Patent Application 17615675 - CROSS-LINKED MILK PROTEIN CO-PRECIPITATE - Rejection

Patent Application 17615675 - CROSS-LINKED MILK PROTEIN CO-PRECIPITATE

Title: CROSS-LINKED MILK PROTEIN CO-PRECIPITATE

Application Information

• Invention Title: CROSS-LINKED MILK PROTEIN CO-PRECIPITATE
• Application Number: 17615675
• Submission Date: 2025-04-10T00:00:00.000Z
• Effective Filing Date: 2021-12-01T00:00:00.000Z
• Filing Date: 2021-12-01T00:00:00.000Z
• National Class: 426
• National Sub-Class: 042000
• Examiner Employee Number: 95276
• Art Unit: 1791
• Tech Center: 1700

Rejection Summary

• 102 Rejections: 0
• 103 Rejections: 2

Cited Patents

The following patents were cited in the rejection:

• US 0068312🔗

Office Action Text

    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 03/05/2025 is acknowledged.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims:				1-6, 9-13, 15-18
Withdrawn claims: 				1-6, 9, 15-16
Previously cancelled claims: 		7-8, 14
Newly cancelled claims:			None
Amended claims: 				10
New claims: 					18
Claims currently under consideration:	10-13, 17-18
Currently rejected claims:			10-13, 17-18
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 03/05/2025 has been entered.

Claim Objections
Claim 10 is objected to because: “wherein the acidified milk product has improved textural properties and comprises a lower content of lactose and of milk protein compared to a method where the dissolved cross-linked protein co-precipitate is not added” should be read as “wherein the acidified milk product has improved textural properties and comprises a lower content of lactose and of milk protein compared to an acidified milk product produced by a method where the dissolved cross-linked protein co-precipitate is not added”.  Appropriate correction is required.

Claim Interpretation
In step (c) of the method of claim 11, the phrase “optionally adding water” will be interpreted as meaning optionally adding water to the milk protein co-precipitate obtained in step (c).

 Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):

(b)  CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.

Claim 18 is rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA  35 U.S.C. 112, the applicant), regards as the invention.
Claim 18  recites a ratio of dissolved cross-linked milk protein co-precipitate to second milk substrate of 80% to 20%, respectively.  However, the claim does not disclose units of measurement associated with the ratio (e.g., weight ratio, volume ratio).  Therefore, the claim is indefinite.  For the purpose of this examination, the ratio will be interpreted as being a weight ratio.

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 and 18 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).
Regarding claim 10, 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].  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 to obtain the desired balance (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.  It discloses that the protein content in the solids of the whey protein solution is 80-100% [0018].  It 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 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 (3) 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.
However, Ottenhof teaches a method for preparing a milk protein co-precipitate (column 1, lines 61-63), the method comprising the steps of: (a) 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); (b) 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 (c) separating a fraction comprising the precipitated milk protein of step (b), thereby obtaining a milk protein co-precipitate (column 3, lines 54-56) and optionally adding water (corresponding to dissolving the co-precipitate in water) (column 4, lines 5-8).  The amount of denatured whey protein disclosed by Ottenhof in step (a) falls within the claimed range; and the amount of precipitated milk protein disclosed by Ottenhof in step (b) falls within the claimed range.  Ottenhof teaches that the method then comprises the steps of: (d) adjusting the pH of the milk protein co-precipitate of step (c) 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) and that the co-precipitate is dried into a powder, wherein the protein content of the solids is about 98% (corresponding to the powder having a dry solids content of 96.3 wt.% and a protein content of 93.9 wt.%) (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 transglutaminase-treated protein powder 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, 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.  Therefore, the claimed steps (a)-(d) are rendered 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 (e)-(h) of the claimed method, thereby rendering steps (e)-(h) obvious.
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 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 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 a 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 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 second 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].  It 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.

Claims 13 and 17 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 applied to claim 10 above, and further in view of Bech (US 6,190,879; previously cited).
Regarding claim 13, 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.
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 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 (e) 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 (e) 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. §103 of claims 10-12 over Sasaki and Ottenhof; claims 13 and 17 over Sasaki, Ottenhof, and Bech: Applicant’s arguments have been fully considered and are considered unpersuasive.
Applicant stated that the presently claimed invention is directed toward making acidified product having improved textural properties while having the same or lower contents of protein and lactose.  Applicant pointed to Example 3 of the present specification as showing that 20% of a yogurt milk was drawn and used as a substrate to produce a dissolved cross-linked milk protein co-precipitate.  Applicant stated that this dissolved cross-linked milk protein co-precipitate was then returned to the yogurt milk from which the substrate for producing the dissolved cross-linked milk protein co-precipitate was drawn.  After this addition, Applicant stated that the mixture was heat-treated, inoculated with starter culture, and allowed to acidify to form an acidified milk product.  Applicant stated that this process leads to a lower lactose and protein content in the recombined yogurt milk and in the resulting acidified milk product as the protein was purified away from lactose during the co-precipitation process and that the co-precipitation process does not capture all of the milk protein originally present in the drawn yogurt milk.  Applicant then argued that the method and resulting acidified milk product of Sasaki are different from the claimed method and resulting product as the method of Sasaki increases the protein content of the acidified milk product while the presently claimed method decreases the protein content of the acidified milk product (Applicant’s Remarks, page 5, 1st paragraph under section I – page 6, 1st paragraph).
However, the presently claimed invention recites that the formation of the dissolved cross-linked milk protein co-precipitate occurred on a first milk substrate and that the formation of the mixed milk substrate and resulting acidified milk product occurred by combining the dissolved cross-linked milk protein co-precipitate with a second milk substrate.  These disclosures of “a first milk substrate” and “a second milk substrate” as well as the absence of steps (1) directed toward drawing of a portion of a milk substrate to produce the dissolved cross-linked milk protein co-precipitate and (2) directed to recombining the drawn portion containing the dissolved cross-linked milk protein co-precipitate with the remaining initial milk substrate indicate that the first milk substrate and the second milk substrate are different substrates, wherein one substrate is not a drawn portion of the other substrate and wherein the two substrates are not recombined.  Therefore, the claims are not commensurate in scope with Applicant’s arguments or with Example 5 of the present specification.  
In response to the assertion that Sasaki is different from the claimed method and its resulting product, the combination of Sasaki and Ottenhof are shown to render the presently claimed method obvious as described in the rejection of claim 10 above.  In response to the assertion that the method of Sasaki increases the protein content of the acidified milk product while the presently claimed method decreases the protein content of the acidified milk product, as described above in the rejection of claim 10, the combination of prior art discloses the presently claimed method, including the step of adding the dissolved cross-linked milk protein co-precipitate to a 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 obvious.
Applicant then argued that Ottenhof does not remedy the deficiencies of Sasaki (Applicant’s Remarks, page 6, 2nd paragraph).
However, the combination of Sasaki and Ottenhof has been shown to render amended claim 10 as well as claims 11-12 obvious.  The combination of Sasaki, Ottenhof, and Bech has been shown to render claims 13 and 17 obvious.  Since the prior art has been shown to render the present claims obvious and Applicant’s arguments have been shown to be unpersuasive, the rejections of the claims are maintained as written herein.

Conclusion
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/KELLY P KERSHAW/Examiner, Art Unit 1791