DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 14-18, 31, 39-43, and 48 are pending in the application and are being examined on the merits.
Applicant’s amendment to the claims, filed November 13, 2025 is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s remarks filed November 13, 2025 in response to the non-final rejection mailed June 13, 2025 are acknowledged and have been fully considered.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Restriction/Election
Claims 39-43 and 48 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim.
Claims 14-18 and 31 are being examined on the merits.
Claim Interpretation
As amended, claims 14-18 and 31 are drawn to a type A gelatin hydrolysate composition having an endotoxin content of 20 EU/g gelatin hydrolysate or less,
wherein the gelatin hydrolysate has a molecular weight of 30 kDa or less,
wherein the gelatin hydrolysate is free of surfactant and enzyme, and
wherein the type A gelatin is skin, tendon, ligaments or bone derived type A gelatin.
According to the instant specification at p. 1, line 16, “[g]elatin obtained by acid treatment is called Type A gelatin.” In view of the specification’s description, the recitation of “Type A gelatin” is interpreted as a product-by-process limitation, i.e., gelatin obtained by acid treatment. Applicant’s attention is directed to MPEP 2113 regarding product-by-process claims.
The recitation of “wherein the type A gelatin is skin, tendon, ligaments or bone derived type A gelatin” in claim 14 is interpreted as a product-by-process limitation. Given that the process step(s) for deriving the type A gelatin from skin, tendon, ligaments or bone are unlimited, other than a recited molecular weight range, the structural and functional properties of the peptides of the type A gelatin hydrolysate composition derived from skin, tendon, ligaments or bone are unlimited.
Regarding claims 14-18 and 31, other than a recited molecular weight, the structure(s) of the peptides of the type A gelatin hydrolysate composition is/are unlimited.
Claim Rejections - 35 USC § 102/103
Claims 14-18 and 31 are rejected under 35 U.S.C. 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Chang et al. (US 6,992,172 B1; cited on the IDS filed August 8, 2023; hereafter “Chang”). The instant rejection has been modified from its previous version to address the instant amendment to the claims.
Regarding claims 14-18 and 31, Chang teaches an acid hydrolysate of a recombinant gelatin with a molecular weight distribution of 0-10 kDa (column 63, Example 10) and teaches recombinant gelatins with molecular weights of approximately 14 kDa or 16 kDa (column 22, lines 50-53). Chang teaches the recombinant gelatin has less than 0.005 EU/mg (Table 3).
Given that the recitation of “type A gelatin” in claims 14-18 and 31 is a product-by-process limitation and the structure(s) and function(s) of the peptides of the recited type A gelatin hydrolysate composition are unlimited, Chang’s acid hydrolysate of a recombinant gelatin is considered to be encompassed by claims 14-18 and 31.
Although Chang does not teach or suggest the recombinant gelatin is “free of surfactant and enzyme,” Chang teaches the gelatins of the invention can be purified to homogeneity by methods known in the art (column 35, lines 49-51) and Chang teaches the recombinant gelatin that is used for acid hydrolysis is purified (column 61, lines 57-60). As such, the acid-hydrolyzed recombinant gelatin of Chang is considered to be “free of surfactant and enzyme.”
Alternatively, it would have been obvious to one of ordinary skill in the art before the effective filing date for Chang’s recombinant gelatins and acid hydrolysates of recombinant gelatins to be free of surfactant and enzyme. This is because Chang taught gelatin hydrolysates are used in the pharmaceutical and food industries (column 27, lines 11-13) and it would have been obvious to one of ordinary skill in the art to remove surfactant and enzyme for downstream uses in the pharmaceutical and food industries. One would have had a reasonable expectation of success for Chang’s recombinant gelatins and acid hydrolysates of recombinant gelatins to be free of surfactant and enzyme because methods for purifying gelatins were known in the art before the effective filing date (e.g., Chang at column 35, lines 49-51).
In this case, there is no evidence of record that the gelatin of Chang is structurally and/or functionally different in any way from the type A gelatin hydrolysate composition of instant claims 14-18 and 31. Since the Office does not have the facilities for examining and comparing applicants’ gelatin hydrolysate with the gelatin or gelatin hydrolysate of the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed product and the product of the prior art. See MPEP 2112.V and MPEP 2113.II.
Therefore, claims 14-18 and 31 are anticipated by or, in the alternative, are obvious in view of Chang.
RESPONSE TO REMARKS: Applicant argues Chang teaches the recombinant gelatin is a “homogeneous product with controlled characteristics,” while gelatins extracted from animals are heterogeneous products with a range of molecular weights that is different from the recombinant gelatin of Chang. Thus, according to applicant, the recited type A gelatin is different from Chang’s recombinant gelatin.
Applicant’s argument is not found persuasive. There is no limitation that requires the recited type A gelatin or hydrolysate thereof to be heterogeneous with a range of molecular weights. As stated above, the process steps for deriving the type A gelatin from skin, tendon, ligaments or bone are unlimited and other than a recited molecular weight, the structural and functional properties of the peptides of the type A gelatin hydrolysate composition derived from skin, tendon, ligaments or bone are unlimited.
While Chang teaches that it is possible to achieve a homogenous gelatin product, Chang also teaches that the recombinant gelatin has molecular weight distributions similar to natural gelatins. For example, Chang teaches “[u]sing suitable and controllable hydrolysis conditions, the present methods produced recombinant human gelatins with molecular weight distributions similar to those of commercially available gelatin” (column 22, lines 18-21); Chang teaches “[s]imilar to the hydrolysis of natural gelatins…the acid hydrolysates of recombinant human collagen showed several discrete molecular weight bands” (column 63, lines 30-33); and Chang teaches “recombinant gelatin with a molecular weight similar to that of some commercially available gelatins, of from about 10 to 70 kDa, could be produced” (column 32, lines 41-43).
Applicant argues type A gelatin from animal sources contains a high degree of hydroxyproline and also comprises hydroxylysine that are not present to the same degree in Chang’s recombinant gelatin. Applicant argues this difference in degrees of hydroxylation results in distinct structural and functional features.
Applicant’s argument is not found persuasive. There is no limitation that requires the presence of hydroxyproline and/or hydroxylysine, a degree of hydroxylation, and/or cross-linking of the recited type A gelatin or hydrolysate thereof. As stated above, the process steps for deriving the type A gelatin from skin, tendon, ligaments or bone are unlimited and other than a recited molecular weight, the structural and functional properties of the peptides of the type A gelatin hydrolysate composition derived from skin, tendon, ligaments or bone are unlimited.
Even so, Chang teaches the recombinant gelatin comprises hydroxyproline and hydroxylysine residues (e.g., column 24, lines 24-28 and column 26, lines 42-46); Chang teaches the recombinant gelatins can have any degree of hydroxylation by mixing specified percentages of recombinant gelatins with different degrees of hydroxylation (e.g., column 24, lines 29-42); teaches covalent cross-links (column 25, line 60 to column 26, line 14); Chang teaches the characteristics of the recombinant gelatins including percentage hydroxylation and degrees of cross-linking can be varied to produce recombinant gelatins with desired molecular weights (column 23, lines 33-35); and Chang teaches the recombinant gelatin is intended as a substitute for animal sourced gelatin (column 3, line 43 to column 4, line 2). In view of the teachings of Chang, one of ordinary skill in the art would have recognized that Chang’s recombinant gelatin can have the same degree of hydroxylation and crosslinking as type A gelatin from natural sources.
For these reasons, it is the examiner’s position that the claimed invention is anticipated by or is obvious over Chang.
Claims 14-18 and 31 are rejected under 35 U.S.C. 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Kanayama et al. (EP 1829946 A1; cited on the IDS filed July 22, 2024; hereafter “Kanayama”). The instant rejection has been modified from its previous version to address the instant amendment to the claims.
Regarding claims 14-18 and 31, Kanayama teaches acid-treated pig skin gelatins with an average molecular weight of 1 kDa to 2 kDa were prepared to 12% w/v and subjected to ultrafiltration using a membrane with a molecular weight cutoff of 10,000 (Example 4, paragraph [0074]). Kanayama teaches the filtered gelatin solution has less than 0.03 EU/mL and has various molecular weights (paragraphs [0054] and [0075]). Given that the concentration of the gelatin solution is 12% w/v, which is equivalent to 12 g per 100 mL, the filtered gelatin solution of Kanamaya has less than 0.25 EU/g.
Although Kanamaya does not teach or suggest the filtered gelatin solution is “free of surfactant and enzyme”, Kanamaya does not teach adding surfactant and/or enzyme to the unfiltered or filtered gelatin solution. As such, the filtered gelatin solution of Kanamaya is considered to be “free of surfactant and enzyme.”
Alternatively, it would have been obvious to one of ordinary skill in the art before the effective filing date for the filtered gelatin solution of Kanamaya to be free of surfactant and enzyme. This is because Kanamaya taught the gelatin can be suitably employed in medical devices and pharmaceuticals (paragraph [0055]) and it would have been obvious to one of ordinary skill in the art to remove surfactant and enzyme for downstream uses in medical devices and pharmaceuticals. One would have had a reasonable expectation of success for the filtered gelatin solution of Kanamaya to be free of surfactant and enzyme because methods for purifying gelatins were known in the art before the effective filing date.
Therefore, claims 14-18 and 31 are anticipated by or, in the alternative, are obvious in view of Kanayama.
RESPONSE TO REMARKS: Applicant argues that it is generally known that ultrafiltration results in strong dilution of a filtrate and because Kanayama is silent about the gelatin content after filtration, no conclusion can be made about the final endotoxin content of the total amount of gelatin.
Applicant’s argument is not found persuasive. There is no evidence of record that the ultrafiltration of Kanamaya results in dilution of the filtrate and arguments presented by applicant cannot take the place of evidence (MPEP 716.01(c).II).
Kanayama teaches that when the molecular weight cut-off of the ultrafiltration membrane is sufficiently higher than the average molecular weight of the gelatin in the gelatin solution, the average molecular weight of the gelatin in which the endotoxin quantity has been reduced will be roughly equivalent to the average molecular weight of the gelatin in the gelatin solution (paragraph [0040]). Since the average molecular weights of the 12% w/v acid-treated pig skin gelatins were between 1,000 to 2,000 and the molecular weight cut off of the ultrafiltration membrane is 10,000 (see Example 4 of Kanayama), one of ordinary skill in the art would have expected the acid-treated pig skin gelatins to pass through the ultrafiltration membrane and be present in the filtrate. One would have expected the same results using the low or medium molecular weight gelatins of Kanayama when applied to an ultrafiltration membrane with a molecular weight cutoff that is sufficiently higher than the average molecular weights of the low or medium molecular weight gelatins.
For these reasons, it is the examiner’s position that the claimed invention is anticipated by or is obvious over Kanayama.
Claims 14-18 and 31 are rejected under 35 U.S.C. 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Olijve et al. (NL 2013880 B1; cited on the IDS filed July 22, 2024; hereafter “Olijve”). The instant rejection has been modified from its previous version to address the instant amendment to the claims.
Regarding claims 14-18 and 31, Olijve teaches gelatin is obtained by aqueous extraction of skin, tendons, ligaments, bones etc. in acid conditions (p. 1, lines 6-9) and teaches type A gelatin having a LPS content of less than 1 EU/g (p. 11, lines 9-13). Olijve teaches the average molecular weight of the gelatin can have an upper limit of 4 kDa or 15 kDa (p. 5, lines 10-13). Olijve’s method for preparing the gelatin comprises treatment with a micelle-forming surfactant and removal of the surfactant using a solid adsorbent and is free of an enzymatic treatment step (p. 4, lines 25-33; p. 7, lines 5-24). Given that Olijve’s method includes a step of removing surfactant and is free of an enzymatic treatment step, Olijve’s type A gelatin is considered to be free of surfactant and enzyme.
Alternatively, it would have been obvious to one of ordinary skill in the art before the effective filing date for the gelatin of Olijve to be free of surfactant and enzyme. This is because Olijve taught the gelatin can be applied in food, pharmaceutical, and medical applications (p. 1, lines 18-20) and it would have been obvious to one of ordinary skill in the art to remove surfactant and enzyme for downstream uses in food, pharmaceutical, and medical applications. One would have had a reasonable expectation of success for the gelatin of Olijve to be free of surfactant and enzyme because methods for purifying gelatins were known in the art before the effective filing date.
Therefore, claims 14-18 and 31 are anticipated by or, in the alternative, are obvious in view of Olijve.
RESPONSE TO REMARKS: Applicant argues that while the gelatin of Olijve may be free of enzymes, one of ordinary skill in the art would recognize that the gelatin of Olijve is not free of surfactant.
Applicant’s argument is not found persuasive. There is no evidence of record that the gelatin of Olijve is not free of surfactant and arguments presented by applicant cannot take the place of evidence (MPEP 716.01(c).II).
Olijve provides extensive and detailed teachings regarding removal of surfactant (see entire document), and teaches repeating the adsorption step in order to remove any residual surfactant not removed in a first round of adsorption until a surface tension value of 65 - 67mN/m equal to pure gelatin is obtained (p. 17, lines 17-20). In view of the teachings of Olijve, one of ordinary skill in the art would have recognized that Olijve is teaching removal of surfactant to achieve pure gelatin.
For these reasons, it is the examiner’s position that the claimed invention is anticipated by or is obvious over Olijve.
Claim Rejections - Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 14-18 and 31 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 6, 8, and 9 of U.S. Patent No. 11,725,118 B2 (cited on Form PTO-892 mailed July 22, 2024). The instant rejection has been modified from its previous version to address the instant amendment to the claims. Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding instant claims 14-18, claim 1 of the patent recites a method for the preparation of a gelatin hydrolysate having a decreased endotoxin content, comprising the steps of:
a) incubating a solution of gelatin or gelatin hydrolysate at a temperature of 80-96° C at a pH of 3.5 or less for a time period of at least 15 minutes, and
b) recovering the gelatin hydrolysate having a decreased endotoxin content,
wherein in the method, no surfactant is added to the gelatin or gelatin hydrolysate;
claim 6 of the patent recites the method of claim 1, being free of an enzymatic treatment step;
claim 8 of the patent recites the method of claim 1, wherein the gelatin hydrolysate of step b) has a molecular weight of 30 kDa or less; and
claim 9 of the patent recites the method of claim 1, wherein the gelatin hydrolysate of step b) has an endotoxin level of 20 EU/g gelatin hydrolysate or less.
The claims of the patent do not recite “type A,” however, given that the gelatin hydrolysate is prepared by acid treatment of gelatin, the gelatin of the hydrolysate is considered to be “type A” in accordance with the instant specification’s description of “Type A gelatin” as being gelatin obtained by acid treatment.
The claims of the reference application do not recite the gelatin is derived from skin, tendon, ligaments, or bone. However, according to MPEP 804.II.B.1, “the portion of the specification of the reference that describes subject matter that falls within the scope of a reference claim may be relied upon to properly construe the scope of that claim” and the disclosed working example of the specification of the patent discloses that the gelatin used is pig skin gelatin type A (p. 7, line 1).
Regarding instant claim 31, the claims of the reference application do not recite the gelatin hydrolysate has a molecular weight between 10 and 30 kDa or between 10 kDa and 20 kDa. However, according to MPEP 804.II.B.1, “the portion of the specification of the reference that describes subject matter that falls within the scope of a reference claim may be relied upon to properly construe the scope of that claim” and the specification of the reference application describes that the gelatin hydrolysate preferably has a molecular weight of 30 kDa or less, 20 kDa or less, or 10 kDa or less (p. 6, lines 1-2).
Therefore, claims 14-18 and 31 of this application are unpatentable over claims 1, 6, 8, and 9 of the patent.
RESPONSE TO REMARKS: The applicant requests that the rejection be held in abeyance until withdrawal of all additional objections and rejections. The applicant’s request is acknowledged.
Claims 14-18 and 31 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of U.S. Patent No. 10,155,805 B2 (cited on Form PTO-892 mailed June 13, 2025) in view of Olijve. The instant rejection has been modified from its previous version to address the instant amendment to the claims. Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding instant claims 14-18 and 31, claim 1 of the patent recites a method of removing lipopolysaccharide from an aqueous medium comprising gelatin and lipopolysaccharides, said method comprising the steps of:
1) providing an aqueous medium comprising at least 2 w/w % gelatin and lipopolysaccharides,
2) adding to the aqueous medium 0.01-1.5 w/w % of a micelle-forming surfactant,
3) contacting the medium of step 2) with a solid adsorbent,
4) separating the solid adsorbent of step 3) from the medium,
5) recovering the aqueous medium comprising the gelatin,
wherein each of the steps 1)-5) are performed at a temperature of 68° C or less, said temperature being below the cloud point of the micelle-forming surfactant, at least steps 2) and 3) being performed at a temperature of at least 30° C.
The claims of the patent do not recite a “type A gelatin hydrolysate” of claims 14-18 and 31 of this application.
However, Olijve, which is the published foreign priority application of the patent, teaches type A gelatin having a LPS content of less than 1 EU/g (p. 11, lines 9-13). Olijve teaches the average molecular weight of the gelatin can have an upper limit of 4 kDa or 15 kDa (p. 5, lines 10-13). Olijve’s method for preparing the gelatin corresponds to the method recited in claim 1 of the patent and comprises treatment with a micelle-forming surfactant and removal of the surfactant using a solid adsorbent and is free of an enzymatic treatment step (p. 4, lines 25-33; p. 7, lines 5-24). Olijve teaches gelatin is obtained by aqueous extraction of skin, tendons, ligaments, bones etc. in acid conditions (p. 1, lines 6-9).
In view of Olijve, it would have been obvious to one of ordinary skill in the art before the effective filing date for the aqueous medium prepared according to claim 1 of the patent to comprise gelatin obtained by aqueous extraction of skin, tendons, ligaments, bones in acid conditions with an average molecular weight having an upper limit of 4 kDa or 15 kDa and a LPS content of less than 1 EU/g and to be free of surfactant and enzyme. This is because Olijve, which is the published foreign priority application of the patent, teaches a type A gelatin obtained by aqueous extraction of skin, tendons, ligaments, bones in acid conditions with an average molecular weight having an upper limit of 4 kDa or 15 kDa and a LPS content of less than 1 EU/g and being free of surfactant and enzyme, the gelatin being prepared by the same method recited in the claim of the patent.
Therefore, claims 14-18 and 31 of this application are unpatentable over claim 1 of the patent in view of Olijve.
RESPONSE TO REMARKS: Applicant argues the claims of the patent are patentably distinct from the claims of this application because Olijve teaches away from the presently claimed invention.
Applicant’s argument is not found persuasive. There is no evidence of record that the gelatin of prepared according to the claims of the patent as modified by Olijve is not free of surfactant (interpreted as being below the limit of detection) and arguments presented by applicant cannot take the place of evidence (MPEP 716.01(c).II).
Olijve provides extensive and detailed teachings regarding removal of surfactant (see entire document), and teaches repeating the adsorption step in order to remove any residual surfactant not removed in a first round of adsorption until a surface tension value of 65 - 67mN/m equal to pure gelatin is obtained (p. 17, lines 17-20). In view of the teachings of Olijve, one of ordinary skill in the art would have recognized that Olijve is teaching removal of surfactant to achieve pure gelatin and would have applied these teachings to the method of the claims of the patent.
For these reasons, it is the examiner’s position that the claimed invention is anticipated by or is obvious over Olijve.
Conclusion
Status of the claims:
Claims 14-18, 31, 39-43, and 48 are pending.
Claims 39-43 and 48 are withdrawn from consideration.
Claims 14-18 and 31 are rejected.
No claim is in condition for allowance.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
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/David Steadman/Primary Examiner, Art Unit 1656