In 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 08/10/2026 has been entered.
Amendments Received
Amendments to the claims were received and entered on 08/10/2026.
Status of Claims
Claim 5 is cancelled; claim 7 is newly added.
Claims 1-4 and 6-7 are currently pending and under consideration.
Priority
The present application claims status as a 371 (National Stage) of PCT/IB2021/060415 filed on November 10, 2021 and claims priority to South African application ZA2020/07000, filed on November 11, 2020. Acknowledgment is made of applicant' s claim for foreign priority and papers submitted under 35 U.S.C. 119 (a)-(d). The present application is being examined with an effective filing date of November 11, 2020. In future actions, the effective filing date may change due to amendments or further review of priority documents.
Withdrawn Rejections
In view of Applicant’s amendments, rejections of claims 1-4 and 6 under 35 USC § 103 are hereby withdrawn.
Claim Objections
Claim 7 is objected to because of the following informalities:
A period is missing at the conclusion of the claim.
Appropriate correction is required.
Modified Rejections Necessitated by Amendment
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.
Claims 1-4 and 6 are rejected under 35 U.S.C. 103 as being unpatentable over PRNewswire (Geltor Unveils First Biodesigned Human Collagen for Skincare Market, 2019, https://www.prnewswire.com/news-releases/geltor-unveils-first-biodesigned-human-collagen-for-skincare-market-300819885.html, cited in a previous office action), Dioguardi, F. (US5198465A, cited in PTO-892), and Nassa et al. (Analysis of human collagen sequences. Bioinformation. 2012;8(1):26-33, cited in a previous office action), as evidenced by Geltor (HumaColl21, 2019, https://geltor.com/humacoll21-biomimetic-human-collagen, cited in a previous office action).
Claim 1 is directed to a vegan, plant-based alternative to animal-sourced collagen formulated for use in oral nutraceuticals, comprising free-form amino acids of vegan origin, wherein the composition is specified by recited amino-acid percentages and mimics targeted human collagen type I. Under the broadest reasonable interpretation, the claim is not limited to a native collagen molecule or an intact triple-helical collagen structure, but encompasses a mixture of free-form amino acids of vegan origin having the recited amino-acid percentages and designed to correspond to a known human collagen type I amino-acid profile. In particular, the limitation that the free-form amino acids “mimics the targeted human collagen type I” does not require that the recited amino-acid composition duplicate the complete amino-acid composition of a native human type I collagen heterotrimer, nor does the claim require that the recited percentages be derived from a weighted combination of the α1(I) and α2(I) chains. It is further noted that claim 1 recites that the composition is “formulated for use in oral nutraceuticals” and is “aiming at providing the same health and cosmetic benefits as obtained by animal collagen.” These limitations are interpreted as statements of intended use or intended result and do not, by themselves, require a structural distinction in the recited free-form amino-acid composition. Accordingly, the claimed composition is not distinguished from an otherwise structurally corresponding amino-acid composition merely by its intended oral nutraceutical use or intended health and cosmetic benefits.
Regarding claim 1, PRNewswire discloses HumaColl21®, “the first ever human collagen created for cosmetics formulations, sustainably produced with zero animal inputs,” specifically human Type XXI collagen. PRNewswire teaches that the sustainable fermentation process used to produce these consumer proteins enables production using only a fraction of the land, water, and time required to process animal collagen. PRNewswire further teaches that HumaColl21® represents the use of bioactive proteins such as collagen across new categories and expressly states that HumaColl21® can safely be used across “beauty, the food and beverage industry, and beyond.” Thus, PRNewswire teaches an animal-free, sustainably produced human collagen composition and expressly contemplates use of such collagen technology in both beauty and food/beverage applications. PRNewswire further teaches that, of the 28 types of collagen produced by the human body, Type XXI collagen has been identified as a critical precursor to human collagen Types I and III, which are identified as essential components in the maintenance of skin elasticity and youthfulness. Thus, although PRNewswire exemplifies HumaColl21®, a human Type XXI collagen, PRNewswire expressly directs the skilled artisan to human Type I collagen as a collagen associated with the desired skin-related benefits. PRNewswire/Geltor therefore teaches an animal-free, biomimetic human collagen composition produced by fermentation, expressly contemplates expansion of the collagen technology to food and beverage applications, and identifies human Type I collagen as important to the desired skin-related effects. However, PRNewswire/Geltor does not expressly disclose a composition comprising free-form amino acids having the specific amino-acid percentage profile recited in claim 1 as an orally administered composition.
Dioguardi teaches compositions comprising amino acids for enhancing collagen synthesis. More specifically, these compositions may comprise proline, glycine, and lysine, together with vitamin C and optionally additional amino acids including methionine, cysteine, cystine, and valine (col. 2, lines 12–20). Dioguardi expressly teaches that the compositions may be administered systemically, mainly by oral administration, and that compositions suitable for oral use contain the same amino acids and vitamin C as the topical compositions (col. 2, lines 27-31 and 59–62). Significantly, Dioguardi identifies prevention of dermal aging in subjects exposed to UV rays, cold, and sun as an indication for systemic administration (col. 2, lines 62–67). Dioguardi additionally demonstrates oral administration of a composition comprising proline, glycine, lysine, vitamin C, and methionine to human subjects (col. 3, lines 30–42).
Nassa et al. teaches that human collagens comprise 28 genetically distinct members and reports a comparative characterization of the alpha-1 chains of human collagens with known amino-acid compositions. Nassa et al. specifically identifies “Col 1” as human “Collagen alpha-1(I) chain” (p. 30, Supplementary Table 1) and discloses the amino-acid compositions of the alpha-1 chains of all 28 collagen types as relative percentages, including Collagen 1 (p. 31, Supplementary Table 2). For human collagen alpha-1(I), Nassa et al. discloses the following amino-acid composition (percentages): alanine 9.5%, arginine 4.8%, asparagine 1.2%, aspartic acid 4.5%, cysteine 1.2%, glutamine 3.3%, glutamic acid 5.1%, glycine 26.7%, histidine 0.6%, isoleucine 1.6%, leucine 3.3%, lysine 3.9%, methionine 0.9%, phenylalanine 1.8%, proline 19.0%, serine 4.1%, threonine 3.1%, tryptophan 0.4%, tyrosine 0.9%, and valine 3.2% (p. 31, Supplementary Table 2). Thus, Nassa et al. further shows that different human collagen types have distinct but well-characterized amino-acid profiles, demonstrating that collagen amino-acid profiles were known and selectable based on the desired collagen type. Notably, Nassa et al. expressly characterizes the alpha-1(I) chain as corresponding to “Col 1,” i.e., human Collagen 1, and uses the alpha-1 chain for its analysis of the collagen proteins. Comparison of the Nassa et al. human collagen alpha-1(I) profile with the recited composition of claim 1 demonstrates close correspondence. Claim 1 recites glycine 27.08% vs. 26.7% in Nassa et al., proline 18.35% vs. 19.0%, alanine 9.48% vs. 9.5%, arginine 4.98% vs. 4.8%, aspartic acid 4.08% vs. 4.5%, serine 4.01% vs. 4.1%, lysine 3.82% vs. 3.9%, leucine 3.66% vs. 3.3%, valine 3.47% vs. 3.2%, threonine 3.07% vs. 3.1%, phenylalanine 1.77% vs. 1.8%, methionine 0.84% vs. 0.9%, histidine 0.77% vs. 0.6%, tryptophan 0.40% vs. 0.4%, and tyrosine 0.98% vs. 0.9%, with similarly close correspondence for the remaining amino acids. Accordingly, the amino-acid composition of the human collagen alpha-1(I) chain disclosed by Nassa et al. provides a known amino-acid profile closely corresponding to the recited composition for mimicking targeted human collagen Type I.
Regarding claims 2 and 3, Dioguardi further teaches that the hydroxylation of proline and lysine by proline hydroxylase and lysine hydroxylase permits collagen synthesis to proceed in vivo, and that these enzymes require vitamin C for activation (col. 1, lines 17–24). Dioguardi further teaches that a lack of vitamin C results in cessation of collagen synthesis by interrupting reactions catalyzed by vitamin C (col. 1, lines 24–29). Accordingly, Dioguardi teaches vitamin C as an inducer that stimulates the body to use the administered amino-acid precursors in the in vivo synthesis of collagen. Additionally, Dioguardi expressly includes vitamin C in its amino-acid compositions for enhancing collagen synthesis (col. 2, lines 12–20), including compositions suitable for oral administration (col. 2, lines 59–62).
Regarding claim 4, as described above, Dioguardi teaches that the compositions may be systemically administered, mainly by oral administration, and further teaches deionized water as a preferred diluent for such systemically administered compositions (col. 2, lines 35–39). Dioguardi expressly teaches that compositions suitable for oral use contain the amino acids and vitamin C together with excipients and diluents (col. 2, lines 59–62). It would have been obvious to one of ordinary skill in the art to formulate the orally administered amino-acid composition in liquid form using the deionized-water diluent expressly taught by Dioguardi, particularly in view of PRNewswire/Geltor’s express contemplation of collagen compositions for use in the food and beverage industry, since doing so would have amounted to the predictable use of a known liquid diluent in an orally administered composition.
Regarding claim 6, PRNewswire/Geltor, Dioguardi, and Nassa et al. teach the limitations of the amino-acid composition for the reasons discussed above regarding claim 1. Dioguardi further teaches a method of enhancing collagen synthesis in humans by orally administering a composition comprising amino-acids and vitamin C. Dioguardi teaches that systemic administration is mainly by oral administration (col. 2, lines 27–31) and specifically demonstrates oral administration of a composition comprising proline, glycine, lysine, vitamin C, and methionine to human subjects (col. 3, lines 30–42). Dioguardi further teaches that hydroxylation of proline and lysine permits collagen synthesis to proceed in vivo and that the enzymes responsible for such hydroxylation require vitamin C for activation (col. 1, lines 17–24). Thus, Dioguardi teaches orally administering amino acids together with vitamin C for enhancing collagen synthesis in vivo. It would therefore have been obvious to orally administer the vegan amino-acid composition of PRNewswire/Geltor, as modified by Dioguardi and Nassa et al. as discussed above, together with vitamin C as taught by Dioguardi, in order to provide the amino-acids and coenzyme necessary to enhance collagen synthesis in vivo.
An invention would have been obvious to a person of ordinary skill in the art if some teaching in the prior art would have led that person to combine the prior art teachings to arrive at the claimed invention. Before the effective filing date of the claimed invention, the teachings of PRNewswire/Geltor, which disclose a vegan, animal-free biomimetic human collagen composition, expressly contemplate use of such collagen technology across beauty and the food and beverage industry, and identify human collagen Types I and III as essential components in the maintenance of skin elasticity and youthfulness, combined with the teachings of Dioguardi, which disclose enhancing collagen synthesis by providing individual amino-acids to increase the bioavailability of collagen precursors to fibroblasts, including by oral administration for dermal-aging applications, would have led a person of ordinary skill in the art to formulate the animal-free collagen-related composition of PRNewswire/Geltor as an orally administered composition comprising individual amino-acids as taught by Dioguardi. Such a modification would have provided a known alternative means for promoting collagen synthesis and obtaining the desired collagen-related skin benefits while providing the composition in a form suitable for the food and beverage applications expressly contemplated by PRNewswire/Geltor. In view of Dioguardi, which further teaches including vitamin C with the amino-acids based on its known role in the in vivo collagen-synthesis pathway, one of ordinary skill in the art would have been motivated to include vitamin C with the amino-acid precursors in order to facilitate their use in collagen synthesis, as expressly taught by Dioguardi. Furthermore, because Dioguardi teaches deionized water as a preferred diluent for systemically administered compositions, which are taught to be administered mainly orally, and PRNewswire/Geltor expressly contemplates food and beverage applications, it would have been obvious to formulate the orally administered composition in liquid form using the known aqueous diluent taught by Dioguardi. A person of ordinary skill in the art would further have been motivated to formulate the amino-acid composition according to the known human collagen alpha-1(I) amino-acid profile disclosed by Nassa et al. because PRNewswire/Geltor expressly identifies human Type I collagen as associated with the desired skin elasticity and youthfulness benefits, and Nassa et al. provides a known and quantifiable amino-acid profile associated with human Collagen 1. Accordingly, where the objective was to provide an animal-free amino-acid composition mimicking targeted human Type I collagen, it would have been obvious to select the known human collagen alpha-1(I) amino-acid profile taught by Nassa et al. as the profile upon which to formulate the amino-acid composition. There is a reasonable expectation of success because Dioguardi demonstrates that orally administered amino-acid compositions can be used to enhance collagen synthesis, including compositions containing vitamin C, while Nassa et al. provides the known amino-acid composition of human collagen alpha-1(I) from which the amino-acid profile could predictably be selected and formulated. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
Claim 7 is rejected under 35 U.S.C. 103 as being unpatentable over PRNewswire/Geltor, Dioguardi, and Nassa et al. as applied to claim 1 above, and further in view of Yoshihara et al. (US5164307A, cited in PTO-892).
Regarding claim 7, PRNewswire/Geltor in view of Dioguardi and Nassa et al. teaches the composition of claim 1 as discussed above, but does not expressly teach that the free-form amino acids are derived from a fermentation process using molasses, sugar cane, corn, or other plants.
Yoshihara et al. teaches processes for producing L-amino acids by fermentation, wherein L-amino-acid-producing bacteria are cultured in a medium containing cane molasses, sucrose, or glucose as a main carbon source, and the resulting L-amino acid is harvested. Yoshihara et al. specifically teaches that the L-amino acids produced by the fermentation process include glutamic acid, lysine, glutamine, arginine, isoleucine, valine, threonine, histidine, phenylalanine, tryptophan, serine, tyrosine, and leucine. Yoshihara et al. further exemplifies fermentation using cane molasses as a carbon source for production of an L-amino acid (Claim 1).
An invention would have been obvious to a person of ordinary skill in the art if some teaching in the prior art would have led that person to modify the prior art to arrive at the claimed invention. Before the effective filing date of the claimed invention, the teachings of Yoshihara et al., which disclose the production of L-amino acids by fermentation using cane molasses as a carbon source, would have led a person of ordinary skill in the art to produce the free-form amino acids of the animal-free amino-acid composition of PRNewswire/Geltor, as modified by Dioguardi and Nassa et al., by fermentation using cane molasses as taught by Yoshihara et al. Such a modification would have provided a known fermentation-based process for producing the individual amino acids used in the composition and would have been consistent with PRNewswire/Geltor’s express teaching of using sustainable fermentation to produce animal-free collagen products. One of ordinary skill in the art would have had a reasonable expectation of success because Yoshihara et al. successfully demonstrates the production of L-amino acids by fermentation using cane molasses as a carbon source. Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention.
Response to Arguments for Prior Art Rejections
Applicant’s arguments, in the response filed on 08/10/2026, have been fully considered but are not persuasive. Applicant contends that Nassa et al.‘s disclosure of the amino-acid composition of human collagen α1(I) does not represent Type I collagen because native Type I collagen comprises two α1(I) chains and one α2(I) chain. However, claim 1 does not recite an intact collagen polypeptide, a native Type I collagen heterotrimer, an α2(I) chain, a 2:1 ratio of α1(I) to α2(I), or require that the recited amino-acid percentages be calculated from a weighted combination of α1(I) and α2(I) chains. Rather, claim 1 recites free-form amino acids having the specified percentages that “mimics the targeted human collagen type I” and does not use language that requires that the composition identically duplicate the complete amino-acid composition of native Type I collagen. The claim does not use language such as “identical to,” “corresponding to the complete heterotrimer,” “derived from a complete Type I collagen molecule,” or “calculated from two α1(I) chains and one α2(I) chain.” The asserted requirement that the recited percentages include an α2(I) contribution or reflect a weighted 2:1 α1(I):α2(I) combination would improperly import an unrecited molecular-structure and stoichiometry limitation into a claim expressly directed to free-form amino acids. As discussed in the rejection above, PRNewswire/Geltor expressly identifies human Type I collagen as associated with the desired skin-related benefits, and Nassa et al. specifically identifies and provides the known amino-acid composition of the human collagen α1(I) chain.
Applicant further argues that the cited references provide no motivation to proceed from the topical Type XXI collagen of PRNewswire/Geltor to an orally administered, free-form amino-acid composition targeting Type I collagen and that the proposed modification is based on hindsight. These arguments are addressed by the rejection set forth above. In particular, PRNewswire/Geltor itself expressly contemplates use of its animal-free collagen technology in the food and beverage industry and expressly teaches that Type XXI collagen is a critical precursor to human collagen Types I and III, which are identified as essential components in the maintenance of skin elasticity and youthfulness. Thus, PRNewswire/Geltor itself provides an express connection between its Type XXI collagen and Type I collagen and identifies the desired skin-related benefits associated with Type I collagen. Dioguardi further independently teaches orally administering amino-acid compositions for enhancing collagen synthesis. Accordingly, the motivation for the modifications is provided by the prior art rather than Applicant’s disclosure.
Applicant’s argument that Type I and Type XXI collagen perform different biological roles is likewise not persuasive because the rejection does not rely upon Type I and Type XXI collagen proteins as being functionally interchangeable. As already discussed, PRNewswire/Geltor itself expressly links Type XXI collagen to Type I collagen by identifying Type XXI as a critical precursor to Types I and III and identifies Types I and III as associated with the desired skin-related benefits. Also discussed above, PRNewswire/Geltor provides the animal-free collagen technology and the express connection to Type I collagen; Dioguardi teaches the oral amino-acid approach for enhancing collagen synthesis; and Nassa et al. specifically identifies and provides the known amino-acid composition of human collagen α1(I).
Conclusion
No claim is in condition for allowance.
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/NAGHMEH NINA MOAZZAMI/Examiner, Art Unit 1652
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