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 .
Applicant’s response filed 6/17/2026 has been received and entered into the case. Claims 1-4, 6-23 are pending and have been considered on the merits. All arguments and amendments have been considered.
The previous rejections of record are withdrawn in light of applicants claim amendments and further consideration.
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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 16 and 17 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, 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 16 is drawn to a method of preparing collagen peptides comprising forming an amylase-containing composition of claim 1, which comprises denatured collagen and an enzymatic formulation, thus the composition of claim 1 and of claim 16 contains both denatured collagen and an enzymatic formulation in one composition, in which the denatured collagen would be in contact with the enzymatic formulation, thus the contacting step of claim 16 is unclear. Further, claim 17, further comprises a denaturing step to form the denatured collagen; however, the composition of claim 1, already includes a denatured collagen. Thus, the method steps fail to distinctly claim the invention and the metes and bounds of the method are not clear.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim(s) 1-4, 6-13, 16-20, 23 is/are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Salamone et al. (US20170151314) supported by Al Hajj et al. (Heliyon, vol. 10, 2024, p. 1-15).
Regarding claim 1, Salamone teaches an amylase containing composition comprising boiled pig skin, i.e., denatured collagen (0157-0162, Tables 1-5), and an enzymatic formulation comprising at least 50 wt% of amylase (0023, 0050-0052) , and wherein the formulation comprises less than 0.1 wt% of proteolytic enzymes given that the reference teaches the amount of proteolytic enzyme is 0, less than 0.01% or less than 0.001% (0029).
Regarding claim 2, the formulation comprises at least 50 wt% α-amylase (0052).
Regarding claim 3, the formulation comprises α-amylase, β-amylase, ɣ-amylase (0027, Table 1-5, for example).
Regarding claim 4, the enzymatic formulation comprises a weight ratio of non-proteolytic enzymes to proteolytic enzymes of at least 10:1, as the reference teaches that the amylase is present in amounts of at least 80 wt% up to 100 wt%, with the remaining weight % being other enzymes including proteolytic enzymes (0052).
Regarding claims 6 and 18, the denatured collagen comprises mammalian/porcine collagen, i.e. boiled pig skin (0157-0162, Tables 1-5), and murine collagen, i.e., boiled rat skin (0164, 0165, Table 7 and 8).
Regarding claims 7, 8, 23, the composition comprises a keratolytic agent, specifically urea, salicylic acid, and α-hydroxyacids including lactic acid, glycolic acid and citric acid (0049, table 5)
Regarding claim 9, the keratolytic agent in present in the composition in amounts of up to 15 wt% (0049).
Regarding claim 10, the composition comprises a surfactant in amounts of up to 10 wt% (0042, 0044, 0076, 0095-0098).
Regarding claim 11-13, the composition can have a pH ranging from 3-10, or 4.5-8 or from 5.5-7.5 (0053).
The composition may additionally comprise a penetration enhancer (0056).
Regarding claim 16, the reference teaches an amylase-containing composition and contacting boiled pig and rat skin, i.e. denatured collagen, with the amylase-containing composition (0157-0162, Tables 1-5, 0164, 0165, Table 7 and 8). While the reference does not specifically teach resulting collagen peptides, the peptides are taken to necessarily be a result of the contact step.
Regarding claim 17 and 19, the boiling, i.e. heat treatment, of the skin is a denaturing step which would form denatured collagen in the boiled skin (0157-0162, 0164, 0165). For support see Al Hajj, who teach that thermal treatment of above 40°C causes native collagen to denature (p. 2, 1st full parag.).
Regarding claim 20, the contacting step comprises contacting the boiled pig skin with the amylase formulation for about 1-48 hours (0054).
Thus, the reference anticipates the claimed subject matter.
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.
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.
Claim(s) 14 is/are rejected under 35 U.S.C. 103 as being unpatentable over Salamone et al. (US20170151314) as applied to claims 1-4, 6-13, 16-20, 23 above, and further in view of KR20200048610 to Kim et al.
The teachings of Salamone are found above. Salamone teaches the composition to comprise a penetration enhancer but are silent as to the amounts present in the composition as found in claim 14.
Regarding claim 14, KR20200048610 teaches methods of producing a LMW collagen hydrolysate (LMW of 600-800 Da, p. 4, 5th parag.) wherein a denatured collagen (claim 1, p. 3, last 6 parag.-p. 4, 1st 3 parag.) is treated with enzymes (p. 7, 2nd full parag.) to make a composition formulated as a cosmetic composition comprising a surfactant (p. 9, last parag.) and penetration enhancers including ethanol, propylene glycol, cetyl octanoate, for example (p. 9, 3rd and 4th parag.), wherein these components are added in amounts ranging from 0.01 to 5% by weight of the compositions (p. 10, 1st parag.).
Thus, before the effective filing date of the claimed invention amylase containing-compositions comprising a collagen hydrolysate were formulated for example, as a pharmaceutical or cosmetic formulations, and were known to comprise keratolytic agents, surfactants and penetration enhancers in amounts of up to 5% to deliver the hydrolysate as the active ingredient in the composition. Therefore, it would have been obvious to use the claimed components together in a composition in art suggested amounts because these ingredients and amounts were known to be used in formulating compositions comprising the collagen hydrolysate as the active ingredient to be delivered to the body.
Claim(s) 15, 21, 22 is/are rejected under 35 U.S.C. 103 as being unpatentable over Salamone et al. (US20170151314) as applied to claims 1-4, 6-13, 16-20, 23 above, and further in view of KR20230026757 and Hong et al. (Food Chem, 2021, vol. 352, p. 1-8).
The teachings of Salamone are found above.
The reference differs from the claimed invention in that it does not teach the limitations of claims 15, 21, 22.
KR20230026757 teaches an amylase-containing composition and method of preparing collagen peptides comprising adding amylase to denatured collagen, i.e. a collagen material treated with acid. The method produces collagen peptides have a low molecular weight (LMW) of 500 Da (abstract, p. 3, 2nd to last parag., p. 4, 2nd to last parag., p. 5, 5th and 6th parag.). The reference teaches a two-step enzymatic hydrolysis method (p. 6, 4th and 2nd to last parag.), wherein the denatured collagen is treated with pepsin followed by amylase and trypsin (p. 6, last 4 parag.-p. 7, 1st 4 parag.). The reference teaches amylase to be added in an amount of 1-3 wt% of the hydrolysate but that the concentration and amount of the enzyme used can be adjusted accordingly (p. 6, last parag.-1st line p. 7), additionally, ex. 1 teaches the enzyme formulation to comprise 50% amylase in the formulation. The formulation comprises β-amylase (p. 7, 2nd and 3rd parag.) from a marine source, fish by-products (abstract, p. 4, 6th parag., p. 5, 9th parag. ) and is in an aqueous composition with a pH of 6-8 (p. 6, 3rd to last parag., and Ex. 1).
Regarding claim 15, the weight ratio of denatured collagen to enzymatic formulation ranges from 100:1 to 10:1 as the reference teaches 1-3 wt% of amylase to hydrolysate (p. 6, last 2 lines).
Thus, it would be within the purview of a posita to optimize amounts of the enzyme in the formulation as the art teaches that enzyme amounts can be adjusted.
Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation.” In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%.); see also Peterson, 315 F.3d at 1330, 65 USPQ2d at 1382 (“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 of percentage ranges is the optimum combination of percentages.”). See MPEP 2144.05
Regarding claim 21, the amylase enzyme is taken to be deactivated by the sulfurous acid treatment to the secondary hydrolysate (the hydrolysate achieved after amylase treatment) (p. 7, 5th full parag.).
Regarding claim 22, while the reference teaches a two-step hydrolysis wherein the denatured collagen is treated with pepsin and then followed by trypsin and amylase, the reference teaches that the amylase breaks carbohydrate bonds to increase the efficiency of protein hydrolysis by pepsin and trypsin because the enzymes break bonds in different ways to further increase hydrolysis efficiency, allowing for low molecular weight collagen peptides (p. 6, 2nd to last parag, p. 7, 1st-3rd parag.). Therefore, while the method of KR757 teaches first treating with pepsin and then treating with amylase and trypsin, the method teaches combining multiple enzymes (and two enzymatic formulations) which cleave different bonds increasing efficiency and allowing one to successfully produce LMW collagen peptides.
Further, Hong teach a method of preparing low molecular weight collagen peptides comprising treating collagen containing skin (from hen, bovine, porcine and tilapia) with amylase for 6 hours. Regarding claim 21, the amylase is deactivated and collagen was extracted. The collagen extract was then hydrolyzed with papain and low molecular weight collagen peptides were obtained (section 2.4). Hong teaches that amylases cleave and hydrolyzed glycosidic bonds in collagen making the collagen more accessible to proteolytic attack as well as enabling the conversion of large molecular weight polypeptides into low MW peptides (p. 2, 1st and 2nd parag., section 3.3, ). Thus, treatment with amylase followed by an additional hydrolysis step is effective for obtaining low MW peptides from collagen (section 3.5).
Thus, before the effective filing date of the claimed invention, it would have been obvious to a posita to add a second contacting step using a second enzymatic formulation because the step would have yielded predictable results and resulted in an improved hydrolysis method to obtain low molecular weight collagen peptides.
Response to Arguments
Applicant’s arguments with respect to the claims 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
Any inquiry concerning this communication or earlier communications from the examiner should be directed to TIFFANY MAUREEN GOUGH whose telephone number is (571)272-0697. The examiner can normally be reached M-Thu 8-5.
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/TIFFANY M GOUGH/ Examiner, Art Unit 1651
/MELENIE L GORDON/ Supervisory Patent Examiner, Art Unit 1651
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