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 .
This Office Action was written in response to the Applicants Remarks filed 12/9/25. Claims 1-20 are pending. Claims 17-20 are new. Claims 10-16 were previously withdrawn. Claims 1-9, and 17-20 have been examined on the merits.
Withdrawn Rejections
The 102(a)(1) rejections of claims 1-3, 5, 6, 7, and 8 as being anticipated by Bhowmik et al. US 2011/0045138 as evidenced by Innocenzi (US 2012/0027897) have been withdrawn.
The 103(a) rejections of claims 4, and 7-9, over Bhowmik et al. US 2011/0045138 as evidenced by Innocenzi (US 2012/0027897) in further view of Soong et al. (US 2013/0157307) have been withdrawn.
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 1-8, 17, and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Hiroki (WO 2021/002195) on Applicants’ IDS in view of Bhowmik et al. US 2011/0045138 and Naveed et al. “Protease-A Versatile and Ecofriendly Biocatalyst with Multi‑Industrial Applications: An Updated Review” July 2020 vol. 151 pages 307-323.
Regarding Claim 1: Hiroki discloses a method of producing a cysteine containing product by treating a protein/a glutathione containing food with a γ-glutamyl peptide hydrolase, and with a microbial acid protease that is derived from a microorganism or specifically a fungal protease [abstract; 0012]. Hiroki discloses that cysteine is produced as a result of the reaction [abstract]. Hiroki discloses that the Maillard reaction product of cysteine produces a meaty flavor and that in heat treated food, flavor can be enhanced [0002]. Hiroki discloses an induction of a Maillard reaction, which is known in the art to inherently involve heat (the thermal exchange of energy).
Hiroki, although disclosing a microbial acid protease, does not explicitly disclose bacterial acid protease.
Bhowmik discloses a method of hydrolyzing a plant material and producing a proteolytic product [0010-0012] comprising treating the plant material with a γ-glutamyl peptide hydrolase [0024; 0046], a protease derived from filamentous fungi (Aspergillus sojae); A. oryzae [0024; 0006], and a bacterial protease derived from Bacillus sp. [0024; 0048].
Naveed teaches proteases derived from fungi and bacteria [abstract; pg. 312]. Naveed discloses that bacterial proteases are alkaline in nature and have a higher activity at pH levels of 8 to 12 [pg. 312, “3.3.2 Bacterial”].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to modify the method of Hiroki to further include a bacterial protease as in Bhowmik in order to ensure proteolytic activity across a pH spectrum since Hiroki discloses the use of acidic fungal protease and Naveed discloses bacterial proteases as being alkaline in nature and having higher activities at pH levels of 8-12 and since Bhowmik also treats its plant material utilizing both bacterial and fungal proteases.
The Examiner also notes that, the new limitation reciting “so as to induce a Maillard reaction when the protein material is heated” is an intended use of the claimed invention and in order to patentably distinguish the claimed invention from the prior art, the recitation must result in a structural difference between the claimed invention and the prior art. MPEP 2103 states that intended use language "does not limit a claim to a particular structure does not limit the scope of a claim". The above mentioned phrase does not limit the claim to any particular structure, so it is not interpreted to limit the scope of the claims. If the prior art structure is capable of performing the intended use, then it meets the claim.
Regarding Claims 2-4: Hiroki discloses as discussed above in claim 1. Hiroki discloses wherein the γ-glutamyl peptide hydrolase is a glutaminase, a γ- glutamyltransferase, or a y-glutamylcyclotransferase [claim 7]; wherein the γ-glutamyl peptide hydrolase is a glutaminase derived from Bacillus microorganisms [claim 8]; wherein the γ-glutamylpeptide hydrolase is a glutaminase derived from Bacillus amyloliquefaciens [claim 9].
Regarding Claims 5 and 6: Hiroki discloses as discussed above in claim 1. Hiroki discloses wherein the filamentous fungi-derived protease is an acid protease derived from Aspergillus microorganisms [0012]; wherein the filamentous fungi-derived protease is an acid protease derived from Aspergillus oryzae [0012].
Regarding Claims 7 and 8: Hiroki discloses as discussed above in claim 1. Hiroki discloses a cysteine containing proteolytic product where the protein is animal protein, plant protein, or yeast (microbial) protein [claim 12; 0014].
Regarding Claim 17: Hiroki discloses a method of producing a cysteine containing product by treating a protein/a glutathione containing food with a γ-glutamyl peptide hydrolase, and with a microbial acid protease that is derived from a microorganism or specifically a fungal protease [abstract; 0012]. Hiroki discloses that cysteine is produced as a result of the reaction [abstract]. Hiroki discloses that the Maillard reaction product of cysteine produces a meaty flavor and that in heat treated food, flavor can be enhanced [0002]. Hiroki discloses an induction of a Maillard reaction, which is known in the art to inherently involve heat (the thermal exchange of energy).
Hiroki discloses wherein the filamentous fungi-derived protease is an acid protease derived from Aspergillus microorganisms [0012]; wherein the filamentous fungi-derived protease is an acid protease derived from Aspergillus oryzae [0012]. Hiroki discloses wherein the γ-glutamyl peptide hydrolase is a glutaminase, a γ- glutamyltransferase, or a y-glutamylcyclotransferase [claim 7]; wherein the γ-glutamyl peptide hydrolase is a glutaminase derived from Bacillus microorganisms [claim 8].
Hiroki, although disclosing a microbial acid protease, does not explicitly disclose bacterial acid protease.
Bhowmik discloses a method of hydrolyzing a plant material and producing a proteolytic product [0010-0012] comprising treating the plant material with a γ-glutamyl peptide hydrolase [0024; 0046], a protease derived from filamentous fungi (Aspergillus sojae); A. oryzae [0024; 0006], and a bacterial protease derived from Bacillus sp. [0024; 0048].
Naveed teaches proteases derived from fungi and bacteria [abstract; pg. 312]. Naveed discloses that bacterial proteases are alkaline in nature and have a higher activity at pH levels of 8 to 12 [pg. 312, “3.3.2 Bacterial”].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to modify the method of Hiroki to further include a bacterial protease as in Bhowmik in order to ensure proteolytic activity across a pH spectrum since Hiroki discloses the use of acidic fungal protease and Naveed discloses bacterial proteases as being alkaline in nature and having higher activities at pH levels of 8-12 and since Bhowmik also treats its plant material utilizing both bacterial and fungal proteases.
The Examiner also notes that, the new limitation reciting “so as to induce a Maillard reaction when the protein material is heated” is an intended use of the claimed invention and in order to patentably distinguish the claimed invention from the prior art, the recitation must result in a structural difference between the claimed invention and the prior art. MPEP 2103 states that intended use language "does not limit a claim to a particular structure does not limit the scope of a claim". The above mentioned phrase does not limit the claim to any particular structure, so it is not interpreted to limit the scope of the claims. If the prior art structure is capable of performing the intended use, then it meets the claim.
Regarding Claim 18: Hiroki as modified discloses as discussed above in claim 17. Hiroki discloses conducting the enzymatic treatment for 5 minutes-24 hours [0021].
Although Hiroki does not explicitly disclose 15 minutes to 6 hours one having ordinary skill in the art at the effective filing date of the invention would have considered the invention to have been obvious because the range taught by Hiroki overlaps the instantly claimed range and therefore is considered to establish a prima facie case of obviousness. In re Malagari 182 USPQ 549,553.
Claim 9 is rejected under 35 U.S.C. 103 as being unpatentable over Hiroki (WO 2021/002195) on Applicants’ IDS in view of Bhowmik et al. US 2011/0045138 and Naveed et al. “Protease-A Versatile and Ecofriendly Biocatalyst with Multi‑Industrial Applications: An Updated Review” July 2020 vol. 151 pages 307-323 as applied to claim 1 above and in further view of Soong et al. (US 2013/0157307).
Regarding Claim 9: Hiroki discloses as discussed above in claim 1. Hiroi does not disclose wherein the protein material is a protein material derived from peas, soybeans, fava beans, chickpeas, barley, wheat, oats, rice, buckwheat, chives, millet, hemp, algae, almonds, cashew nuts, hazelnuts, pecan nuts, macadamia nuts, pistachios, walnuts, brazil nuts, peanuts, or coconuts.
Soong discloses the plant material as barley, beans, peas, rice, and wheat [0023]. Soong discloses a process of fermenting a plant material and including deamidases for hydrolysis [abstract]. Soong discloses using a glutaminase derived from B. amyloliquefaciens [0077].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to modify the plant material of Hiroki to include the barley, beans, peas, rice, and wheat as in Soong in order to prepare a flavor enhancer based on other vegetable sources and since Hiroki discloses generally that vegetables can be the protein material.
Claims 19 and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Hiroki (WO 2021/002195) on Applicants’ IDS in view of Bhowmik et al. US 2011/0045138 and Naveed et al. “Protease-A Versatile and Ecofriendly Biocatalyst with Multi‑Industrial Applications: An Updated Review” July 2020 vol. 151 pages 307-323 as applied to claim 17 above and in further view of Faith et al. (US 3, 697,285).
Regarding Claim 19: Hiroki as modified discloses as discussed above in claim 17. Hiroki discloses glutaminase at 0.001% to 10% or 0.01% to 1% [0021]. Hiroki discloses fungal protease at 0.001% to 10% or 0.01% to 2% [0017].
Hiroki as modified does not disclose the amount of bacterial protease between about 0.01% to about 2%.
Faith discloses utilizing an alkaline bacterial protease for the hydrolyzation of fish protein material and the production of soluble protein extracts [abstract; col. 1, lines 66-72; col. 2, lines 41-49; claim 6]. Faith discloses using the bacterial protease in amounts of from 0.1% to 1.0% [col. 2, lines 61-65].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to further modify the method of Hiroki which as modified contains bacterial protease to include the bacterial protease at 0.1 to 1.0 % as in Faith in order to aid in the production of hydrolyzed protein and since at the recited amount hydrolyzed protein is produced.
Regarding Claim 20: Hiroki as modified discloses as discussed above in claim 17. Hiroki discloses glutaminase at 0.001% to 10% or 0.01% to 1% [0021]. Hiroki discloses fungal protease at 0.001% to 10% or 0.01% to 2% [0017].
Hiroki as modified does not disclose the ratio of wherein a ratio of the γ-glutamyl peptide hydrolase to the filamentous fungi-derived protease to the bacterial protease is 25% : 50% : 25%.
Faith discloses utilizing an alkaline bacterial protease for the hydrolyzation of fish protein material and the production of soluble protein extracts [abstract; col. 1, lines 66-72; col. 2, lines 41-49; claim 6]. Faith discloses using the bacterial protease in amounts of from 0.1% to 1.0% [col. 2, lines 61-65].
At the effective filing date of the invention it would have been obvious to one of ordinary skill in the art to further modify the method of Hiroki which as modified contains bacterial protease to include the bacterial protease at 0.1 to 1.0 % as in Faith in order to aid in the production of hydrolyzed protein and since at the recited amount hydrolyzed protein is produced.
Since Hiroki discloses glutaminase at 1% and fungal protease at 2% and when combined with the bacterial protease at 1.0 %, the ratio becomes 1:2:1 or 25%: 50%: 25%.
Response to Arguments
The 102(a)(1) rejections of claims 1-3, 5, 6, 7, and 8 as being anticipated by Bhowmik et al. US 2011/0045138 as evidenced by Innocenzi (US 2012/0027897) have been withdrawn.
The 103(a) rejections of claims 4, and 7-9, over Bhowmik et al. US 2011/0045138 as evidenced by Innocenzi (US 2012/0027897) in further view of Soong et al. (US 2013/0157307) have been withdrawn.
Conclusion
10. 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.
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FELICIA C TURNER whose telephone number is (571)270-3733. The examiner can normally be reached Mon-Thu 8:00-4:00 pm.
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/Felicia C Turner/Primary Examiner, Art Unit 1793