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 .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 9/23/2025 has been entered.
Status of claims
Claims 1-8 and 10-16 as amended on 9/08/2025 are pending and under examination in the instant office action.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1-3, 7, 8 and 10-16 are rejected under 35 U.S.C. 103 as being unpatentable over CN 106480142 (Cheng et al), Leon-Lopez et al (“Hydrolyzed Collagen - Sources and Applications”, Macromolecules. 2019, published 11/07/2019, 4031, pages 1-16), Schmidt et al (“Collagen extraction process”, International Food Research Journal, 2016, 23(3), pages 913-922) and US 11,008,544 (Bugeon et al).
CN 106480142 (Cheng et al) discloses a method for producing collagen peptides from bones, wherein the method comprises the following steps (see English abstract):
a ) providing bones of vertebrates or bovine bone (see abstract);
b ) mechanically crushing the bones using sieve with 40 mesh (400 µm), thus, to a particle size of less than 1000 µum as recited in pending claims; temperature during crushing appears to be a room temperature, and, thus, less than 70°C as recited in pending claims;
d ) heating the crushed bones in an aqueous suspension (upon addition of water) to a temperature of 110-120°C (or above 100° C as recited in pending claims) for about 2 hours;
e ) adding one or more proteases to the suspension in order to obtain an aqueous solution of collagen peptides; and
f ) separating off the aqueous solution of collagen peptides from the crushed bones.
The method as disclosed by CN 106480142 (Cheng et al) does not comprise treatment of bones with an acid or liming with a base within the meaning of the claims (*wherein” clause of claim 1).
Thus, as applied to claim 1: the cited CN 106480142 (Cheng et al) discloses the similar, if not the same method, for producing collagen peptide from bones except for 3 structural elements.
First, with respect to limitation drawn to “isoelectric point of less than 5.6”: collagen peptides are final product as encompassed by the claimed method for producing collagen peptides; and, thus, the claim-recited limitation about isoelectric point relates to characterization of a final product. In view of as-filed specification, the isoelectric point of “collagen peptides” is established at the very end of the process, after both heat treatment and enzymatic treatment and after separating collagen peptides from suspension (see par. 0047 at the published publication US 2022/0256886). In the claimed method “crushed bones” submitted to pH adjustment before heat treatment are still bones containing collagen but not hydrolyzed collagen or “collagen peptides”. Thus, “isoelectric point of less than 5.6” in the claimed method is a characteristics of the final product made by the whole method as intended. The cited reference by Leon-Lopez teaches that upon hydrolysis of native collagen to the collagen peptides the isoelectric point (pI) value is shifted from 7-8 of native collagen to lower values between 3.68 and 5.7 for hydrolyzed collagen or “collagen peptides” (see table 1 on page 4; see page 4, line 14). Thus, the recited limitation refers to final characteristic of the product such as “collagen peptides” (hydrolyzed collagen); and it falls within the art recognized range.
Secondly, with regard to limitation drawn to pH adjustment to 7.9-8.6: The cited above reference by Leon-Lopez teaches that collagen extraction from starting collagen-containing materials can be carried out by an acid or alkaline treatment (page 2, par. 7, first line). The reference by Schmidt (which is referred by Leon-Lopez) further teaches that before collagen can be extracted a pre-treatment is performed using an acid or alkaline process, which varies accordingly to the origin of the raw material (page 915, col. 2, par. 3, lines 1-4). The alkaline pre-treatment is applied to materials, that require a more aggressive penetration by subsequent treatment, such as bovine ossein or bovine bone matrix (page 917, paragraph bridging col. 1 and col. 2); while the acid pre-treatment is applied to fragile material such as skin (page 917, col. 1). In the method of the cited CN 106480142 (Cheng et al) starting raw material are bovine bones.
Therefore, it would have been obvious to one having ordinary skill in the art at the time the claimed invention was filed to add alkaline pre-treatment or to adjust crushed bone suspension pH to the alkaline pH before heat treatment in the method of CN 106480142 (Cheng et al) for producing collagen peptides by hydrolysis of bone collagen with a reasonable expectation of success in providing hydrolyzed collagen peptides from bones or from bovine bones because the prior art teaches and suggests alkaline pre-treatment of bones, as collagen-containing raw materials requiring an aggressive treatment by alkaline pH, in order to allow for more efficient hydrolysis by subsequent steps of collagen hydrolysis.
Thus, the claimed invention as a whole was clearly prima facie obvious, especially in the absence of evidence to the contrary.
The claimed subject matter fails to patentably distinguish over the state art as represented be the cited references. Therefore, the claims are properly rejected under 35 USC § 103.
Third, with regard to limitation drawn to heat treatment of crushed bones “at temperature of above 100°C for a period of 1 to 30 min”: The cited CN 106480142 (Cheng et al) discloses bone heat treatment at a temperature of 110-120°C (or above 100° C as recited in pending claims) for about 2-2.5 hours or longer than in the claimed method. However, one of skill in the art would obviously recognize that in order to avoid a total collagen destruction the time of exposure to extremely high temperature should be reduced. One of skill in the art could obviously optimize temperature and time to temperature exposure upon routine experimentation depending of materials, available equipment and final goals.
Therefore, it would have been obvious to one having ordinary skill in the art at the time the claimed invention was filed to modify or to decrease time period for heating step of crushed bones with a reasonable expectation of success for producing collagen peptides from bones because it is considered within the skills on ordinary practitioners to modify or for optime time period for collagen extraction depending on specific materials used and specific conditions of experimental design.
Thus, the claimed invention as a whole was clearly prima facie obvious, especially in the absence of evidence to the contrary.
The claimed subject matter fails to patentably distinguish over the state art as represented be the cited reference. Therefore, the claims are properly rejected under 35 USC § 103.
As applied to claim 2: in the method of CN 106480142 (Cheng et al) the bones are from mammas or they are bovine bone (see abstract).
As applied to claim 3: in the method of CN 106480142 (Cheng et al) describes the use of bones; and, thus, one would reasonably expect that the bones are cleaned from meat.
As applied to claim 7: in the method of CN 106480142 (Cheng et al) the mechanical crushing with mesh appears is same as claimed dry grinding.
As applied to claim 8: in the method of CN 106480142 (Cheng et al) the ratio of bones to water for the heating step is 1: (3.5-4), thus, about 25% bones in aqueous suspension which is about 0.25 kg/L and falls within the claim-recited range 0.05-0.5 kg/L.
As applied to claim 10: in the method of CN 106480142 (Cheng et al) after the heating step the temperature of the aqueous suspension is cooled for optimal enzymatic activity of proteases to 47-50°C (see abstract).
As applied to claim 11: in the method of CN 106480142 (Cheng et al) one protease is “flavourzyme” (see abstract) which is microbial enzyme preparation from Aspergillus containing endo-protease (as evidenced by US 11,008,544 (Bugeon et al), see col. 3, lines 25-26 and col. 6, lines 36-37).
As applied to claim 12: the cited CN 106480142 (Cheng et al) discloses the use of enzymes such 4000 units of enzymatic activity per gram of bones. Thus, it is considered within the skills on ordinary practitioners to estimate amounts of enzyme per dry weight of bones for optimal enzymatic reaction.
As applied to claim 13: in the method of the cited CN 106480142 (Cheng et al) the enzymatic reaction is carried for 4.5-5 hours (see abstract) or for about same 4 hours as encompassed by the claims. It is considered within the skills on ordinary practitioners to modify or for optime time period for enzymatic reaction depending on specific materials used including enzymatic activity of specific enzymes used.
As applied to claim 14: although the cited CN 106480142 (Cheng et al) does not appear explicitly describe repetition of heating, enzymatic treatment and separating steps, it would be obvious to one of skill in the art to repeat these steps to maximize and/or to improve hydrolysis of starting and/or intermediate collagen materials as intended for the desired final MW and amounts of final product with collagen peptides.
As applied to claims 15-16: the method of cited CN 106480142 (Cheng et al) comprises steps of separation of collagen peptides by filtration and further drying to provide for a powder (see abstract).
Thus, the claimed invention as a whole was clearly prima facie obvious, especially in the absence of evidence to the contrary.
The claimed subject matter fails to patentably distinguish over the state art as represented be the cited reference. Therefore, the claims are properly rejected under 35 USC § 103.
Claims 1-4, 7, 8, 10-16 are rejected under 35 U.S.C. 103 as being unpatentable over CN 106480142 (Cheng et al), Leon-Lopez et al (“Hydrolyzed Collogen - Sources and Applications”, Macromolecules. 2019, published 11/07/2019, 4031, pages 1-16), Schmidt et al (“Collagen extraction process”, International Food Research Journal, 2016, 23(3), pages 913-922) and US 11,008,544 (Bugeon et al) as applied to claims 1-3, 7, 8, 10-16 above, and further in view of US 3,098,014 (Denton et al).
The cited CN 106480142 (Cheng et al) is relied upon as explained above for the disclosure of a method for producing collagen peptides from bones, wherein the method comprises the steps of providing bones, crushing bones, heating, enzymatically treating, and separating collagen peptides (see English abstract).
As applied to claim 4: The cited CN 106480142 (Cheng et al) does not explicitly teach cleaning bones before crushing. But it is well known that enzymes are used for cleaning bones and for removing meat from bones. For example: see US 3/098,014 (Denton et al) at title and at col. 2, lines 22-57.
Therefore, it would have been obvious to one having ordinary skill in the art at the time the claimed invention was filed to practice or add step of cleaning bones from attached meat by using enzymes in the method of CN 106480142 (Cheng et al) with a reasonable expectation of success in providing collagen peptides from bones because it is well known to use enzymes for cleaning bones and for removing meat from bones as (US 3,098,014 (Denton et al)).
Thus, the claimed invention as a whole was clearly prima facie obvious, especially in the absence of evidence to the contrary.
The claimed subject matter fails to patentably distinguish over the state art as represented be the cited references. Therefore, the claims are properly rejected under 35 USC § 103.
Claims 1-8 and 10-16 are rejected under 35 U.S.C. 103 as being unpatentable over CN 106480142 (Cheng et al), Leon-Lopez et al (“Hydrolyzed Collogen - Sources and Applications”, Macromolecules. 2019, published 11/07/2019, 4031, pages 1-16), Schmidt et al (“Collagen extraction process”, International Food Research Journal, 2016, 23(3), pages 913-922), US 11,008,544 (Bugeon et al) and US 3, 098,014 (Denton et al) as applied to claims 1-3, 7, 8, 10-16 above, and further in view of Yanli Ma et al (Journal of Cleaner Production, 2019, 209, pages 916-926) and Viguet-Cariin et al (Osteoporos Int., 2006, 17, pages 319-336).
The cited CN 106480142 (Cheng et al) is relied upon as explained above for the disclosure of a method for producing collagen peptides from bones, wherein the method comprises the steps of providing bones, crushing bones, heating, enzymatically treating, and separating collagen peptides (see English abstract).
As applied to claims 5-6: The cited CN 106480142 (Cheng et al) does not explicitly describe fat and collagen contents in the bones before crushing and extracting collagen materials.
But it is known that defatted bones that are further used for extraction of collagen materials and that fat content in the defatted bones is less than 4% or about 1.6%. For example: see reference by Yanli Ma et al at page 917, col. 2, section “materials”.
It is also known that major collagen in bones is type I collagen and it comprises about 80% of the total proteins in bones. For example: see reference by Viguet-Cariin et al at page 320, col. 2, par. 3, lines 4-7.
Thus, the claimed invention as a whole was clearly prima facie obvious, especially in the absence of evidence to the contrary.
The claimed subject matter fails to patentably distinguish over the state art as represented be the cited references. Therefore, the claims are properly rejected under 35 USC § 103.
Response to Arguments
Applicant's arguments filed on 9/08/2025 have been fully considered but they are not persuasive.
With regard to the claim rejections under 35 USC § 103 Applicants’ main argument is that the cited CN 106480142 (Cheng et al) does not teach pH adjustment before heating step and does not recognize isoelectric point value of collagen peptides obtained. Applicants farther argue that the disclosure by Leon-Lopez is not correct with regard to values of isoelectric point (pI)of all collagen peptides since the specification example 1 demonstrates pI value of 6.3 of final collagen peptides when no pH adjustment (no pre-treatment) is done before heating step.
These arguments are not found persuasive.
The pI value of 6.3 as argued and disclosed in the specification particular example for the final collagen peptides is obtained when no pH adjustment (no pre-treatment) is done before heating step. This value of 6.3 is between characterizations of “native collagen” and “hydrolyzed peptides” accordingly to table 1 of the cited Leon-Lopez. Thus, it would be reasonably to conclude that there was no full hydrolysis of starting collagen material in the lack of pH adjustment in the specification example 1. The specification example 2, which describes acid treatment (not the claimed alkaline pH) is silent about isoelectric point value. There is no example with alkaline treatment or with alkaline pH in order to consider what might be correct or incorrect for the values of isoelectric point of final hydrolyzed collagen (collagen peptides) in the cited prior art. The cited reference by Leon-Lopez teaches that collagen extraction might be done by either acid or alkaline pre-treatment and that the final values are 3.68-5.7 (table 1) which overlap the claim-recited value of “less than 5.6”.
No claims are allowed.
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Vera Afremova
February 20, 2026
/VERA AFREMOVA/ Primary Examiner, Art Unit 1653