DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
In view of the pre-appeal review filed March 2, 2026 prosecution is reopened.
Claims 1-3, 5, 11. 12. 14-17, 22-26, 29-30, 32-36 and 40 are pending examination.
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 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.
Claims 1-3, 5, 9, 11, 12, 14-17, 22-25, 28-30, 32, 34 and 40 rejected under 35 U.S.C. 103 as being unpatentable over Huang et al. (CN 107325977-Clarivate Analytics English translation ) in view of Feng et al. (CN 109007035 A – Clarivate Analytics English translation).
Regarding claims 1, 2, 5, 9, 16, 23-25 and 40, Huang et al. disclose a functional beverage comprising 1-2% w/v soy protein isolate, 20 U to 50 U (per gram of protein) protein glutaminase and soybean polysaccharide (i.e., stabilizer- p. 7, p. 16-17/Example 8 – Use of Protein Glutaminase in the Development of Soy Protein Functional Beverage).
Huang et al. disclose adding different proportions of protein glutaminase and soybean polysaccharide to the functional drink composition to increase the protein solubility and stability of the functional drink (p. 18). Therefore, one of ordinary skill in the art would have been motivated to adjust, in routine, processing the amount of soybean polysaccharide (i.e., stabilizer) to add to the functional beverage to obtain a desired protein solubility, stability and taste.
Huang et al. disclose protein glutaminase is a type of hydrolase that can remove amino groups of protein, peptides or short peptides (p. 1). Specifically, Huang et al. disclose protein glutaminase is an enzyme that deamidates glutaminyl residues in proteins that acts only on the glutamine group of the protein without affecting asparagine residues and free glutamine (p. 1-2).
Huang et al. explains that natural proteins contain more glutamine and asparagine residue which cross-link with other amino acids in the form of hydrogen bonds, resulting in reduced protein solubility. Huang et al. submits a deamidation is an important way to solve this problem (p. 1/Background technique). Specifically, Huang et al. explains that through deamidation, the amide group in the protein is converted to a carboxyl group, the negative charge increases, and the isoelectric point of the protein is reduced (p. 1/Background technique). Huang et al. disclose that when the protein glutaminase is added to a soy protein solution to hydrolyze the protein, the clarity of the soy protein solution (e.g., beverage) is improved (p. 2/Content of the invention).
While Huang et al. does not specify the pH of the functional beverage, Huang disclose it is the combination of protein glutaminase and soybean polysaccharide in the functional drink composition that maintains good protein solubility and stability in the functional drink (p. 18). Therefore, it would have been obvious to one of ordinary skill in the art prior to the effective filing date of the present application to have formulated the functional beverage of Huang et al. at any pH to obtain a beverage with desirable sensory attributes. The skilled artisan would expect that at any pH the solubility, stability and flavor of the protein in the beverage would be maintained.
While Huang et al. teach soybean polysaccharide, the reference is silent with respect to a stabilizer selected from xanthan gum, gellan gum, carrageenan gum, cassia gum, locust bean gum, tara gum, psyllium seed gum, gelatin, tamarind seed gum, gum arabic, propylene glycol alginates, pectin, galactomannan (guar gum), pullulan, carboxymethylcellulose (CMC), methylcellulose (MC), derivatives of any thereof, and combinations of any thereof.
Feng et al. teach a beverage comprising plant protein, milk protein, fruit juice and stabilizer. Feng et al. teach the stabilizer is chosen from the group of carrageenan, microcrystalline cellulose, gellan gum, soybean polysaccharide or combinations thereof (Summary of the invention, Examples 4 and 8-10).
Huang et al. and Feng et al. are combinable because they are concerned with the same field of endeavor, namely protein-based functional beverages comprising stabilizer. Given Feng et al. teaches the interchangeability of using carrageenan, gellan gum and soybean polysaccharide as stabilizers for protein-based functional beverages, it would have been obvious to one of ordinary skill in the art prior to the effective filing date of the present invention to have used carrageenan and/or gellan gum with (or to replace) the soybean polysaccharide as the stabilizer in Huang et al. with a reasonable expectation of success.
Regarding claims 3 and 12, modified Huang et al. disclose all of the claim limitations as set forth above. Huang et al. explains natural proteins contain more glutamine and asparagine residues, which cross-link with other amino acid in the form of hydrogen bonds, resulting in reduced protein solubility (p. 1/Background technique). Huang et al. disclose deamidation is an important way to solve this problem because through deamidation the amide group in the protein is converted to a carboxyl group, the negative charge increases, and the isoelectric point of the protein is reduced (p. 1/Background technique). While Huang et al. disclose a protein glutaminase from Chryseobacterium, an enzyme that deamidates glutaminyl residues into glutamic acid and ammonia and acting only on the glutamine group of the protein (p. 1-2/Background technique), Huang et al. disclose the role of asparagine residues protein solubility. Hence, the skilled artisan provided the disclosure of Huang et al. would have been motivated to deamidate the soy protein isolate using an asparaginase, including asparaginase produced by Penicillium, instead of glutaminase with a reasonable expectation of success.
Regarding claim 11, modified Huang et al. disclose all of the claim limitations as set forth above. Huang et al. disclose wherein the protein glutaminase is produced from Chryseobacterium (p. 3-4).
Regarding claims 14 and 15, modified Huang et al. disclose all of the claim limitations as set forth above. While Huang et al. disclose a protein glutaminase with high activity that is safely applied to food (p.2/Background technique), Huang et al. is silent with respect the protein glutaminase having an amino sequence of SEQ ID NO. 1 or SEQ ID NO 1 and having one or more substitutions or deletions at the specific amino acid residues claimed.
Here, given Huang et al. disclose an enzyme, i.e., a protein glutaminase, capable of deaminating protein, the claimed amino acid sequence does not have patentable weight. The claimed solution appears to be the same as or obvious from the functional beverage of Huang et al., therefore claims 14 and 15 are unpatentable even though the enzyme in the product of Huang et al. has a difference amino acid sequence.
Regarding claim 17, modified Huang et al. disclose all of the claim limitations as set forth above. Given Huang et al. disclose a functional beverage comprising substantially the same components in amounts as claimed, it follows the beverage would exhibit a viscosity with in the broadly claimed range of about 10 to about 250 mPa·s (see MPEP §2112.01 I).
Regarding claim 22, modified Huang et al. disclose all of the claim limitations as set forth above. Given Huang et al. disclose a functional beverage comprising the components required by claim 1, inherently the beverage would display the claimed storage stability (MPEP §2112.01 I).
Regarding claim 28, modified Huang et al. disclose all of the claim limitations as set forth above. Huang et al. disclose the functional beverage is made by: (a) preparing a solution of soy protein isolate in 200 mM acid buffer; (b) add protein glutaminase to the soy protein isolate solution; and (c) incubate the mixture at 37°C for 18 h (p. 16-17/Example 9).
Huang et al. is silent with respect to a specific step of acidifying the mixture to obtain a solution with a pH of from about 3.5 to 5.0.
While Huang et al. does not specify the pH of the functional beverage, Huang disclose it is the combination of protein glutaminase and soybean polysaccharide in the functional drink composition that maintains good protein solubility and stability in the functional drink (p. 18). Therefore, it would have been obvious to one of ordinary skill in the art prior to the effective filing date of the present application to have formulated the functional beverage of Huang et al. (e.g., by acidifying the beverage to obtain an acidic pH)) at any pH to obtain a beverage with desirable sensory attributes. The skilled artisan would expect that at any pH the solubility, stability and flavor of the protein in the beverage would be maintained.
Regarding claim 29, modified Huang et al. disclose all of the claim limitations as set forth above. Huang et al. disclose adding soybean polysaccharide (i.e., stabilizer) to the soy protein isolate solution (p. 17-18/Example 10).
While Huang et al. does not specifically disclose adding the soybean polysaccharide in the form of a solution, it would have been obvious to one of ordinary skill in the art prior to the effective filing date of the present application to have added the soybean polysaccharide in any form, e.g., powder or solution, while maintaining the required dosage, and arrive at the present invention.
Regarding claim 30, modified Huang et al. disclose all of the claim limitations as set forth above. While Huang et al. disclose incubate the mixture at 37°C for 18 h (p. 16-17/Example 9). While Huang et al. does explicitly disclose the pH of the incubation mixture, Huang et al. disclose making up the soy protein isolate solution in a 200 mM acid buffer. Since an acid buffer would necessarily have a pH of less than 7, it follows that the reaction mixture would start at a pH in the claimed range from about 3.0 to about 8.0.
Regarding claim 32, modified Huang et al. disclose all of the claim limitations as set forth above. Huang et al. disclose that during incubation, samples are taken to determine the ammonia content (i.e., concentration of free ammonium ions in the solution)(p. 17/Example 9). Huang et al. disclose the percentage of ammonia in the sample to the total ammonia content is the degree of deamidation (p. 17/Example 9).
Regarding claim 34, modified Huang et al. disclose all of the claim limitations as set forth above.
While Huang et al. disclose a protein glutaminase with high activity that is safely applied to food (p.2/Background technique), Huang et al. is silent with respect the protein glutaminase having an amino sequence of SEQ ID NO. 1.
Here, given Huang et al. disclose an enzyme, i.e., a protein glutaminase, capable of deaminating protein, the claimed amino acid sequence does not have patentable weight. The claimed solution appears to be the same as or obvious from the functional beverage of Huang et al., therefore claim 34 is unpatentable even though the enzyme in the product of Huang et al. has a difference amino acid sequence.
While Huang et al. disclose incubating at 37°C for 18 h (p. 16-17/Example 9), the reference is silent with respect to incubating at a temperature of 50°C for 3 hours. However, one of ordinary skill in the art prior to the effective filing date of the present application to have adjusted, in routine processing, the temperature and time of incubation to obtained the desired level of completion for the enzyme reaction.
Claims 26, 33, 35 and 36 are rejected under 35 U.S.C. 103 as being unpatentable over Huang et al. (CN 107325977-Clarivate Analytics English translation ) in view of Feng et al. (CN 109007035 A – Clarivate Analytics English translation) as applied to claims 1, 24 and 28, and further in view of Kale et al. (“Effect of Different Concentrations of Orange Juice on Quality Characteristics of Soya Milk Blended Beverage”, Food Processing & Technology, Volume 3, Issue 1, (2011), pp. 1-5).
Regarding claim 26, modified Huang et al. disclose all of the claim limitations as set forth above. While Huang et al. disclose a functional beverage as claimed, the reference is silent with respect a functional beverage comprising a fruit juice, fruit juice concentrate, vegetable juice, or vegetable juice concentrate.
Kale et al. teach soy milk beverages fortified with orange juice (Abstract, p. 2/Introduction, p. 2/Materials and Methods/Production of orange soy RTS beverage). Kale et al. teach that by fortifying the soy milk beverage with orange juice the sensorial characteristic and the nutritional quality of the soy milk beverage is improved (p. 2/Introduction).
Huang et al. and Kale et al. are combinable because they are concerned with the same field of endeavor, namely soy based beverages. It would have been obvious to one of ordinary skill in the art prior to the effective filing date of the present application to have fortified the functional beverage of Huang et al. with orange juice, as taught by Kale et al, for the purpose of improving the sensorial characteristics and the nutritional quality of the functional beverage.
Regarding claim 33, modified Huang et al. disclose all of the claim limitations as set forth above. Huang et al. is silent with respect to adding an acidic juice to the functional beverage.
Kale et al. teach soy milk beverages fortified with orange juice (Abstract, p. 2/Introduction, p. 2/Materials and Methods/Production of orange soy RTS beverage). Kale et al. teach that by fortifying the soy milk beverage with orange juice the sensorial characteristic and the nutritional quality of the soy milk beverage is improved (p. 2/Introduction).
Huang et al. and Kale et al. are combinable because they are concerned with the same field of endeavor, namely soy based beverages. It would have been obvious to one of ordinary skill in the art prior to the effective filing date of the present application to have fortified the functional beverage of Huang et al. with orange juice, as taught by Kale et al, for the purpose of improving the sensorial characteristics and the nutritional quality of the functional beverage.
Regarding claims 35 and 36, modified Huang et al. disclose all of the claim limitations as set forth above. Huang et al. is silent with respect to pasteurizing the functional beverage.
Kale et al. teach a soy milk beverage comprising soy milk (i.e., comprising soy protein) and orange juice (Abstract, p. 2/Materials and Methods). Kale et al. teach preparing the beverage by blending the orange juice with soy milk and pasteurizing at 85°C for 10 min and hot filling into sterile bottles (p. 2/Materials and Methods/Production of orange soy RTS beverage).
Huang et al. and Kale et al. are combinable because they are concerned with the same field of endeavor, namely soy based beverages. It would have been obvious to one of ordinary skill in the art to have pasteurized the functional beverage of Huang et al., as taught by Kale et al., for the purpose of eliminating pathogens and extending shelf life.
Response to Arguments
Huang Does Not Teach or Suggest the Recited pH-
Applicant's arguments filed March 2, 2026. with respect to pH. have been fully considered but they are not persuasive.
Applicant submits Huang et al. does not teach or suggest a stable liquid composition having a pH of from 3.5 to 5.0. Applicant submits “a person of ordinary skill in the art would not have had a reasonable expectation that a functional beverage according to Huang would be stable in the acidic pH ranges claimed.” Applicant explains “it is well-known that plant proteins have limited solubility at acidic pH and tend to precipitate.” Applicant notes “the Examiner has not recited any evidence to the contrary.”
Applicant explains FIG 7 of EP 1106606 unequivocally shows that deamidated soybean protein is not soluble at a pH below about 5.5 and that deamidated soybean protein would not be soluble an any pH within the claimed range.
In this case, Huang et al. disclose a functional beverage comprising 1-2% w/v soy protein isolate, 20 U to 50 U (per gram of protein) protein glutaminase and soybean polysaccharide (i.e., stabilizer- p. 7).
Huang et al. disclose adding different proportions of protein glutaminase and soybean polysaccharide to the functional drink composition to increase the protein solubility and stability of the functional drink (p. 18). Therefore, one of ordinary skill in the art would have been motivated to adjust, in routine, processing the amount of soybean polysaccharide (i.e., stabilizer) to add to the functional beverage to obtain a desired protein solubility, stability and taste.
Huang et al. disclose protein glutaminase is a type of hydrolase that can remove amino groups of protein, peptides or short peptides (p. 1). Specifically, Huang et al. disclose protein glutaminase is an enzyme that deamidates glutaminyl residues in proteins that acts only on the glutamine group of the protein without affecting asparagine residues and free glutamine (p. 1-2).
Here, while Huang et al. is silent with respect to pH, given Huang et al. disclose a functional beverage comprising the claimed components, i.e., soy protein isolate, glutaminase and soybean polysaccharide, one of ordinary skill in the art would expect the protein in the functional beverage to display the claimed stability at the claimed pH values. One of ordinary skill in the art, armed with the disclosure of Huang et al. which teaches that when protein glutaminase is added to a soy protein solution to hydrolyze the protein, the clarity of the protein solution is improved, would have considered formulating the functional beverage of Huang et al. at any pH with a reasonable expectation of success. Huang et al. does not teach away from a functional beverage having any given pH value or range.
Here, a prima facie case of obviousness has been established. The burden now shifts to the Applicant to provide evidence to rebut the examiner’s evidence (MPEP §2142).
Huang Does Not Teach or Suggest the Recited Stabilizers-
Applicant’s arguments, filed March 2, 2026, with respect to the stabilizer have been fully considered and are persuasive. Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground(s) of rejection is made in view of Huang et al. and Feng et al.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ELIZABETH A GWARTNEY whose telephone number is (571)270-3874. The examiner can normally be reached M-F: 9 a.m. - 5 p.m. EST.
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ELIZABETH A. GWARTNEY
Primary Examiner
Art Unit 1759
/ELIZABETH GWARTNEY/Primary Examiner, Art Unit 1759
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