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 .
Applicant’s preliminary amendment to the claims, filed November 26, 2024, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Claims 1-13 are pending in the application and are being examined on the merits.
Priority
This application is filed under 35 U.S.C. 371 as a national stage of international application PCT/SE2023/050519, filed May 29, 2023, which claims domestic priority under 35 U.S.C. 119(e) to U.S. provisional application no. 63/346,489, filed May 27, 2022.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on November 26, 2024 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDS has been considered by the examiner.
Specification/Informalities
The disclosure is objected to because of the following informalities:
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code at p. 15, paragraph [0053], p. 32, paragraph [0104], and p. 85, paragraph [0260]. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
The disclosure is also objected to because the sequence listing incorporation statement at paragraph [0002] does not comply with the requirements for a sequence listing, which require the size of the XML file to be listed in bytes (not kilobytes). See MPEP 2422.03. and see MPEP 2422.03(a) for additional information pertaining to EFS-Web submission of sequence listings.
Appropriate correction is required.
Claim Objections
Claims 10 and 11 are objected to because of the following informalities:
Claim 10 is objected to in the recitation of “wherein the enzyme is selected from the group consisting of … and Thermomyces lanuginosus” and in the interest of improving claim form and consistency with claim 9, it is suggested that the noted phrase be amended to recite (with markings to show changes made) “wherein the enzyme is derived fromorThermomyces lanuginosus.”
Claim 10 is also objected to for failing to include a comma following each of the genus/species, e.g., there is no comma following “Aspergillus niger.”
Claim 11 is objected to on the recitation of “wherein the enzyme is Thermomyces lanuginosus” and in the interest of improving claim form and consistency with claim 9, it is suggested that the noted phrase be amended to recite (with markings to show changes made) “wherein the enzyme is derived from Thermomyces lanuginosus.”
Claim Rejections - 35 USC § 112(b)
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.
Claims 1-13 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Claims 1 (claims 2-13 dependent therefrom) and 3-7 are indefinite in the recitation of “about.” The term “about” is a term of approximation and the examiner has reviewed the specification and can find no examples or teachings that can be used for ascertaining the approximation intended by the term “about.” Moreover, there is nothing in the specification or prior art of record to indicate that one of skill in the art could have ascertain the scope of the approximation. It is suggested that applicant clarify the meaning of the term “about” in the context of the claims. See MPEP 2173.05(b).III.A regarding the term “about.”
Claim 12 is indefinite in the recitation of “such as high oleic or low linolenic, low saturated oils (high oleic canola oil, low linolenic soybean oil or high stearic sunflower oils).” The phrase "such as" and the examples presented in the parenthetical phrase render the claim indefinite because it is unclear whether the examples are part of the claimed invention. Description of examples is properly set forth in the specification rather than the claims. See MPEP § 2173.05(d) regarding exemplary claim language.
Claim 12 is also indefinite in the recitation of “high” and “low” (e.g., “high oleic”) because it is unclear from the claims, the specification, and the art of record as to what is encompassed by “high” and “low” in the context of the claim.
Claim 13 is indefinite in the recitation of “The process of claim 1, wherein the enzymatic treatment.” Claim 1 recites a first enzymatic treatment and a second enzymatic treatment and it is unclear from claim 13 as to whether “the enzymatic treatment” is in reference to the first enzymatic treatment, the second enzymatic treatment, or both the first and second enzymatic treatments in claim 1.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1-10, 12, and 13 are rejected under 35 U.S.C. 103 as being unpatentable over Urata et al. (US Patent No. 4,735,900; cited on the IDS filed November 26, 2024; hereafter “Urata”).
Claims 1-10, 12, and 13 are drawn to a process for batch enzymatic treatment of multiple lipid-containing compositions, the process comprising:
providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;
separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition.
Urata is related to an improved process for interesterification between an oil or fat (column 5, lines 11-15).
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9 and 10, Urata teaches exemplary lipases included one produced by Rhizopus, Aspergillus, Candida and Mucor microorganisms (column 6, lines 16-19) including one produced by Rhizopus delemar (column 6, lines 23-24).
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, the process of claims 1-10, 12, and 13 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claim 11 is rejected under 35 U.S.C. 103 as being unpatentable over Urata in view of Mazeaud et al. (WO 2009/010561 A1; cited on the IDS filed November 26, 2024; hereafter “Mazeaud”).
Claim 11 is drawn to the process of claim 10, wherein the enzyme is Thermomyces lanuginosus, interpreted as meaning the enzyme is derived from Thermomyces lanuginosus.
The relevant teachings of Urata as applied to claims 1-10, 12, and 13 are set forth above.
Urata does not teach or suggest the lipase is derived from Thermomyces lanuginosus.
Mazeaud is related to an immobilized enzyme product comprising a preformed single carrier particle and a lipolytic enzyme (p. 1, lines 3-4).
Regarding claim 11, Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the combined teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to use lipase from Thermomyces lanuginosus as the lipase in the interesterification reaction of Urata. One would have been motivated and expected success to do so because Urata teaches an interesterification reaction using an immobilized lipase and Mazeaud teaches suitable lipases including lipase from Thermomyces lanuginosus for an interesterification reaction using an immobilized lipase.
Therefore, the process of claim 11 would have been obvious to one of ordinary skill in the art before the effective filing date.
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.
U.S. Patent No. 8,227,215 B2
Claims 1-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 2 of U.S. Patent No. 8,227,215 B2 (cited on the attached Form PTO-892) in view of Urata and Mazeaud.
Claim 1 of the patent recites a method for biocatalytic synthesis of a structured lipid comprising the following steps:
(a) providing a polypeptide having a palmitase activity, said polypeptide being selected from the group consisting of isolated, synthetic and recombinant polypeptides having a palmitase activity and said polypeptide either
i. being encoded by
a nucleic acid comprising a nucleic acid sequence having at least 85% sequence identity to full length SEQ ID NO:1, and wherein the nucleic acid encodes at least one polypeptide having palmitase activity and the polypeptide having at least one amino acid residue change recited below in Table A, or
ii. having at least 85% sequence identity to full length SEQ ID NO:2, and having at least one amino acid residue change recited in Table A, or
iii. having at least 85% sequence identity to full length of SEQ ID NO:2 and comprising at least one amino acid residue modification D61A; D61E; R72E; R72K; E116A; E116Q; E116R; E116T; E116V; S133A; I151G; I151A; V163R; or D164R
(b) providing a composition comprising a triacylglyceride;
(c) contacting the polypeptide of step (a) with the composition of step (b) under conditions wherein the polypeptide hydrolyzes a palmitic acid residue at the Sn2 position of the triacylglyceride, thereby producing a 1,3-diacylglyceride;
(d) providing an R1 ester, wherein the R1 ester comprises a fatty acid of lower saturation than said hydrolyzed palmitic acid residue;
(e) providing an R1-specific hydrolase, and
(f) contacting the 1,3-diacylglyceride of step (c) with the R1 ester of step (d) and the R1-specific hydrolase of step (e) under conditions wherein the R1-specific hydrolase catalyzes esterification of the Sn2 position, thereby producing the structured lipid; and
claim 2 of the patent recites the method of claim 1, wherein the R1-specific hydrolase is an Sn2-specific lipase.
The claims of the patent do not recite the process of claims 1-13 of this application.
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata is related to an improved process for interesterification between an oil or fat (column 5, lines 11-15).
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Mazeaud is related to an immobilized enzyme product comprising a preformed single carrier particle and a lipolytic enzyme (p. 1, lines 3-4).
Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the reaction of steps (c) to (f) of the claim 1 of the patent according to the interesterification reactions of Urata and Mazeaud. One would have been motivated and expected success to do so because steps (c) to (f) of claim 1 of the patent encompass an interesterification reaction using a lipase and Urata and Mazeaud each teaches an improved interesterification reaction using an immobilized lipase.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9 and 10, Urata teaches exemplary lipases included one produced by Rhizopus, Aspergillus, Candida and Mucor microorganisms (column 6, lines 16-19) including one produced by Rhizopus delemar (column 6, lines 23-24).
Regarding claim 11, Mazeaud teaches a suitable lipase for interesterification includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, claims 1-13 of this application are unpatentable over claims 1 and 2 of the patent in view of Urata and Mazeaud.
U.S. Patent No. 8,313,918 B2
Claims 1-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of U.S. Patent No. 8,313,918 B2 (cited on the attached Form PTO-892) in view of Urata and Mazeaud.
Claim 1 of the patent recites a method of catalyzing an interesterification reaction to produce new triacylglycerides comprising the following steps:
(a) providing a composition comprising a polypeptide having a 1,3-specific palmitase activity, said polypeptide being selected from the group consisting of isolated, synthetic or recombinant polypeptides having a 1,3-specific palmitase activity and said polypeptide either
i. being encoded by
a nucleic acid comprising a nucleic acid sequence having at least 85% sequence identity to full length SEQ ID NO:1, and wherein the nucleic acid encodes at least one polypeptide having 1,3-specific palmitase activity and the polypeptide having at least one amino acid residue change recited below in Table A, or
ii. having at least 85% sequence identity to full length SEQ ID NO:2, and having at least one amino acid residue change recited in Table A,
or
iii. having at least 85% sequence identity to full length of SEQ ID NO:2 and comprising at least one amino acid residue modification D61A; D61E; R72E; R72K; E116A; E116Q; E116R; E116T; E116V; S133A; I151G; I151A; V163R; or D164R
(b) providing a mixture of triacylglycerides and free fatty acids;
(c) treating the mixture of step (b) with the polypeptide under conditions wherein the polypeptide can catalyze exchange of free fatty acids with the acyl groups of triacylglycerides, thereby producing new triacylglycerides enriched in said fatty acids.
The claims of the patent do not recite the process of claims 1-13 of this application.
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata is related to an improved process for interesterification between an oil or fat (column 5, lines 11-15).
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Mazeaud is related to an immobilized enzyme product comprising a preformed single carrier particle and a lipolytic enzyme (p. 1, lines 3-4).
Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the interesterification reaction of the claim of the patent according to the teachings of Urata and Mazeaud as set forth above. One would have been motivated and expected success to do so because claim 1 of the patent recites an interesterification reaction, and Urata and Mazeaud each teaches an improved interesterification reaction using an immobilized lipase.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9 and 10, Urata teaches exemplary lipases included one produced by Rhizopus, Aspergillus, Candida and Mucor microorganisms (column 6, lines 16-19) including one produced by Rhizopus delemar (column 6, lines 23-24).
Regarding claim 11, Mazeaud teaches a suitable lipase for interesterification includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, claims 1-13 of this application are unpatentable over claim 1 of the patent in view of Urata and Mazeaud.
U.S. Patent No. 8,349,578 B2
Claims 1-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 of U.S. Patent No. 8,349,578 B2 (cited on the attached Form PTO-892) in view of Urata and Mazeaud.
Claim 1 of the patent recites a method for biocatalytic synthesis of a structured lipid comprising the following steps:
(a) providing a polypeptide having a palmitase activity, said polypeptide being selected from the group consisting of isolated, synthetic and recombinant polypeptides having a palmitase activity and said polypeptide either
i. being encoded by
a nucleic acid comprising a nucleic acid sequence having at least 85% sequence identity to full length SEQ ID NO:1, and wherein the nucleic acid encodes at least one polypeptide having palmitase activity and the polypeptide having at least one amino acid residue change recited below in Table A, or
ii. having at least 85% sequence identity to full length SEQ ID NO:2, and having at least one amino acid residue change recited in Table A,
or
iii. having at least 85% sequence identity to full length of SEQ ID NO:2 and comprising at least one amino acid residue modification D61A; D61E; R72E; R72K; E116A; E116Q; E116R; E116T; E116V; S133A; I151G; I151A; V163R; or D164R
(b) providing a composition comprising a triacylglyceride;
(c) contacting the polypeptide of step (a) with the composition of step (b) under conditions wherein the polypeptide hydrolyzes a palmitic acid residue at the Sn1 or Sn3 position of the triacylglyceride, thereby producing a 1,2-diacylglyceride or 2,3-diacylglyceride; and
(d) promoting acyl migration in the 1,2-diacylglyceride or 2,3-diacylglyceride of the step (c) under kinetically controlled conditions, thereby producing a 1,3-diacylglyceride;
claim 2 of the patent recites the method of claim 1 comprising the further step of providing an R1 ester and an R1-specific lipase, and contacting the 1,3-diacylglyceride of step (d) with the R1 ester and the R1-specific lipase under conditions wherein the R1-specific lipase catalyzes esterification of the Sn2 position, thereby producing a structured lipid, wherein the R1 ester comprises a fatty acid of lower saturation than the hydrolyzed palmitic acid residue; and
claim 3 of the patent recites the method of claim 1, wherein said R1-specific lipase is an Sn1 or an Sn3-specific lipase.
The claims of the patent do not recite the process of claims 1-13 of this application.
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata is related to an improved process for interesterification between an oil or fat (column 5, lines 11-15).
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Mazeaud is related to an immobilized enzyme product comprising a preformed single carrier particle and a lipolytic enzyme (p. 1, lines 3-4).
Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the reaction of claims 2-3 of the patent according to the interesterification reactions of Urata and Mazeaud. One would have been motivated and expected success to do so because claims 2-3 of the patent encompass an interesterification reaction using a lipase and Urata and Mazeaud each teaches an improved interesterification reaction using an immobilized lipase.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9 and 10, Urata teaches exemplary lipases included one produced by Rhizopus, Aspergillus, Candida and Mucor microorganisms (column 6, lines 16-19) including one produced by Rhizopus delemar (column 6, lines 23-24).
Regarding claim 11, Mazeaud teaches a suitable lipase for interesterification includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, claims 1-13 of this application are unpatentable over claims 1-3 of the patent in view of Urata and Mazeaud.
U.S. Patent No. 8,420,342 B2
Claims 1-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of U.S. Patent No. 8,420,342 B2 (cited on the attached Form PTO-892) in view of Urata and Mazeaud.
Claim 1 of the patent recites an interesterification method for preparing a food, feed or an oil comprising the following steps:
(a) providing an interesterification reaction mixture comprising a stearic acid source material selected from the group consisting of stearic acid, stearic acid monoesters of low molecular weight monohydric alcohols and mixtures thereof,
(b) providing a food, feed or an oil containing a triacylglyceride;
(c) providing a polypeptide having a palmitase activity, said polypeptide being selected from the group consisting of isolated, synthetic and recombinant polypeptides having a palmitase activity and said polypeptide either
i. being encoded by
a nucleic acid comprising a nucleic acid sequence having at least 85% sequence identity to full length SEQ ID NO:1, and wherein the nucleic acid encodes at least one polypeptide having palmitase activity and the polypeptide having at least one amino acid residue change recited below in Table A, or
ii. having at least 85% sequence identity to full length SEQ ID NO:2, and having at least one amino acid residue change recited in Table A,
or
iii. having at least 85% sequence identity to full length of SEQ ID NO:2 and comprising at least one amino acid residue modification D61A; D61E; R72E; R72K; E116A; E116Q; E116R; E116T; E116V; S133A; I151G; I151A; V163R; or D164R
(d) interesterifying the stearic acid source material and the triacylglyceride of the food, feed, or oil, and
(e) separating free fatty acid components from interesterified glyceride components of the interesterification mixture to provide an interesterified oil product and a fatty acid mixture comprising fatty acids, fatty acid monoesters, or mixtures thereof released from the food, feed or oil.
Claim 1 of the patent does not recite the process of claims 1-13 of this application.
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata is related to an improved process for interesterification between an oil or fat (column 5, lines 11-15).
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Mazeaud is related to an immobilized enzyme product comprising a preformed single carrier particle and a lipolytic enzyme (p. 1, lines 3-4).
Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the interesterification reaction of the claim of the patent according to the teachings of Urata and Mazeaud as set forth above. One would have been motivated and expected success to do so because claim 1 of the patent recites an interesterification reaction, and Urata and Mazeaud each teaches an improved interesterification reaction using an immobilized lipase.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9 and 10, Urata teaches exemplary lipases included one produced by Rhizopus, Aspergillus, Candida and Mucor microorganisms (column 6, lines 16-19) including one produced by Rhizopus delemar (column 6, lines 23-24).
Regarding claim 11, Mazeaud teaches a suitable lipase for interesterification includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, claims 1-13 of this application are unpatentable over claim 1 of the patent in view of Urata and Mazeaud.
U.S. Patent No. 8,465,952 B2
Claims 1-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 2 of U.S. Patent No. 8,465,952 B2 (cited on the attached Form PTO-892) in view of Urata and Mazeaud.
Claim 1 of the patent recites a method for biocatalytic synthesis of a structured lipid comprising the following steps:
(a) providing a polypeptide having a palmitase activity, said polypeptide being selected from the group consisting of isolated, synthetic and recombinant polypeptides having a palmitase activity and said polypeptide either
i. being encoded by a nucleic acid comprising a nucleic acid sequence having at least 85% sequence identity to SEQ ID NO:1 and having at least one base residue change recited in Table A, Table B, or Table C below, wherein the nucleic acid encodes at least one polypeptide having a palmitase activity,
or
ii. having at least 85% sequence identity to SEQ ID NO:2, and having at least one amino acid residue change recited in Table A, or Table C above, or
iii. comprising an amino acid sequence of SEQ ID NO:2 but also comprising at least one of amino acid residue modification D61A; D61E; R72E; R72K; E116A; E116Q; E116R; E116T; E116V; S133A; I151G; I151A; V163R; D164R, or a combination thereof, or
iv. comprising an amino acid sequence of SEQ ID NO:2 but also comprising at least one of amino acid residue modification 120L; V62S; G77P; V83C; D88H; Y113G; E116T; E116G; H140K; K146S; I167S; L180E; E194M; A211Q; S212Y; G215C; G215V; G215W; A218H; A218S; V223A; A225M; A225Q, or a combination thereof;
(b) providing a composition comprising a triacylglyceride (TAG);
(c) contacting the polypeptide of step (a) with the composition of step (b) under conditions wherein the polypeptide hydrolyzes a palmitic acid residue at the Sn1 or Sn3 position of the triacylglyceride (TAG), thereby producing a 1,2 diacyglycerol (1,2-DAG) or 2,3-diacylglyceride (2,3-DAG);
(d) promoting acyl migration in the 1,2-DAG or 2,3-DAG of step (c) under kinetically controlled conditions, thereby producing a 1,3-DAG,
(e) providing an R1 ester;
(f) providing an R1-specific hydrolase, and
(g) contacting the 1,3-DAG of step (d) with the R1 ester of step (d) and the R1-specific hydrolase of step (e) under conditions wherein the R1-specific hydrolase catalyzes esterification of the Sn2 position, thereby producing the structured lipid; and
claim 2 of the patent recites the method of claim 1, wherein the R1-specific hydrolase is an Sn2-specific lipase.
The claims of the patent do not recite the process of claims 1-13 of this application.
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata is related to an improved process for interesterification between an oil or fat (column 5, lines 11-15).
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Mazeaud is related to an immobilized enzyme product comprising a preformed single carrier particle and a lipolytic enzyme (p. 1, lines 3-4).
Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the reaction of steps (e) to (g) of the claim 1 of the patent according to the interesterification reactions of Urata and Mazeaud. One would have been motivated and expected success to do so because steps (e) to (g) of claim 1 of the patent encompass an interesterification reaction using a lipase and Urata and Mazeaud each teaches an improved interesterification reaction using an immobilized lipase.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9 and 10, Urata teaches exemplary lipases included one produced by Rhizopus, Aspergillus, Candida and Mucor microorganisms (column 6, lines 16-19) including one produced by Rhizopus delemar (column 6, lines 23-24).
Regarding claim 11, Mazeaud teaches a suitable lipase for interesterification includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, claims 1-13 of this application are unpatentable over claims 1 and 2 of the patent in view of Urata and Mazeaud.
U.S. Patent No. 12,606,812 B2
Claims 1-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 3 of U.S. Patent No. 12,606,812 B2 (cited on the attached Form PTO-892) in view of Urata and Mazeaud.
Claim 1 of the patent recites a biocatalyst for organic synthesis, comprising:
a controlled porosity silica (CPS) as support material;
wherein the support material comprises an amino-functionalized surface comprising the following structure
PNG
media_image1.png
74
118
media_image1.png
Greyscale
; and
a Thermomyces lanuginosus lipase immobilized to the surface via non-covalent interactions;
wherein the support material has a pore diameter from about 20 nm to about 60 nm, a surface area from about 50 m.sup.2/g to about 200 m.sup.2/g, and a pore volume from about 0.5 mL/g to about 2.0 mL/g; and
claim 3 of the patent recites the biocatalyst for organic synthesis according to claim 1, wherein the support material is not a caged structure.
The claims of the patent do not recite the process of claims 1-13 of this application.
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the combined teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to use the biocatalyst of the claims of the patent in the interesterification reaction of Urata. One would have been motivated and expected success to do so because Urata teaches an interesterification reaction using an immobilized lipase, Mazeaud teaches suitable lipases including lipase from Thermomyces lanuginosus for an interesterification reaction using an immobilized lipase, and the claims of the patent recite a biocatalyst comprising an immobilized Thermomyces lanuginosus lipase.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9-11, the biocatalyst of the claims of the patent comprises a Thermomyces lanuginosus lipase.
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, claims 1-13 of this application are unpatentable over claims 1 and 3 of the patent in view of Urata and Mazeaud.
Co-Pending Application No. 19/462,717
Claims 1-13 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 9, 12, 15, 18, 21, and 26 of co-pending application no. 19/462,717 (reference application) in view of Urata and Mazeaud.
Claim 9 of the reference application recites a biocatalyst for organic synthesis, comprising:
a. a controlled porosity silica (CPS) as support material, having a pore diameter from about 20 to about 100 nm, wherein the support material comprises an amino-functionalized surface; and
b. one or more catalytically active enzyme(s) immobilized to the amino-functionalized surface by a covalent linker comprising a bond selected from amino, amide and imidoamide; and
claim 12 of the reference application recites (in relevant part) the biocatalyst according to claim 9, wherein the immobilized enzyme(s) is Thermomyces laguginosus lipase (TLL).
Claim 15 of the reference application recites a biocatalyst for organic synthesis, comprising:
a. a controlled porosity silica (CPS) as support material, having a pore diameter from about 20 to about 100 nm, wherein the support material comprises an amino-functionalized surface; and
b. one or more catalytically active enzyme(s) immobilized to the surface via non-covalent interactions; and
claim 18 of the reference application recites (in relevant part) the biocatalyst according to claim 15, wherein the immobilized enzyme(s) is Thermomyces laguginosus lipase (TLL).
Claim 21 of the reference application recites a biocatalyst for organic synthesis, comprising:
a. a controlled porosity silica (CPS) as support material, having a pore diameter from about 20 to about 100 nm, wherein the support material surface comprises at least two different coatings, of which at least one provides an amino functionalized surface; and
b. one or more catalytically active enzyme(s) immobilized on the surface, optionally by a covalent linker comprising a bond selected from amino, amide and imidoamide; and
claim 26 of the reference application recites (in relevant part) the biocatalyst according to claim 21, wherein the immobilized enzyme(s) is Thermomyces laguginosus lipase (TLL).
The claims of the reference application do not recite the process of claims 1-13 of this application.
Regarding the claim 1 limitations “providing a lipid-containing composition;
contacting the lipid-containing composition with an immobilized enzyme material comprising a carrier and at least one enzyme immobilized on the carrier, wherein the amount of the immobilized enzyme material is about 0.72% or less (by weight of the lipid-containing composition);
mixing the lipid-containing composition with the immobilized enzyme material to form a first enzymatically treated composition, wherein the mixing occurs for about 10 hours or less;”
Urata teaches an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 25 to 300 parts by weight of a fatty acid, 0.01 to 100 parts by weight of a product (obtained by the wetting treatment of 0.1 to 100 parts by weight of a lipase preparation comprising 0.01 to 10 parts by weight of the lipase and the balance of a carrier), and 0.01 to 10 parts by weight of a lipase activator for at least one hour (paragraph bridging columns 8-9).
The weight percent range of the lipase preparation in the interesterification reaction of Urata overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1. For example, the lipase preparation is about 0.0025% by weight in an interesterification reaction carried out by mixing 100 parts by weight of the oil or fat with 300 parts by weight of a fatty acid, 0.01 parts by weight of the lipase preparation, and 0.01 parts by weight of a lipase activator. According to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists and given that the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “about 0.72% or less (by weight of the lipid-containing composition)” as recited in instant claim 1, a prima facie case of obviousness exists.
Regarding the claim 1 limitation “separating the immobilized enzyme material from the first enzymatically treated composition;
contacting the immobilized enzyme material with at least one additional lipid-containing composition; and
mixing the at least one additional lipid-containing composition with the immobilized enzyme material to form a second enzymatically treated composition,”
Urata teaches that after completion of the interesterification reaction, the fatty acid and a small amount of the monoglyceride and diglyceride can be removed easily by conventional separation or purification techniques such as liquid-liquid extraction, alkali neutralization, vacuum or molecular distillation or a combination of these techniques to obtain the refined product (column 9, lines 24-30) and teaches that the lipase is substantially not deactivated in the course of the interesterification reaction and the lipase preparation recovered after completion of the reaction can be used effectively again (column 9, lines 41-45).
Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation.
Mazeaud teaches interesterification batch reactions carried out in flasks containing 0.5 g of immobilized enzyme product and 100 g of vegetable oil blend (p. 13, lines 21-29). Mazeaud teaches consecutive batch reactions with reuse of the enzyme (p. 13, lines 31-32). Mazeaud teaches a suitable lipase includes lipase from Thermomyces lanuginosus (p. 5, lines 27-30).
In view of the combined teachings of Urata and Mazeaud, it would have been obvious to one of ordinary skill in the art before the effective filing date to use the biocatalyst of the claims of the reference application in the interesterification reaction of Urata. One would have been motivated and expected success to do so because Urata teaches an interesterification reaction using an immobilized lipase, Mazeaud teaches suitable lipases including lipase from Thermomyces lanuginosus for an interesterification reaction using an immobilized lipase, and the claims of the reference application recite a biocatalyst comprising an immobilized Thermomyces lanuginosus lipase.
Regarding claim 2, as stated above, Example 3 of Urata (beginning at column 11, bottom) discloses four interesterification reactions with the repeated use of the lipase preparation. According to Example 3 of Urata, the lipase preparation was recovered following each interesterification reaction.
Regarding claims 3-5, the weight percent of the lipase preparation in the interesterification reaction of Urata encompasses a range that overlaps with “from about 0.15% to about 0.72%,” “from about 0.18% to about 0.72%,” and “from about 0.18% to about 0.5%” by weight of the lipid-containing composition as recited in instant claims 3-5, respectively, and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 6, Urata teaches the interesterification reaction is carried out for at least one hour and preferably at least several hours (column 9, lines 12-13) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 7, Urata teaches the interesterification reaction is carried out at a temperature of 20° to 80° C (column 9, lines 14-15) and according to MPEP 2144.05, where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists.
Regarding claim 8, Urata teaches an interesterification reaction (paragraph bridging columns 8-9).
Regarding claims 9-11, the biocatalyst of the claims of the patent comprises a Thermomyces lanuginosus lipase.
Regarding claim 12, Urata teaches the oils and fats include soybean oil (column 6, lines 39-42).
Regarding claim 13, Urata teaches the interesterification reaction is performed in batches with stirring in a closed vessel (see Examples 1 and 3), which is considered to be encompassed by “the enzymatic treatment is carried out in a stirred-tank reactor operating in batch mode” as recited in claim 13.
Therefore, claims 1-13 of this application are unpatentable over claims 9, 12, 15, 18, 21, and 26 of the reference application in view of Urata and Mazeaud. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not been patented.
Conclusion
Status of the claims:
Claims 1-13 are pending.
Claims 1-13 are rejected.
No claim is in condition for allowance.
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/David Steadman/Primary Examiner, Art Unit 1656
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