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 .
Status of the Application
Receipt of the Response and Amendment after Non-Final Office Action filed 11 November 2025 is acknowledged.
Applicant has overcome the following by virtue of amendment of the specification and claims: (1) the objections to the specification and claims have been withdrawn; (2) the 112(b) rejections of claims 2-3 have been withdrawn.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 1-22
Withdrawn claims: 9, 12-14 and 17-18
Previously canceled claims: None
Newly canceled claims: None
Amended claims: 2, 3, and 7
New claims: 19-22
Claims currently under consideration: 1-8, 10-11, 15-16, and 19-22
Currently rejected claims: 1-8, 10-11, 15-16, and 19-22
Allowed claims: None
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1-8, 15, and 19-22 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon (i.e., product of nature) without significantly more.
The claims recite a dry collagen powder comprising at least 70%, up to and including 100%, native collagen protein, and less than 4%, including 0%, gelatin. The broadest reasonable interpretation of the claims, at best, is directed to a purified native collagen protein. The naturally occurring counterpart is the native collagen protein itself. The present case is analogous to the DNA example described in MPEP § 2106.04(c)(II)(A), which provides, “Although the selected counterpart should be in its natural state, examiners should take care not to confuse the counterpart with other material that may occur naturally with, or adjacent to, the counterpart. For example, assume that applicant claims a nucleic acid having a nucleotide sequence derived from naturally occurring gene B. Although gene B occurs in nature as part of a chromosome, the closest natural counterpart for the claimed nucleic acid is gene B, and not the whole chromosome. See, e.g., Ass’n for Molecular Pathology v. Myriad Genetics, Inc., 569 U.S. 576, 591-94, 106 USPQ2d 1972, 1979-81 (2013) (comparing isolated BRCA1 genes and BRCA1 cDNA molecules to naturally occurring BRCA1 gene)”.
Since the collagen powder as claimed may be 100% native collagen protein and 0% gelatin, the product lacks any markedly different characteristics from the naturally occurring counterpart. Markedly different characteristics can be pharmaceutical functions or activities, chemical properties, functional characteristics, or the like. MPEP § 2106.04(c)(II)(B). Isolation of a natural collagen protein without specifically claiming a feature that distinguishes the isolated product from its naturally occurring counterpart is insufficient for subject matter eligibility. This judicial exception is not integrated into a practical application because the claims do not require additional elements beyond the native collagen protein. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the specifically claimed components of the composition are all naturally occurring, and none need be present apart from the native collagen protein. The claimed features of satiating properties, powder particle granulometry, resistance to pepsin digestion, and swelling percentage are properties of the composition, and do not contribute to a change in form or functionality that would amount to significantly more than the judicial exception. Similarly, the animal of origin and/or its age do not contribute anything that would amount to significantly more than the judicial exception. Thus, the claims do not qualify as eligible subject matter and are rejected under 35 U.S.C. § 101.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 22 is rejected under 35 U.S.C. 112(d) as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 22 fails to include all limitations of claim 1. Claim 1 lists gelatin as an ingredient which indicates that gelatin is positively required even though the claim recites “less than 4% by weight”. Claim 22 recites that the dry collagen “lacks gelatin”.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements. It is suggested that Applicant amends claim 1 to recite “comprising collagen… native; and optionally less than 4wt% gelatin” or the like. Such amendment would remove any ambiguity regarding whether presence of gelatin is required. For purposes of examination, claim 1 is interpreted to include zero to less than 4% by weight gelatin.
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 1-7 and 19-22 are rejected under 35 U.S.C. 103 as being unpatentable over Advanced BioMatrix (Tendon, Lyophilized Fibrous Powder (bovine). (2020, September 19). Advanced BioMatrix. Retrieved February 12, 2026 from https://web.archive.org/web/ 20200919131855/https://advancedbiomatrix.com/tendon-powder.html) in view of Scalesciani (US 2016/0106674 A1).
Regarding claim 1, Advanced BioMatrix discloses a lyophilized (i.e., dry) fibrous powder of insoluble (i.e., native) Type I collagen from bovine flexor tendon (p. 1, ¶ 1). “This product has a purity of >96%” (p. 1, ¶ 2). As such, the product comprises more than 70% native collagen and less than 4% by weight of gelatin. Advanced BioMatrix teaches that the collagen product can be readily prepared into such forms as tissue scaffolds, foams, sponges, suspensions, coatings, putties, films, and sheets (p. 1, ¶ 4).
Advanced BioMatrix does not discuss that at least 95% of the dry collagen powder has a granulometry of between 10 µm and 5 mm.
However, Scalesciani teaches a collagen powder for pharmaceutical, medical, or cosmetic compositional use ([0001]). The preferred collagen is type I native collagen from horse and/or cow tendons, and the powder is a lyophilized powder ([0031]). The collagen powder comprises at least 99.5% of the particles having a maximum size of 80 microns ([0026]).
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to have modified the powder of Advanced BioMatrix with the teachings of Scalesciani to produce a native collagen powder in which at least 99.5% of the particles have a maximum size of 80 microns. One of ordinary skill in the art would have been motivated to do so in order to provide a powder suitable for use in pharmaceutical, medical, or cosmetic compositions. One of ordinary skill in the art would have had a reasonable expectation in arriving at the claimed invention because Advanced BioMatrix teaches a lyophilized native collagen powder of greater than 96% purity, and Scalesciani teaches a native collagen powder wherein at least 99.5% of the particles have a maximum size of 80 microns. The claimed range of at least 95% of the dry collagen powder has a granulometry of between 10 µm and 5 mm overlaps with the disclosed range of at least 99.5% of the particles having a maximum size of 80 microns. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
Additionally, Scalesciani discusses several pieces of prior art that illustrate that a common collagen powder size is well below 5 mm ([0014] – [0016]), thus demonstrating that the claimed particle size range overlaps with a well-known size range and therefore would have been obvious.
The claimed “satiating properties” of the dry collagen powder are an inherent feature to the composition. MPEP § 2112.01(I) states, “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).”
Since Advanced BioMatrix discloses a dry collagen powder of high purity as claimed, the products are substantially identical, and necessarily have the same properties, including “satiating properties”.
Therefore, claim 1 is rendered obvious.
Regarding claims 2 and 19-20, Advanced BioMatrix and Scalesciani teach the dry collagen powder according to claim 1.
Advanced BioMatrix also teaches that the dry collagen powder comprises native collagen in more than 80% by weight (re: claim 2), in more than 90% by weight (re: claim 19), and in more than 95% by weight (re: claim 20) – The insoluble collagen “has a purity of >96%” (p. 1, ¶ 2).
Claims 2 and 19-20 are therefore rendered obvious.
Regarding claims 3 and 21-22, Advanced BioMatrix and Scalesciani the dry collagen powder according to claim 1.
Advanced BioMatrix does not discuss that the dry collagen powder comprises a gelatin content of less than 2.5% by weight (re: claim 3), of less than 1% by weight (re: claim 21), or wherein the dry collagen powder lacks gelatin (re: claim 22).
However, Advanced BioMatrix teaches that the collagen product can be readily prepared into such forms as tissue scaffolds, foams, sponges, suspensions, coatings, putties, films, and sheets (p. 1, ¶ 4). Advanced BioMatrix further teaches that the product does not form hydrogels (Id.), indicating that the product comprises essentially no gelatin. Moreover, Advanced BioMatrix does not disclose the addition of gelatin and discloses a purity of greater than 96%, thus the collagen powder of Advanced BioMatrix is understood to have no gelatin present.
Regardless of whether or not there is gelatin in the composition of Advanced BioMatrix, it would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to have further purified the native collagen product of Advanced BioMatrix to its purest form, including 100% purity. At its purest form, the resulting native collagen protein would lack gelatin. One of ordinary skill in the art would have been motivated to do so in order to obtain 100% purified native collagen powder for use as a standard in scientific research. One of ordinary skill in the art would have had a reasonable expectation of success in doing so because purification is part of routine experimentation, subsequent rounds of purification would lead to increased purity, and low-temperature drying by lyophilization would preserve the native collagen.
Claims 3 and 21-22 are therefore rendered obvious.
Regarding claim 5, Advanced BioMatrix and Scalesciani the dry collagen powder according to claim 1, wherein the dry collagen powder has an undigested collagen fraction after a pepsin powder digestion test greater than 30%.
The claimed “undigested fraction after a pepsin powder digestion test” of the dry collagen powder is an inherent feature to the composition. MPEP § 2112.01(I) states, “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).”
Since Advanced BioMatrix discloses a dry collagen powder of high purity as claimed, the products are substantially identical, and necessarily have the same properties, including the claimed “undigested collagen fraction after a pepsin powder digestion test greater than 30%”.
Therefore, claim 5 is obvious for the same reasons as described regarding claim 1 above.
Regarding claim 6, Advanced BioMatrix and Scalesciani the dry collagen powder according to claim 1, wherein a swelling percentage in an acid swelling test of the dry collagen powder is greater than 1550%.
The claimed “swelling percentage” of the dry collagen powder is an inherent feature to the composition. MPEP § 2112.01(I) states, “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).”
Since Advanced BioMatrix discloses a dry collagen powder of high purity as claimed, the products are substantially identical, and necessarily have the same properties, including the claimed “swelling percentage in an acid swelling test of the dry collagen powder greater than 1550%”.
Therefore, claim 6 is obvious for the same reasons as described regarding claim 1 above.
Regarding claim 7, Advanced BioMatrix and Scalesciani the dry collagen powder according to claim 1.
Advanced BioMatrix also teaches that the collagen is of bovine origin – “Type I bovine collagen” (p. 1, ¶ 1).
Claim 7 is therefore rendered obvious.
Claims 1 and 4 are rejected under 35 U.S.C. 103 as being unpatentable over Advanced BioMatrix (Tendon, Lyophilized Fibrous Powder (bovine). (2020, September 19). Advanced BioMatrix. Retrieved February 12, 2026 from https://web.archive.org/web/ 20200919131855/https://advancedbiomatrix.com/tendon-powder.html) in view of Safojan et al. (RU 2476236 C1).
Regarding claims 1 and 4, Advanced BioMatrix discloses a lyophilized (i.e., dry) fibrous powder of insoluble (i.e., native) Type I collagen from bovine flexor tendon (p. 1, ¶ 1). “This product has a purity of >96%” (p. 1, ¶ 2). As such, the product comprises more than 70% native collagen and less than 4% by weight of gelatin. Advanced BioMatrix teaches that the collagen product can be readily prepared into such forms as tissue scaffolds, foams, sponges, suspensions, coatings, putties, films, and sheets (p. 1, ¶ 4).
Advanced BioMatrix does not discuss that at least 95% of the dry collagen powder has a granulometry of between 10 µm and 5 mm (re: claim 1) or a mean granulometry of between 250 µm and 1 mm (re: claim 4).
However, Safojan teaches a collagen powder with a particle size of not more than 500 microns used in preparing a collagen-hydroxyapatite composite (p. 3, lines 1-10) for repairing defects of bone tissue (i.e., a tissue scaffold) (p. 1, “Field of the invention”, ¶ 1). Thus, Safojan teaches that a range of not more than 500 microns is a known suitable size range for collagen powder particles.
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to have modified the powder of Advanced BioMatrix with the teachings of Safojan to produce a native collagen powder in which at least 99.5% of the particles have a maximum size of 500 microns. One of ordinary skill in the art would have been motivated to do so in order to provide a powder suitable for use in tissue scaffold compositions, such as the composite of Safojan. One of ordinary skill in the art would have had a reasonable expectation in arriving at the claimed invention because Advanced BioMatrix teaches a lyophilized native collagen powder of greater than 96% purity, and Safojan teaches that a range of not more than 500 microns is a known suitable size range for collagen powder particles. The claimed range of at least 95% of the dry collagen powder has a granulometry of between 10 µm and 5 mm overlaps with the disclosed range of a particle size of not more than 500 microns. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
The claimed “satiating properties” of the dry collagen powder are an inherent feature to the composition. MPEP § 2112.01(I) states, “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).”
Since Advanced BioMatrix discloses a dry collagen powder of high purity as claimed, the products are substantially identical, and necessarily have the same properties, including “satiating properties”.
Therefore, claims 1 and 4 are rendered obvious.
Claims 1-2, 7, 10-11, 16, and 19-20 are rejected under 35 U.S.C. 103 as being unpatentable over Visser (EP 1270672 A1, cited on the IDS filed on 27 March 2023) in view of Advanced BioMatrix (Tendon, Lyophilized Fibrous Powder (bovine). (2020, September 19). Advanced BioMatrix. Retrieved February 12, 2026 from https://web.archive.org/web/20200919131855/https://advancedbiomatrix.com/tendon-powder.html) and Scalesciani (US 2016/0106674 A1).
Regarding claims 1-2 and 19-20, Visser teaches a process for recovering native collagen from fleshed or unfleshed animal hide or skin ([0001]) and native collagen prepared by such a process ([0025]). Visser states that “native collagen” refers to collagen which has not been denatured, degraded, or gelatinized ([0001]). The entire process of Visser is temperature controlled such that no unacceptable degradation, denaturation, or gelatinization of the native collagen will occur. Visser maintains the temperature below 35 °C, preferably between 23-30 °C ([0015]). Residual flesh is hydrolyzed by proteases and alkali metal metabisulphite, but native collagen is not degraded and remains in suspension ([0018]). The native collagen is separated from the suspension ([0021]) and disinfected ([0022]). During disinfection, traces of hydrolysate and fat are discarded and the native collagen is further purified ([0022]). The native collagen may be dried ([0036]). The native collagen may be used as part of a paste to form sausage casings or edible casings around food ([0024]).
Visser does not specifically discuss that more than 70% (re: claim 1), 80% (re: claim 2), 90% (re: claim 19), or 95% (re: claim 20) by weight of the collagen is native, that the gelatin content is less than 4% by weight, or that the dry product is a powder wherein at least 95% of the dry collagen powder has a granulometry of between 10 µm and 5 mm (re: claim 1) or a mean granulometry between 250 µm and 1 mm (re: claim 4).
However, Visser appears to suggest that the collagen obtained by the method is 100% native, and not denatured, degraded, or gelatinized as indicated by the process steps taken to avoid such denaturation, degradation, and gelatinization as described above.
Notwithstanding, Advanced BioMatrix discloses a lyophilized (i.e., dry) fibrous powder of insoluble (i.e., native) Type I collagen from bovine flexor tendon (p. 1, ¶ 1). “This product has a purity of >96%” (p. 1, ¶ 2). As such, the product comprises more than 70% native collagen and less than 4% by weight of gelatin.
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to purify the native collagen of Visser to at least the levels disclosed by Advanced BioMatrix, such that the native collagen has a purity of >96% and a gelatin content of less than 4% by weight. One of ordinary skill in the art would have been motivated to do so to provide a highly pure native collagen as is the object of Visser. One of ordinary skill in the art would have had a reasonable expectation of success in doing so because Visser teaches precautionary steps in avoiding the degradation, denaturation, and gelatinization of the native collagen, and Advanced BioMatrix demonstrates that such purity is achievable.
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to modify the method of Visser with the teachings of Advanced BioMatrix to dry the collagen by lyophilization. One of ordinary skill in the art would have been motivated to consult Advanced BioMatrix to determine a suitable method of drying since Visser does not describe how the native collagen is dried. One of ordinary skill in the art would have had a reasonable expectation of success because Advanced BioMatrix demonstrates that a high-purity native collagen can be lyophilized.
Regarding the granulometry, Visser teaches that the native collagen may be used as part of a smooth paste to form sausage casings or edible casings around food, the paste formed by a number of successive comminution steps and combining the collagen with additives ([0024]). Visser does not discuss the granulometry of the comminuted collagen.
However, Scalesciani teaches a collagen powder in which at least 99.5% of the particles having a maximum size of 80 microns (Abstract). The preferred collagen is type I native collagen from horse and/or cow tendons, and the powder is a lyophilized powder ([0031]). Additionally, Scalesciani discusses several pieces of prior art that illustrate that a common collagen powder size is well below 5 mm ([0014] – [0016]).
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to have modified the native collagen of Visser with the teachings of Scalesciani to produce a native collagen powder in which at least 99.5% of the particles have a maximum size of 80 microns. Where Visser is silent regarding the powder particle size, one of ordinary skill in the art would have been motivated to consult Scalesciani to determine a common native collagen powder size. One of ordinary skill in the art would have had a reasonable expectation in arriving at the claimed invention because Scalesciani teaches a native collagen powder wherein at least 99.5% of the particles have a maximum size of 80 microns and discusses several pieces of prior art that illustrate that a common collagen powder size is well below 5 mm ([0014] – [0016]), thus demonstrating well-known collagen powder particle sizes. The claimed range of at least 95% of the dry collagen powder has a granulometry of between 10 µm and 5 mm overlaps with the disclosed range of at least 99.5% of the particles having a maximum size of 80 microns. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
The claimed “satiating properties” of the dry collagen powder are an inherent feature to the composition. MPEP § 2112.01(I) states, “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977).”
Since Visser as modified by Advanced BioMatrix discloses a dry collagen powder of high purity as claimed, the products are substantially identical, and necessarily have the same properties, including “satiating properties”.
Claims 1-2 and 19-20 are therefore rendered obvious.
Regarding claim 7, Visser, Advanced BioMatrix, and Scalesciani teach the dry collagen powder according to claim 1.
Visser also teaches that the collagen is at least of bovine or porcine origin – “Although in principle every suitable animal skin can be used, porcine skins and bovine skins are the most interesting, also because of their availability.” ([0012]).
Claim 7 is therefore rendered obvious.
Regarding claim 10, Visser, Advanced BioMatrix, and Scalesciani teach the dry collagen powder according to claim 1.
Visser also teaches a food or dietary supplement comprising the dry collagen powder – Visser teaches that the invention relates to water binding agents or texture improving agents for meat products comprising the native collagen ([0026]). That is, part of a food.
Claim 10 is therefore rendered obvious.
Regarding claim 11, Visser, Advanced BioMatrix, and Scalesciani teach the dry collagen powder according to claim 1.
Ten Kate further teaches a food product comprising the dry collagen powder – Visser teaches that the invention relates to meat products comprising the native collagen ([0026]).
Claim 11 is therefore rendered obvious.
Regarding claim 16, Visser, Advanced BioMatrix, and Scalesciani teach the food or dietary supplement according to claim 10.
Visser also teaches a food product comprising the food or dietary supplement – Visser teaches that the invention relates to meat products comprising the native collagen ([0026]), for example sausages with good water binding and texture improving properties ([0036]).
Claim 16 is therefore rendered obvious.
Claims 8 and 15 are rejected under 35 U.S.C. 103 as being unpatentable over Visser in view of Advanced BioMatrix and Scalesciani, as applied to claim 7 above, in view of Liu et al. (Liu, S., Li, Q., & Li, G. (2019). Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids. Journal of Leather Science and Engineering, 1(1), 11. https://doi.org/10.1186/s42825-023-00121-x).
Regarding claims 8, and 15, Visser, Advanced BioMatrix, and Scalesciani teach the dry collagen powder according to claim 7.
The cited prior art does not discuss that the collagen of bovine origin is from an animal between 0 and 3 years old (re: claim 8), or from an animal less than 2.5 years old (re: claim 15).
However, Liu teaches isolation of native collagen from calf skin (p. 2, col. 2, ¶ 3). A calf is understood to be a bovine animal less than 2.5 years old.
MPEP § 2144.07 states, “The selection of a known material based on its suitability for its intended use support[s] a prima facie obviousness determination”.
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to modify Visser with the teachings of Liu to select calf skin as the bovine skin from which to isolate the native collagen. One of ordinary skill in the art would have been motivated to do so and would have had a reasonable expectation of success in doing so because Visser teaches that the skin may any suitable skin, including bovine skin, and Liu teaches that calf skin is a suitable material from which to isolate native collagen.
Claims 8 and 15 are therefore rendered obvious.
Response to Arguments
Specification Objections:
Applicant has overcome the objection to the specification by amendment. Accordingly, the objection has been withdrawn.
Claim Objections:
Applicant has overcome the objections to the claims by amendment. Accordingly, the objections have been withdrawn.
Claim Rejections – 35 U.S.C. § 112:
Applicant has overcome the 35 U.S.C. § 112(b) rejections of claims 2-3 based on amendment to the claims. Accordingly, the 35 U.S.C. § 112(b) rejections have been withdrawn.
Claim Rejections – 35 U.S.C. § 101: Applicant' s arguments filed on 24 January 2025 have been fully considered, but they are not persuasive.
Applicant first argued that native collagen does not exist in nature in powdered form with the claimed particle size distribution and in a dry state (p. 7, ¶ 1).
Applicant’s argument has been considered, but it is not persuasive. Applicant is directed to a similar case presented in MPEP § 2106.04(c)(II)(C)(2), which discusses that in Myriad, the BRCA1 and BRCA2 genes isolated from the rest of the chromosome on which they exist in nature were not markedly different from their naturally occurring counterparts (the BRCA genes), and thus were product of nature exceptions. In the present case, the isolated native collagen is analogous to the isolated BRCA1 and BRCA2 genes. Thus, separating the collagen protein from its natural source does not render the isolated native collagen markedly different. The individual collagen molecules of the powder and of the natural source are not markedly different because both are in native form.
Applicant next argued that it is known in the art that isolating native collagen is a complex technical challenge, and prior attempts to obtain collagen powder with an increased content of collagen have been unsuccessful in achieving a percentage of native collagen as high as in the claimed dry collagen powder, presenting a significant technical challenge (p. 7, ¶ 3).
Applicant’s argument has been considered, but it is not persuasive at least because Advanced BioMatrix, cited in the rejections hereinabove, clearly demonstrates that it is possible to obtain a dry native collagen powder with >96% purity.
Applicant next argued that as a result of the technical steps, the dry collagen powder of the claimed invention comprises collagen fibers that are shorter and drier than collagen fibers that occur in nature, and although the claimed dry collagen powder has a high percentage of native collagen, such native collagen neither possesses the same characteristics nor properties as the collagen found in its natural state (p. 7, ¶ 4).
Applicant’s argument has been considered, but it is not persuasive. The individual collagen molecules are the natural counterpart. The individual collagen molecules of the claimed powder and of the natural source are not markedly different because both are in native form. The length of the fibers is not at issue. “Native collagen” refers to the collagen molecules maintaining their native structure.
Applicant next argued that the claimed dry collagen powder contains small amounts of gelatin, which is a degraded form of collagen not existing in nature (p. 7, ¶ 5).
Applicant’s argument has been considered, but it is not persuasive. The breadth of the claims is such that an embodiment exists wherein the dry collagen powder does not comprise any gelatin and only comprises native collagen.
Applicant further argued that the collagen powder of the invention possesses satiating properties, which are not associated with collagen found in its natural state (p. 7, ¶ 6).
Applicant’s argument has been considered, but it is not persuasive. Any satiating properties are characteristics inherent to the collagen. Moreover, Applicant’s definition of “satiating properties” as the ability of the powder of the invention to satisfy the need for food or drink for a certain period of time (specification, p. 5, lines 31-32), is incredibly broad. What constitutes satisfied? How is the need for food or drink determined? By fullness of the stomach? By caloric requirement for metabolic function? How long is “a certain period of time”? It is considered that eating enough of anything, including native collagen, regardless of its source, provides satiating properties.
For at least these reasons, Applicant’s arguments are not persuasive, and the rejection under 35 U.S.C. § 101 is maintained.
Claim Rejections – 35 U.S.C. § 102:
Applicant’s arguments filed 11 November 2025 (p. 8, ¶ 5 – p. 9, ¶ 3) with respect to the rejection of claims 1-3, 5-8, and 15 under 35 U.S.C. § 102(a)(1) or in the alternative 35 U.S.C. § 103 have been fully considered and are persuasive. Therefore, the rejection has been withdrawn.
Applicant’s arguments filed 11 November 2025 (p. 9, ¶ 4 – p. 10, ¶ 2) with respect to the rejection of claims 1-3, 5-7, 10-11, and 16 under 35 U.S.C. § 102(a)(1) have been fully considered and are persuasive. Therefore, the rejection has been withdrawn.
However, upon further consideration, new grounds of rejection of claims 1-8, 10-11, 15-16, and 19-22 are made as presented hereinabove.
Claim Rejections – 35 U.S.C. § 103:
Applicant’s arguments with respect to claim 4 filed on 11 November 2025 (p. 10, ¶ 3 – p. 12, ¶ 1) have been considered but are moot because the new ground of rejection does not rely on any reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument.
Conclusion
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/JAMES P. SHELLHAMMER/Examiner, Art Unit 1793
/Jennifer McNeil/Primary Examiner, Art Unit 1793