Prosecution Insights
Last updated: April 19, 2026
Application No. 17/615,675

CROSS-LINKED MILK PROTEIN CO-PRECIPITATE

Non-Final OA §103§112
Filed
Dec 01, 2021
Examiner
KERSHAW, KELLY P
Art Unit
1791
Tech Center
1700 — Chemical & Materials Engineering
Assignee
Novozymes A/S
OA Round
5 (Non-Final)
18%
Grant Probability
At Risk
5-6
OA Rounds
3y 2m
To Grant
35%
With Interview

Examiner Intelligence

Grants only 18% of cases
18%
Career Allow Rate
36 granted / 201 resolved
-47.1% vs TC avg
Strong +17% interview lift
Without
With
+17.1%
Interview Lift
resolved cases with interview
Typical timeline
3y 2m
Avg Prosecution
80 currently pending
Career history
281
Total Applications
across all art units

Statute-Specific Performance

§101
2.0%
-38.0% vs TC avg
§103
40.4%
+0.4% vs TC avg
§102
21.2%
-18.8% vs TC avg
§112
25.8%
-14.2% vs TC avg
Black line = Tech Center average estimate • Based on career data from 201 resolved cases

Office Action

§103 §112
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 . Status of the Application Receipt of the Request for Continued Examination (RCE under 37 CFR 1.114), the Response, and Amendment filed 01/06/2026 is acknowledged. Applicant has overcome the following rejections by virtue of the amendment: the 35 U.S.C. §112(d) rejections of claims 19-20 have been withdrawn. The status of the claims upon entry of the present amendment stands as follows: Pending claims: 1-6, 9-13, 15-24 Withdrawn claims: 1-6, 9, 15-16 Previously cancelled claims: 7-8, 14 Newly cancelled claims: None Amended claims: 10, 13, 18-20 New claims: 21-24 Claims currently under consideration: 10-13, 17-24 Currently rejected claims: 10-13, 17-24 Allowed claims: None 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 01/06/2026 has been entered. Claim Rejections - 35 USC § 112 The following is a quotation of the first paragraph of 35 U.S.C. 112(a): (a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention. Claims 10-13 and 17-24 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. Claims 10 and 19 recite a step of combining the dissolved cross-linked milk protein co-precipitate, the first milk substrate of step (a), and water to form a mixed milk substrate wherein the mixed milk substrate has the same volume as the first milk substrate of step (a). However, neither the present specification nor previous versions of the claim set recites the addition of water to the dissolved cross-linked milk protein co-precipitate and the first milk substrate of step (a). Therefore, the addition of water at this step constitutes new matter. Claims 11-13, 17-18, and 20-24 are rejected by reason of dependency from claim 10. 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 10-12, 18-20, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Sasaki (US 2009/0068312; previously cited) in view of Ottenhof (US 4,519,945; previously cited) as evidenced by Dairy UK (“The Nutritional Composition of Dairy Products”, 2025, Dairy UK, https://milk.co.uk/nutritional-composition-of-dairy/milk/; previously cited) and Dairy (“Nutritional Composition of Skim Milk Powder”, 2025, Dairy for Global Nutrition, https://www.dairyglobalnutrition.org/nutrition/ milk-powder; previously cited). Regarding claim 10 and 19, Sasaki teaches a method for preparing an acidified milk product (corresponding to yogurt) [0012], the method comprising: treating a dissolved milk protein (corresponding to whey protein solution) with transglutaminase to form a dissolved cross-linked milk protein [0024]; mixing the dissolved cross-linked milk protein with a second milk substrate (corresponding to adding the modified whey protein to a raw material milk) to form a mixed milk substrate [0028]; pasteurizing the mixed milk substrate (corresponding to maintaining the mixture at 95°C for 5 minutes) [0034]; and acidifying the substrate to obtain an acidified milk product [0028], [0034]. Sasaki teaches that the addition of the transglutaminase-treated milk protein to the raw material milk advantageously uses a very small amount of transglutaminase, while preventing water separation and increasing viscosity of the product without significantly changing the original flavor and texture of the product [0006], [0027]. Sasaki also discloses an example wherein 53 parts of cow milk, 4.8 parts of skim milk powder, and 39.5 parts water were combined to form a yogurt mix; and wherein 94 parts of the yogurt mix was combined with 3 parts of the whey protein solution comprising the transglutaminase-treated milk protein so that the resulting substrate (corresponding to raw material milk) comprises 0.5 wt.% transglutaminase-treated milk protein [0033]-[0034]. Whole cow milk comprises 3.5 wt.% protein as evidenced by Dairy UK (3rd row of table) while skim milk powder comprises 34-37 wt.% protein as evidenced by Dairy (1st row of table). Therefore, Sasaki exemplifies a mixed milk substrate wherein 11.9 -12.5 wt.% of the total protein in the substrate is obtained from the transglutaminase-treated milk protein, which falls within the range of 10-30 wt.% of total protein recited in present claim 10. Furthermore, as the cost, water separation, viscosity, flavor, and texture are variables that can be modified, among others, by adjusting the contents of transglutaminase-treated milk protein and the raw material milk (consequently, the amount of protein within the raw material milk), the contents of transglutaminase-treated milk protein and the protein in the raw material milk would have been considered a result effective variable by one having ordinary skill in the art before the effective filing date of the invention. As such, without showing unexpected results, the claimed contents of transglutaminase-treated milk protein and the protein in the raw material milk cannot be considered critical. Accordingly, one of ordinary skill in the art before the effective filing date of the invention would have optimized, by routine experimentation, contents of transglutaminase-treated milk protein and the protein in the raw material milk in the yogurt of Sasaki using the 11.9 -12.5 wt.% of transglutaminase-treated protein content based on the weight of total protein in order to obtain the desired balance between characteristics in the resulting yogurt (In re Boesch, 617 F.2d. 272, 205 USPQ 215 (CCPA 1980)), since it has been held that where the general conditions of the claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. (In re Aller, 105 USPQ 223). MPEP § 2144.05.II. Sasaki teaches that the method of producing the whey protein solution is not particularly limited and that the whey protein solution may be powdered. Sasaki discloses that the protein content in the solids of the whey protein solution is 80-100% [0018]. Sasaki also teaches that the acidified milk product has improved textural properties when compared to an acidified milk product produced by a method where the dissolved cross-linked protein is not added (corresponding to rich feel, smooth structure, and less water separation) [0005], [0012]. Sasaki does not teach: (1) a method of producing the powdered whey protein solution; (2) that the first milk substrate of step (a) and water are combined with the dissolved cross-linked milk protein co-precipitate of step (f) or step (g) to form a mixed milk substrate having the same volume as the first milk substrate in step (a); (3) that the concentration of lactose and protein in the mixed milk substrate comprising the dissolved cross-linked milk protein co-precipitate is less than that of the second milk substrate; or (4) that the concentration of lactose and of milk protein in the acidified milk product comprising the dissolved cross-linked milk protein co-precipitate is less than that of an acidified milk product produced by a method which does not add dissolved cross-linked milk protein co-precipitate as recited by present claims 10 and 19. However, Ottenhof teaches a method for preparing a milk protein co-precipitate (column 1, lines 61-63), the method comprising the steps of: (b) heating a milk substrate comprising casein and whey protein under conditions so that 100 wt.% of the whey protein is denatured (corresponding to heating the at a temperature and for a time at least sufficient to denature the whey protein) (column 3, lines 26-29); (c) adjusting the pH of the heated milk substrate of step (a) to a pH of 4.4-4.7, thereby precipitating 96 wt.% of the milk protein originally present in the milk substrate (corresponding to curd formation) (column 3, lines 42-51; column 5, lines 9-11); and (d) separating a fraction comprising the precipitated milk protein of step (c), thereby obtaining a milk protein co-precipitate (column 3, lines 54-56). Ottenhof teaches that water may be added to the milk protein co-precipitate (corresponding to dissolving the co-precipitate in water) (column 4, lines 5-8). The amount of denatured whey protein disclosed by Ottenhof in step (b) falls within the claimed range; and the amount of precipitated milk protein disclosed by Ottenhof in step (c) falls within the claimed range. Ottenhof teaches that the method then comprises the steps of: (e) adjusting the pH of the milk protein co-precipitate of step (d) to a pH of 6.5-8.0 (column 4, lines 5-8) such as 6.7 (column 5, lines 14-17), thereby dissolving 95 wt.% of the precipitated milk protein (corresponding to a protein solubility of 95) to produce a dissolved cross-linked milk protein co-precipitate (column 5, line 25). The pH and protein solubility disclosed by Ottenhof fall with the claimed ranges. Ottenhof discloses that the milk protein co-precipitate is suitable for use in food (corresponding to baby food, meat products, foam compositions) due to its excellent solubility (column 2, lines 9-14). Ottenhof also discloses that the co-precipitate may contain 35-50 wt.% dry solids (column 4, lines 5-6) and that the protein may comprise about 98 wt.% of the dry solids (corresponding to the co-precipitate containing 96.3 wt.% dry solids and 93.9 wt.% protein when dried into a powder) (column 5, lines 18-21). It would have been obvious for a person of ordinary skill in the art to have modified the method of Sasaki by producing a whey protein solution as taught by Ottenhof. Since Sasaki teaches that its method begins with treating a whey protein solution with transglutaminase to form a cross-linked milk protein [0024] and that the protein content in the solids of the whey protein solution is 80-100% [0018], but does not disclose a method of producing the whey protein solution having such a protein content, a skilled practitioner would have been motivated to consult an additional reference such as Ottenhof in order to determine a suitable method of producing a whey protein solution (i.e., dissolved milk protein) comprising a protein content of 80-100% relative to the dry solids. Since Ottenhof discloses method steps corresponding to the claimed steps (c)-(e) in order to produce a whey protein solution having a protein content relative to a dry solids content of 98 wt.%, which falls within the range of 80-100% required by Sasaki, the combination of Ottenhof and Sasaki renders the claimed steps (c)-(e) obvious. In disclosing subsequent treatment of the whey protein solution comprising: treating a dissolved milk protein (corresponding to whey protein solution) with transglutaminase to form a dissolved cross-linked milk protein [0024]; mixing the dissolved cross-linked milk protein with a second milk substrate (corresponding to adding the modified whey protein to a raw material milk) to form a mixed milk substrate [0028]; pasteurizing the mixed milk substrate (corresponding to maintaining the mixture at 95°C for 5 minutes) [0034]; and acidifying the substrate to obtain an acidified milk product [0028], [0034], Sasaki discloses steps (f)-(i) of the claimed method, thereby rendering steps (f)-(i) obvious. The combination of Sasaki and Ottenhof does not disclose that the method comprises obtaining a first milk substrate, wherein the substrate comprises casein and whey; and removing a portion of the first milk substrate as recited in steps (a) and (b) of present claim 10. However, Sasaki discloses that the co-precipitate is made from cow milk; and that the co-precipitate is added to a raw material milk [0014] which also contains cow milk [0033]. Therefore, the first milk substrate and the second milk substrate of the prior art may be cow’s milk and the prior art thus suggests using a particular amount of cow’s milk to form the co-precipitate and adding the formed co-precipitate to another amount of cow’s milk (e.g., using 20 grams of cow’s milk to form a co-precipitate and adding the co-precipitate to 80 grams of cow’s milk to form a mixed milk substrate). This suggested method may provide the same effect as obtaining a first milk substrate and removing a portion of the first milk substrate as recited in claimed steps (a) and (b) (e.g., a first milk substrate contains 100 grams of milk substrate and 20 grams of the first milk substrate is portioned out to form a co-precipitate; then the co-precipitate is added to the remaining 80 grams of the first milk substrate to form a mixed milk substrate). For these reasons, Sasaki is considered to render the claimed features of obtaining a first milk substrate, wherein the substrate comprises casein and whey; and removing a portion of the first milk substrate as recited in steps (a) and (b) of present claim 10 obvious. In regard to combining the first milk substrate of step (a) and water with the dissolved cross-linked milk protein co-precipitate of step (f) or step (g) to form a mixed milk substrate having the same volume as the first milk substrate in step (a), Ottenhof discloses that water may be added to the milk protein co-precipitate; and Sasaki discloses that the solid content in the whey protein solution may be 3-30 wt.% [0019], thereby providing motivation to add water to the milk protein co-precipitate until the solids content reaches 3-30 wt.%. Since Sasaki at least suggests that the first milk substrate in step (a) of the method may be cow’s milk as explained above and cow’s milk typically has a solids content of about 13 wt.%, the prior art is considered to at least suggest adding amounts of water which would lead to the mixed milk substrate having the same volume as the first milk substrate in step (a) (i.e., the volume of the first substrate of the prior art being the combined amounts of milk used to make the co-precipitate and the milk with which the co-precipitate is combined as described above), thereby rendering obvious the limitation requiring the volume of the mixed milk substrate to be the same as the volume of the first milk substrate in step (a). Furthermore, since Ottenhof discloses adding water to the milk protein co-precipitate, this step renders obvious the claimed step of adding water with the cross-linked co-precipitate to form the mixed milk substrate recited in present claims 10 and 19, specifically wherein a skilled practitioner would recognize that water may be added at multiple steps in the process to achieve a particular taste in the resulting product. In regard to the acidified milk product containing the dissolved cross-linked protein co-precipitate having improved textural properties when compared to an acidified milk product produced by a method where the dissolved cross-linked protein co-precipitate is not added, Sasaki discloses that the acidified milk product has improved textural properties when compared to an acidified milk product produced by a method where the dissolved cross-linked protein is not added (corresponding to rich feel, smooth structure, and less water separation) [0005], [0012]. Since the combination of prior art discloses that the dissolved cross-linked protein is a dissolved cross-linked protein co-precipitate, the prior art at least suggests that the acidified milk product containing the dissolved cross-linked protein co-precipitate has improved textural properties when compared to an acidified milk product produced by a method where the dissolved cross-linked protein co-precipitate is not added. Therefore, the claimed improved textural properties as recited in present claim 10 are rendered obvious. In regards to the concentration of lactose in the mixed milk substrate comprising the dissolved cross-linked milk protein co-precipitate being less than that of the second milk substrate; and the concentration of lactose in the acidified milk product comprising the dissolved cross-linked milk protein co-precipitate being less than that of an acidified milk product produced by a method which does not add dissolved cross-linked milk protein co-precipitate, the addition of dissolved cross-linked milk precipitate to the second substrate as disclosed by Sasaki [0028] would necessarily result in a decrease of components such as lactose in the second substrate (e.g., the addition of dissolved cross-linked milk protein co-precipitate to a second substrate to form the mixed milk substrate, wherein the addition results in the substrate containing 10 wt.% of the co-precipitate; and wherein the second substrate contained 10 wt.% lactose prior to the addition of the co-precipitate would result in the amount of lactose in the mixed milk substrate being reduced to 9 wt.%). Since the acidified milk product is made from the mixed milk substrate comprising the dissolved cross-linked milk protein co-precipitate, the acidified milk product would also necessarily have a lower lactose content than an acidified milk product produced by a method which does not add dissolved cross-linked milk protein co-precipitate. Therefore, the claimed lower lactose content in the mixed milk substrate comprising the dissolved cross-linked milk protein co-precipitate and in the acidified milk product comprising the dissolved cross-linked milk protein co-precipitate as recited by present claim 10 are inherently disclosed by the prior art. In regards to the concentration of protein in the mixed milk substrate comprising the dissolved cross-linked milk protein co-precipitate being less than that of the second milk substrate; and the concentration of protein in the acidified milk product comprising the dissolved cross-linked milk protein co-precipitate being less than that of an acidified milk product produced by a method which does not add dissolved cross-linked milk protein co-precipitate, the combination of prior art discloses the presently claimed method, including the step of adding the dissolved cross-linked milk protein co-precipitate to the second substrate to form a mixed milk substrate and the step of acidifying the mixed milk substrate to produce the acidified milk product. Therefore, the method of the prior art provides the same results seen in the claimed method including a concentration of protein in the mixed milk substrate being lower than in the second substrate and a concentration of protein in the acidified milk product being less than that of an acidified milk product without added dissolved cross-linked milk protein co-precipitate. The lower protein concentrations seen in the mixed milk substrate and the resulting acidified milk product of the prior art are due to the dissolved cross-linked milk protein co-precipitate being a solution comprising water (among potentially other ingredients), wherein the addition of the water to the second substrate dilutes the second substrate (and the proteins within the substrate), thereby providing a mixed milk substrate that is more dilute than the second substrate and containing a lower protein concentration than the undiluted second substrate. This lower protein concentration would be also observed in the acidified milk product produced from the mixed milk substrate. As such, the prior art renders the claimed lower protein concentrations as recited by present claim 10 obvious. Regarding claim 11, Sasaki teaches the invention as described above in claim 10, including the mixed milk substrate is acidified to 4.6 [0034], which falls within the claimed range. Regarding claim 12, modified Sasaki teaches the invention as described above in claim 10, including the milk substrate is heated to a temperature of 80-100°C for 5-20 minutes, such as 90-98°C for 8-12 minutes (Ottenhof, column 3, lines 26-31), which fall within the claimed temperature and time frames. Regarding claim 18, Sasaki teaches the invention as described above in claim 10, including the amount of dissolved cross-linked milk protein co-precipitate added to the first milk substrate is 0.05-3 wt.% based on the weight of the dissolved cross-linked milk protein co-precipitate (corresponding to the solution of the modified whey protein is added to raw material milk of a yogurt in an amount of 0.05% to 3% of the raw material milk in terms of the weight of the whey protein) [0027]. Sasaki also discloses that the amount of whey in the solution used to produce the dissolved cross-linked milk protein co-precipitate is 3-30 wt.% ([0018], claim 1). Therefore, the dissolved cross-linked milk protein co-precipitate in the second milk substrate is an amount from 0.0015 wt.% (corresponding to a 3 wt.% whey solution providing 0.05 wt.% modified whey to the raw material) to an amount of 100 wt.%. As such, Sasaki discloses that the dissolved cross-linked milk protein co-precipitate is added to the raw milk in a range of ratios which encompass the claimed ratio. It would have been obvious to one of ordinary skill in the art to select any portions of the disclosed ranges including the instantly claimed ranges from the ranges disclosed in the prior art references, particularly in view of the fact that; "The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set percentage ranges is the optimum combination of percentages" In re Peterson 65 USPQ2d 1379 (CAFC 2003). Also In re Malagari, 182 USPQ 549,533 (CCPA 1974) and MPEP §2144.05.I. Regarding claim 20, modified Sasaki teaches the invention as described above in claim 10, including that water may be added to the milk protein co-precipitate (Ottenhof, column 4, lines 5-8); and that the solid content in its whey protein solution may be 3-30 wt.% (Sasaki [0019]), thereby providing motivation to add water to the milk protein co-precipitate until the solids content reaches 3-30 wt.%. Since Sasaki at least suggests that the first milk substrate in step (a) of the method may be cow’s milk as explained above in the rejection of claim 10 and cow’s milk typically has a solids content of about 13 wt.%, the prior art is considered to at least suggest adding amounts of water which would lead to the milk protein co-precipitate having the same volume as the portion of the first milk substrate removed in step (b), thereby rendering present claim 20 obvious. Regarding claim 24, Sasaki teaches the invention as described above in claim 10, including the subsequent treatment of the whey protein solution comprising: treating a dissolved milk protein (corresponding to whey protein solution) with transglutaminase to form a dissolved cross-linked milk protein [0024]; mixing the dissolved cross-linked milk protein with a second milk substrate (corresponding to adding the modified whey protein to a raw material milk) to form a mixed milk substrate [0028]; pasteurizing the mixed milk substrate (corresponding to maintaining the mixture at 95°C for 5 minutes) [0034]; and acidifying the substrate to obtain an acidified milk product [0028], [0034]. Therefore, Sasaki discloses steps (f)-(i) of the claimed method, including a step of pasteurization. Although Sasaki discloses a step of pasteurization to occur after the dissolved cross-linked milk protein co-precipitated of step (f) is mixed with the first milk substrate of step (a), the “selection of any order of mixing ingredients is prima facie obvious”. MPEP 2144.04.IV(C). Therefore, the claim is rendered obvious. Claims 13, 17, and 21-23 are rejected under 35 U.S.C. 103 as being unpatentable over Sasaki (US 2009/0068312; previously cited) in view of Ottenhof (US 4,519,945; previously cited) as evidenced by Dairy UK (“The Nutritional Composition of Dairy Products”, 2025, Dairy UK, https://milk.co.uk/nutritional-composition-of-dairy/milk/) and Dairy (“Nutritional Composition of Skim Milk Powder”, 2025, Dairy for Global Nutrition, https://www.dairyglobalnutrition.org/nutrition/ milk-powder) as applied to claim 10 above, and further in view of Bech (US 6,190,879; previously cited). Regarding claims 13, 21, 22, and 23, Sasaki teaches the invention as described above in claim 10, including the transglutaminase in the method has transglutaminase activity and may be derived from a microorganisms belonging to the genus Streptomyces [0021]. Sasaki does not teach that the transglutaminase has at least 60% homology to SEQ ID NO:1. However, Bech teaches a transglutaminase having transglutaminase activity, wherein the transglutaminase is isolated from microorganisms of the Streptomyces genus (column 3, lines 15-17; column 7, lines 24-25) and is used to prepare milk products (column 3, lines 63-66). Bech also teaches that its transglutaminase is SEQ ID NO: 3 (column 41- column 43) which has 100% homology to claimed SEQ ID NO: 1 (see Result 1 in the search report titled “Pending_Patents_AA_Main” filed 08/05/2024), which falls within the claimed range of homology recited in present claims 13, 21, 22, and 23. It would have been obvious for a person of ordinary skill in the art to have modified the method of Sasaki to include using the transglutaminase taught by Bech. Since Sasaki discloses that the transglutaminase used in its yogurt-making method has transglutaminase activity and may be derived from a microorganisms belonging to the genus Streptomyces [0021], but does not disclose a specific enzyme having such features, a skilled practitioner would have been motivated to consult an additional reference such as Bech in order to determine a suitable transglutaminase. Therefore, the claimed transglutaminase recited in present claims 13, 21, 22, and 23 is rendered obvious. Regarding claim 17, modified Sasaki teaches the invention as described above in claim 10, including producing a whey protein solution containing casein and whey co-precipitate (Ottenhof, column 3, lines 26-29, 42-51, 54-56; column 5, lines 9-11) and treating the whey protein solution with transglutaminase to form cross-linked milk protein (Sasaki [0024]). Therefore, modified Sasaki teaches that the cross-linked milk protein co-precipitate of step (f) is characterized by comprising cross-linked casein and whey protein [0024]. It also teaches that the transglutaminase in the method has transglutaminase activity and may be derived from a microorganism belonging to the genus Streptomyces (Sasaki [0021]). It does not teach that the casein and whey protein are crosslinked by iso-peptide cross-linking bonds between glutamine and lysine residues of the casein and whey protein polypeptides. However, Bech teaches a transglutaminase having transglutaminase activity, wherein the transglutaminase is isolated from microorganisms of the Streptomyces genus (column 3, lines 15-17; column 7, lines 24-25) and is used to prepare milk products (column 3, lines 63-66). Bech also teaches that its transglutaminase forms iso-peptide cross-linking bonds between glutamine and lysine residues (corresponding to the transglutaminase catalyzing an acyl transfer reaction to form γ-glutamyl-ε-lysyl crosslinks) (column 1, lines 21-30). It would have been obvious for a person of ordinary skill in the art to have modified the method of Sasaki to include using the transglutaminase taught by Bech. Since Sasaki discloses that the transglutaminase used in its yogurt-making method has transglutaminase activity and may be derived from microorganisms belonging to the genus Streptomyces [0021], but does not disclose a specific enzyme having such features, a skilled practitioner would have been motivated to consult an additional reference such as Bech in order to determine a suitable transglutaminase. In using the transglutaminase of Bech in the method of Sasaki, the cross-linked milk protein co-precipitate of step (f) is characterized by comprising casein and whey protein crosslinked by iso-peptide cross-linking bonds between glutamine and lysine residues of the casein and whey protein polypeptides as presently claimed; therefore, the claim is rendered obvious. Response to Arguments Claim Rejections – 35 U.S.C. §112(d) of claims 19-20: Applicant amended the claims to fully address the rejections; therefore, the rejections are withdrawn. Claim Rejections – 35 U.S.C. §103 of claims 10-13 and 17-20 over Sasaki and Ottenhof as evidenced by Dairy UK and Dairy; claims 13 and 17 Sasaki, Ottenhof, and Bech as evidenced by Dairy UK and Dairy: Applicant’s arguments and amendments have been fully considered and are not considered to overcome the cited prior art. Applicant amended claim 10 to recite that the volume of the mixed milk substrate is the same as the volume of the first milk substrate in step (a) of the claimed method; and that water may be added to the mixture to achieve this volume. Applicant stated that the present specification does not disclose the addition of water during this step (h) of the method, but that a skilled practitioner would recognize that the full amount of water that is disclosed in the present specification as being added during step (d) could be added at multiple steps of the method. Applicant then argued that Sasaki and Ottenhof do not teach or suggest the claimed method as neither reference disclose removing a portion of the starting milk substrate, precipitating milk protein and treating the protein with transglutaminase, and then returning the treated portion to the initial milk substrate and restoring the initial milk substrate to its initial volume (Applicant’s Remarks, pages 6-8, section II). However, per the 35 U.S.C. §112(a) rejection of claims 10 and 19 written above and per Applicant’s admission in the paragraph beginning “Support for claim 10 amendments” on page 7 of Applicant’s Remarks, the present specification does not disclose the claimed method either since the present specification does not disclose adding water at step (h). Therefore, Applicant’s arguments regarding the present specification being the only source of the claimed method for producing an acidified milk product which has improved textural properties and comprises a lower content of lactose and milk protein are not supported. Furthermore, the combination of Sasaki and Ottenhof are shown to render the claims obvious, including the step of adding water at step (h). Since the prior art has been shown to render the claims obvious and Applicant’s arguments have been shown to be unpersuasive, the rejections of the claims are maintained as written herein. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to Kelly Kershaw whose telephone number is (571)272-2847. The examiner can normally be reached Monday - Thursday 9:00 am - 4:00 pm. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Nikki Dees can be reached at (571) 270-3435. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /KELLY P KERSHAW/Examiner, Art Unit 1791
Read full office action

Prosecution Timeline

Dec 01, 2021
Application Filed
Aug 05, 2024
Non-Final Rejection — §103, §112
Nov 11, 2024
Response Filed
Dec 20, 2024
Final Rejection — §103, §112
Feb 19, 2025
Response after Non-Final Action
Mar 05, 2025
Request for Continued Examination
Mar 08, 2025
Response after Non-Final Action
Apr 04, 2025
Non-Final Rejection — §103, §112
Jul 09, 2025
Response Filed
Oct 10, 2025
Final Rejection — §103, §112
Dec 15, 2025
Response after Non-Final Action
Jan 06, 2026
Request for Continued Examination
Jan 11, 2026
Response after Non-Final Action
Feb 21, 2026
Non-Final Rejection — §103, §112 (current)

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THERMOLABILE PIGMENTS FOR MEAT SUBSTITUTES DERIVED BY MUTATION OF THE PIGMENT OF CORAL ECHINOPORA FORSKALIANA
2y 5m to grant Granted Aug 05, 2025
Patent 12336556
COMPOSITIONS FOR RETARDING RANCIDITY IN OIL-BASED FOOD SAUCES AND DRESSINGS
2y 5m to grant Granted Jun 24, 2025
Patent 12048316
SWEETENER AND FLAVOR COMPOSITIONS, METHODS OF MAKING AND METHODS OF USE THEREOF
2y 5m to grant Granted Jul 30, 2024
Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

5-6
Expected OA Rounds
18%
Grant Probability
35%
With Interview (+17.1%)
3y 2m
Median Time to Grant
High
PTA Risk
Based on 201 resolved cases by this examiner. Grant probability derived from career allow rate.

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