mixture so that the charged membrane lipids and neutral lipids are separated from the aqueous phase; (d) adjusting the pH of the aqueous phase to less than about 5.5 by adding hydrochloric acid or citric acid, to precipitate the protein; and (e) collecting the precipitated edible protein by centrifugation (C2/L10-C3/L14, C4/L21-C6/L24).
Hultin et al. disclose wherein the animal muscle may be of low value (C1/L36-37) and be sources from fish fillets, deheaded and gutted fish, crustacean, molluscs, chicken and other poultry, beef, pork or lamb (C7/L25-31). Given Hultin et al. disclose a source of animal muscle from a broad range of muscle types and species, clearly Hultin et al. intends the use of animal muscle having a fat and lean content in the range presently claimed.
While Hultin et al. disclose separating fat from the solubilized protein to produce a lipid-free edible protein, the reference is silent with respect to heating the solubilized protein and fat mixture so that the fat becomes liquid.
O’Brien teaches separation of fat from fatty tissues of animals is called rendering. O’Brien teaches that rendering consists of two basic steps including: (a) heating meat by-product at a temperature below 120ºF to melt the fat present; and (b) separating the fat from the solid proteinaceous material (p 199-4/ B. Rendering). O’Brien teaches when a better quality protein is desired, processing with lower temperature, i.e. below 120ºF, is desired (p. 199/4/B. Rendering).
Hultin et al. and O’Brien are combinable because they are concerned with the same field of endeavor, namely processing of animal muscle. It would have been obvious to one of ordinary skill in the art to have separated the fat in the solubilized protein solution of Hultin et al., made from animal muscle and water, by heating the solution to low temperatures, melting the fat and separating the fat and water from the precipitated protein, i.e. well known rendering process as taught by O’Brian.
Here, given O’Brien teaches the concept of rendering, since Hultin et al. teach meat protein solubilized in a solution of water and fat, one of ordinary skill in the art applying the rendering concept to the process of Hultin et al. would have found in obvious to have removed the fat from the heated solution before or after precipitating the protein. Moreover, if the melted fat is removed before precipitation, it would have been obvious to have cooled the solution for ease of handling in subsequent steps.
Given Hultin et al. disclose the concept of separating the water, fat and protein components, it would have been obvious to one of ordinary skill in the art to have included a step of removing water from the liquid fat.
Given the combination of Hultin et al. and O’Brien suggest a process substantially similar to that presently claimed, intrinsically the resulting edible protein would exhibit the claimed color, lean content, fat content, and water binding ability as presently claimed. Moreover, one of ordinary skill in the art would expect the resulting edible protein would exhibit the functionality of raw meat as presently claimed.
Regarding claim 2, modified Hultin et al. disclose all of the claim limitations as set forth above. Hultin et al. disclose wherein the animal muscle can in generally constitute 50% or less by weight of the mixture with water (C2/L23-25).
Response to Arguments
Applicant's arguments filed September 30, 2025 have been fully considered but they are not persuasive.
Applicant submits “[o]ne of ordinary skill in the art would not increase the temperature used in Hultin to render the fats as in O’Brien” Applicant argues “while one of ordinary skill in the art COULD select a lower temperature, they would still not be motivated to select a temperature so low that the fat would not melt.” Further, Applicant submits “ [o]ne of ordinary skill in the art would not be motivated to raise the temperatures to that of the present invention because Hultin specifically teaches against it.”
While Hultin et al. disclose maintaining temperatures of at least 15°C (59°F) or less in each of its steps to prevent denaturing the protein, the reference does not disclose at what temperature a particular muscle would denature. There is no evidence on the record demonstrating that at a temperature of less than 120°F and above the melting point of a particular meat fat, the meat proteins would denature.
Applicant provides an exhibit with three references to show proteins denature when heat is applied.
The Pang et al. reference demonstrates the influence of meat temperature on moisture loss, muscle water properties and protein profiles in the broiler pectoralis major having severe woody breast condition (Abstract). The reference teaches the denaturation of meat proteins or changes in meat protein structure depends on proteins and cooking temperature. For example myosin molecules start to denature at 40 °C (104 °F) and completely denature when heating above 53 °C (127 °F). Pang et al. also teach the actin denaturation starts at much higher temperatures, i.e., 66-73 °C (150 °F – 163 °F). The disclosure of Pang is specific chicken breast muscle and does not suggest that at temperatures below 120 °F, the muscle proteins completely denature or that their quality would be significantly impacted.
The Richie et al. reference is directed to protein denaturation of liver and white muscle of Wistar rat. This reference is not considered analogous to the present invention directed to proteins from meat producing animals.
The Tornberg reference teaches sarcoplasmic proteins aggregate between 40° and 60 °C but for some of them the coagulation can extend up to 90 °C and for myofibrillar protein in solution, unfolding starts at 30° and 32 °C, followed by protein-protein association at 36°-40 °C and subsequent gelation at 45°-50 °C. Tornberg does not teach that at temperatures less than 120 °F (i.e., about 49 °C), the muscle proteins significantly denature or that their quality is impacted.
Conclusion
All claims are identical to or patentably indistinct from, or have unity of invention with claims in the application prior to the entry of the submission under 37 CFR 1.114 (that is, restriction (including a lack of unity of invention) would not be proper) and all claims could have been finally rejected on the grounds and art of record in the next Office action if they had been entered in the application prior to entry under 37 CFR 1.114. Accordingly, THIS ACTION IS MADE FINAL even though it is a first action after the filing of a request for continued examination and the submission under 37 CFR 1.114. See MPEP § 706.07(b). 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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ELIZABETH A. GWARTNEY
Primary Examiner
Art Unit 1759
/ELIZABETH GWARTNEY/Primary Examiner, Art Unit 1759