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 is in response to the application filed on November 10, 2025. The earliest effective filing date of the application is May 11, 2023.
Status of Application
The amendments filed on July 23, 2026 have been entered with the Remarks. The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 1 – 17 and 21 – 23
Withdrawn claims: None
Amended claims: 2 – 4, and 11
Previously cancelled claims: 18 – 20
Claims currently under examination: 1 – 17 and 21 – 23
By not repeating the previously presented objection/rejection(s), it is sufficiently clear that said
objection/rejection(s) are withdrawn.
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.
Claims 1, 9 – 11, 14 – 16, and 21 – 23 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Sun et al. (US 20030165592 – IDS Filed on November 13, 2025) as evidenced by Dong et al. (Bioinformatic mapping of a more precise Aspergillus niger degradome. Scientific Reports. Vol 11. Iss 693. (2021)).
Regarding claim 1, Sun teaches a method of rendering wine heat-stable comprising the step of: adding to wine, prior to bottling, a protease that will hydrolyze proteins that cause heat-induced protein haze or precipitate ([0028]). Sun teaches the protease is Aspergillus niger ([0074]). As evidenced by Dong et al. Aspergillus niger produces S53 serine peptidases (Table 6 Serine proteases encoded by A. niger strains CBS 513.88 and ATCC 1015). Therefore, Sun teaches a method of dehazing a beverage of interest comprising a step of adding a protease from the S53 family to a beverage of interest, thereby forming a composition comprising the beverage of interest and the protease.
Regarding claim 9, Sun teaches preparing wine samples by contacting Sauvignon blanc wine with protease (Example 1, [0075] – [0095]). Sun teaches the wine samples 2 – 4 are prepared by using 180 and 540 mg/L protease (Example 1; [0082] – [0090]).
Regarding claims 10 and 15, Sun teaches preparing wine samples by contacting Sauvignon blanc wine (i.e., white wine) with protease (Example 1, [0075] – [0095]).
Regarding claim 11, Sun teaches preparing wine samples by contacting Sauvignon blanc with protease (Example 1, [0075] – [0095]). Sun teaches the samples were subjected to a heat test in which they were heated at 60 °C for 15 hours (i.e., the composition is incubated for 15 hours – [0091]).
Regarding claim 14, Sun teaches Table 1, which shows the precipitate content and haziness of the heat-treated wines of Example 1 (Examples 1; [0091]). While Sun does not explicitly state the protein content of the wines were monitored, by monitoring the haziness and precipitate content of the wine samples, Sun has monitored the protein content of the wines to assess the degree of haze reduction, because haziness and precipitation are known to be caused by proteins present in wine.
Regarding claim 16, Sun teaches preparing samples by contacting Sauvignon blanc grape juice with protease prior to fermentation (Example 7, [0124] – [0129]). Therefore, the beverage of interest is a grape juice.
Regarding claim 21, Sun teaches preparing wine samples by contacting sauvignon blanc with protease (Example 1, [0075] – [0095]). Sun teaches wine samples 2 – 4 are prepared by using 180 and 540 mg/L protease (Example 1; [0082] – [0090]). Sun teaches the addition of protease at 180 and 540 mg/L effectively eliminated all of the heat-induced precipitate from grape/wine proteins (i.e., at least 85% of heat-unstable proteins are removed – Example 1; [0093]).
Regarding claim 22, Sun teaches the clarified or clear wine is filtered through a layer of diatomaceous earth, followed by filtration using a 0.45 .quadrature. membrane ([0070]). Sun teaches this process renders the wine substantially free from haze particles ([0070]).
Regarding claim 23, Sun teaches treating Sauvignon blanc wine with 180 mg/L protease and 180 mg/L bentonite (i.e., a fining agent) removes heat-induced haze and precipitates (Table 6; [0122]). Sun teaches to achieve the same reduction by using only bentonite (i.e., a fining agent), 1080 mg/L was required (Table 6; [0123]). Therefore, Sun teaches adding a fining agent to the composition, wherein the fining agent is bentonite, and wherein the amount of fining agent used is less than the amount needed to dehaze the beverage of interest in the absence of the protease.
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.
Claims 2 – 7 are rejected under 35 U.S.C. 103 as being unpatentable over Sun et al. (US 20030165592 – IDS Filed on November 13, 2025) as evidenced by Dong et al. (Bioinformatic mapping of a more precise Aspergillus niger degradome. Scientific Reports. Vol 11. Iss 693. (2021)), as applied to claim 1 above, and further in view of Siegel et al. (US 20200383351, which is Application No. 16/767,535 in Search Results filed on June 4, 2026).
Regarding claims 2, 4, 6, and 7, Sun does not teach the protease comprises SEQ ID NO 14. However, as noted in the rejection of claim 1 above, Sun teaches the use of S53 serine peptidases in a food product.
Siegel teaches the use of S53 serine peptidases in a food product. One S53 serine peptidase that Siegel teaches is SEQ ID No. 16, which has 100% to SEQ ID No. 14 of the instant application (p. 24, SEQ ID No. 16). The alignment of SEQ ID No. 14 of the instant application (Qy) to with SEQ ID No. 16 of Siegel (Db) is shown below:
SEQ ID NO 16
LENGTH: 552
TYPE: PRT
ORGANISM: Bacillus sp.
Query Match 100.0%; Score 2866; Length 552;
Best Local Similarity 100.0%;
Matches 552; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MSDMEKPWKEEEKREVLAGHARRQAPQAVDKGPVTGDQRISVTVVLRRQRGDELEAHVER 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MSDMEKPWKEEEKREVLAGHARRQAPQAVDKGPVTGDQRISVTVVLRRQRGDELEAHVER 60
Qy 61 QAALAPHARVHLEREAFAASHGASLDDFAEIRKFAEAHGLTLDRAHVAAGTAVLSGPVDA 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 QAALAPHARVHLEREAFAASHGASLDDFAEIRKFAEAHGLTLDRAHVAAGTAVLSGPVDA 120
Qy 121 VNQAFGVELRHFDHPDGSYRSYVGDVRVPASIAPLIEAVLGLDTRPVARPHFRLRRRAEG 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VNQAFGVELRHFDHPDGSYRSYVGDVRVPASIAPLIEAVLGLDTRPVARPHFRLRRRAEG 180
Qy 181 EFEARSQSAAPTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDETSLAQYFASLGVS 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 EFEARSQSAAPTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDETSLAQYFASLGVS 240
Qy 241 APQVVSVSVDGATNQPTGDPNGPDGEVELDIEVAGALAPGAKIAVYFAPNTDAGFLNAIT 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 APQVVSVSVDGATNQPTGDPNGPDGEVELDIEVAGALAPGAKIAVYFAPNTDAGFLNAIT 300
Qy 301 TAVHDPTHKPSIVSISWGGPEDSWAPASIAAMNRAFLDAAALGVTVLAAAGDSGSTDGEQ 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 TAVHDPTHKPSIVSISWGGPEDSWAPASIAAMNRAFLDAAALGVTVLAAAGDSGSTDGEQ 360
Qy 361 DGLYHVDFPAASPYVLACGGTRLVASAGRIERETVWNDGPDGGSTGGGVSRIFPLPSWQE 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 DGLYHVDFPAASPYVLACGGTRLVASAGRIERETVWNDGPDGGSTGGGVSRIFPLPSWQE 420
Qy 421 RANVPPSANPGAGSGRGVPDVAGNADPATGYEVVIDGETTVIGGTSAVAPLFAALVARIN 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 RANVPPSANPGAGSGRGVPDVAGNADPATGYEVVIDGETTVIGGTSAVAPLFAALVARIN 480
Qy 481 QKLGKPVGYLNPTLYQLPPEVFHDITEGNNDIANRARIYQAGPGWDPCTGLGSPIGIRLL 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 QKLGKPVGYLNPTLYQLPPEVFHDITEGNNDIANRARIYQAGPGWDPCTGLGSPIGIRLL 540
Qy 541 QALLPSASQAQP 552
||||||||||||
Db 541 QALLPSASQAQP 552
In the instant case, both Sun and Siegel teach the use of S53 proteases in food products. It would have been obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have used SEQ ID No. 16 of Seigel as the protease in the method of Sun. One of ordinary skill in the art would have been motivated to do so to eliminate heat-unstable proteins that cause heat-induced haze or precipitates in food products. One of ordinary skill in the art would have had a reasonable expectation of success for doing so because the use of functional equivalents is routinely practiced in the art.
Regarding claims 3 and 5, SEQ ID No. 16 of Siegel comprises an active site comprising the amino acid substitution E266 as highlighted on the sequence above.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Sun et al. (US 20030165592 – IDS Filed on November 13, 2025) as evidenced by Dong et al. (Bioinformatic mapping of a more precise Aspergillus niger degradome. Scientific Reports. Vol 11. Iss 693. (2021)).
Sun does not teach a protein load of the protease in the composition does not exceed 1%.
Absent a definition in the instant specification, the broadest reasonable interpretation of “protein load of the protease” encompasses the amount of protein substrate embedded in the protease active sites. Therefore the protein load of the protease in the composition not exceeding 1% would mean that no more than 1% of the active sites have protein substrates embedded within them at any point in the process.
Given that Sun teaches removal of heat unstable protein with S53 protease, it would be prima facie obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to practice the method of Sun to remove all the heat unstable protein with the S53 protease. By removing all of the heat unstable protein with the S53 protein, the protein load on S53 protease would be zero. One of ordinary skill in the art would have been motivated to do so to remove all the heat unstable protein from wine, as taught by Sun. One of ordinary skill in the art would have had a reasonable expectation of success because Sun established that S53 protein removes heat unstable protein from wine.
Claims 12 and 13 are rejected under 35 U.S.C. 103 as being unpatentable over Sun et al. (US 20030165592 – IDS Filed on November 13, 2025) as evidenced by Dong et al. (Bioinformatic mapping of a more precise Aspergillus niger degradome. Scientific Reports. Vol 11. Iss 693. (2021)), as applied to claim 1 above, and further in view of Benucci et al. (Immobilised native plant cysteine proteases: packed-bed reactor for white wine protein stabilisation. J Food Sci Technol. Vol 53. Iss (2) Pp. 1130–1139. (2016)).
Regarding claim 12, Sun does not teach the protease is immobilized on a solid support prior to contacting with the beverage of interest.
Benucci teaches a method of using a packed bed reactor (PBR) containing immobilized native plant cysteine proteases as a specific and mild alternative technique relative to the usual bentonite fining for white wine protein stabilization (p. 1130, paragraph 1). Benucci teaches one ideal solution for protein stabilization, suitable for industrial-scale use, would be the treatment of unstable white wine in a continuous flow reactor, such as a PBR, so as to assure the reuse of immobilized protease without a separation step (p. 1131, paragraph 4). Benucci teaches a PBR is also more cost effective than batch operation and the easy automation and control of the system allow a greater productivity, as well as an improved enzyme stability (p. 1131, paragraph 4). Benucci teaches the PBR consists of an unbreakable glass tube with internal volume of 7.29 cm3 (i.e., a solid support) – p. 1132, paragraph 3). Benucci teaches the column was packed with 5.3 g of biocatalyst (i.e., protease) and the lower and upper ends of the tube were layered with glass beads (p. 1132, paragraph 3). Benucci teaches The PBR was connected to the rest of the apparatus and a peristaltic pump was used for feeding in the model wine (i.e., the beverage of interest), fortified with the synthetic substrate, which moved upwards in the column at varying flow rates (p. 1132, paragraph 3). Therefore, Benucci teaches the protease is immobilized on a solid support prior to contacting with the beverage of interest.
Sun and Benucci are combinable because they are concerned with the same field of endeavor, namely, enzymatic stabilization of white wine protein. It would have been obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have utilized a PBR for the administration of the protease in the method of Sun, as taught by Benucci because PBRs are suitable of industrial use, assure the reuse of immobilized protease without a separation step, and are cost effective.
Regarding claim 13, Benucci teaches The PBR was connected to the rest of the apparatus and a peristaltic pump was used for feeding in the model wine, fortified with the synthetic substrate, which moved upwards in the column at varying flow rates (p. 1132, paragraph 3). Therefore, the PBR of Benucci comprises a solid support which is a column or another device that permits the beverage to flow through and to contact the immobilized protease.
Claim 17 is rejected under 35 U.S.C. 103 as being unpatentable over Sun et al. (US 20030165592 – IDS Filed on November 13, 2025) as evidenced by Dong et al. (Bioinformatic mapping of a more precise Aspergillus niger degradome. Scientific Reports. Vol 11. Iss 693. (2021)), as applied to claim 1 above, and further in view of Lopez et al. (Effective Prevention of Chill-Haze in Beer Using an Acid Proline-Specific Endoprotease from Aspergillus niger. J. Agric. Food Chem. Vol 53. Pp. 7944-7949. (2005)).
Sun does not teach the wine (i.e., the beverage of interest) is fermented grain.
Lopez investigates the effectiveness of an Aspergillus niger-native prolyl endoprotease on haze prevention in beer. Lopez teaches surprisingly low dosages of the A. niger protease could stabilize beer as effectively as the conventionally used polyvinylpolypyrrolidone (PVPP), but yielding a final product containing higher polyphenol levels and featuring higher reducing capacities than PVPP-treated beers (p. 7948, paragraph 3). Lopez teaches adverse effects of the enzyme on beer foam stability were almost absent (p. 7948, paragraph 3).
Sun and Lopez are combinable because they are concerned with the same field of endeavor, namely, use of Aspergillus niger protease to prevent haze in alcoholic beverages. It would have been obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have used the method of Sun on beer (i.e., a fermented grain) instead of wine, as taught by Lopez, because Aspergillus niger protease, which comprises the S53 enzymes evidenced by Dong, and the prolyl endoprotease described by Lopez, which stabilizes beer and yields a final product with high polyphenol content without loss of foam stability.
Response to Arguments
Applicant's arguments filed July 23, 2026 have been fully considered but they are not persuasive.
Applicant argues the evidence presented does not establish the protease of Sun comprises S53 serine peptidases (p. 6, paragraph 4).
Applicant’s argument has been carefully considered however the argument is not persuasive. Sun teaches a method of rendering wine heat-stable comprising the step of: adding to wine, prior to bottling, a protease that will hydrolyze proteins that cause heat-induced protein haze or precipitate ([0028]). Sun teaches the protease is Aspergillus niger ([0074]). While Sun does not name the S53 class of enzymes as present in the protease, Sun indicates broadly that the protease can be anything from the noted sources, so long as it has sufficient activity at fruit pH to eliminate heat-unstable proteins ([0063]). The fact that Sun is silent with respect to the class of the proteases, does not mean that the proteases described by Sun were necessarily not in the S53 class. Simply put, any protease that produces the effect required in [0063] would work, which would include S53 proteases. This is not based on inherency, but a broad interpretation of the disclosure of Sun.
Applicant argues Sun does not teach the protein-removal limitation of claim 21 (p. 7, paragraph 2).
Applicant’s argument has been carefully considered however the argument is not persuasive. Sun teaches the addition of protease at 180 and 540 mg/L effectively eliminated all of the heat-induced precipitate from grape/wine proteins (i.e., at least 85% of heat-unstable proteins are removed – Example 1; [0093]). Furthermore, with respect to the SDS-PAGE data provided by Sun, Sun states most wine researchers found wine proteins in the molecular weight range of 20,000-30,000 Dalton are responsible for heat-induced protein precipitation ([0112]). However, when the wine samples are heated under the same condition as the heat test, no protein bands appear in the SDS-PAGE analysis ([0112]). Sun states the results of the above SDS-PAGE tests provide strong supporting data that protease can indeed hydrolyze (i.e., remove) the heat-unstable proteins when used under the standard winemaking conditions prescribed above ([0113]). Therefore, while Sun is silent with respect to the exact percent removal of heat-unstable proteins, the evidence provided by Sun in the SDS-PAGE gels shows at least 85% of heat-unstable proteins are removed from the wine.
Applicant argues there is no reasonable expectation that Siegel’s SEQ IN NO: 16 would dehaze wine (p. 8, paragraph 2).
Applicant’s argument has been carefully considered however the argument is not persuasive. While Sun discourages the use of Bromelain, Sun is silent regarding Siegel’s SEQ IN NO: 16. With respect to the ability of Siegel’s SEQ ID NO: 16 to dehaze wine, claim 1 only requires "contacting" the enzyme and the beverage but does not specifically require any degree of dehazing or any other effect. The method also does not require the enzyme per se to be the cause of the dehazing. There is no requirement in claim 1 for the S53 protease to be an active dehazing agent, nor for it to be the only protease contacted with the beverage.
Applicant argues Lopez does not teach using an S53 protease enzyme in beer (p. 9, paragraph 2).
Applicant’s argument has been carefully considered however the argument is not persuasive. Lopez is not relied upon to provide the rationale for using an S53 protease enzyme in beer. Lopez provides the rationale to utilize the method of Sun on beer instead of wine, because Aspergillus niger protease is also known to be useful for beer-making. It would have been obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have used the method of Sun on beer (i.e., a fermented grain) instead of wine, as taught by Lopez, because Aspergillus niger protease, which comprises S53 enzymes evidenced by Dong, and prolyl endoprotease described by Lopez, stabilizes beer and yields a final product with high polyphenol content without loss of foam stability.
Conclusion
No claims are allowed.
THIS ACTION IS MADE FINAL. 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 LARK JULIA MORENO whose telephone number is (571)272-2337. The examiner can normally be reached 6:30 - 4:30 M - F.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Emily Le can be reached at (571) 272-0903. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/JEFFREY P MORNHINWEG/Primary Examiner, Art Unit 1793
/L.J.M./Examiner, Art Unit 1793
Prosecution Insights