Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
1. Claims 1-16 filed 5/16/24 are present and under consideration.
2. Applicants’ filing that 18665634 filed 05/16/2024 is a Divisional of 16621957 , filed 12/12/2019, is incorrect.
This application is a continuation of 16621957 , filed 12/12/2019.
3. Priority
Applicant’s claim for domestic priority under 35 U.S.C. 119(e), filed 6/16/17, is acknowledged.
4. Drawings
The drawings filed on 5/16/24 are acknowledged.
5. Specification
The specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant's cooperation is requested in correcting any errors of which applicant may become aware in the specification.
6. IDS(s) filed 5/16/24 & 5/16/24 are acknowledged. Signed copies of the IDS(s) are provided with this Office Action.
7. Claim Rejections - 35 USC § 112
Claims 5-9 & 12 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 5-9 & 12 recites the limitation "wherein the alpha-amylase" in claim 1. There is insufficient antecedent basis for this limitation in the claim.
8. Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 1-6, 10, 11, and 13-16 is/are rejected under 35 U.S.C. 103 as being unpatentable over Poet Research (WO2017/059083 A1), Inc. (hereinafter Poet Research) in view of Slupska et al. (US 2011/0039308 A1) (hereinafter Slupska).
Regarding Claim 1, Poet Research teaches a method for increasing the oil yield in an ethanol production process [Para. §0003]. Also taught are methods and systems that provide improved processes for obtaining oils from a fermentation production process, such as an ethanol production process. In one aspect of the present application is disclosed a method of obtaining an oil composition from a stillage composition including: adding one or more alpha amylase enzymes to a first stillage composition to form a second stillage composition), comprising: adding a liquid enzyme formulation having at least one enzyme [Para. (§0016)]. Also disclosed herein is a method that includes adding alpha amylase to various stages in the processing and/or production of whole stillage to facilitate recovery of oil; [§0020], An enzyme can be added at one or more points of processing and production of still age composition to facilitate the recovery of oil. As shown in FIG. 1, enzyme 326 may be added to the stillage composition at one or more of 327, 328 and 329; [§0025], the alpha amylase may be added to the stillage composition and/or beer at a pH less than 4.2. In other embodiments, the alpha amylase may be added to a stillage composition and/or beer at a pH less than 4.0, or at a pH from about 3.2 to 3.9), to a beer, a distillation, a whole stillage [§0016]. Also disclosed herein is a method that includes adding alpha amylase to various stages in the processing and/or production of whole stillage to facilitate recovery of oil, a centrifugation, a thin stillage, an evaporator, a syrup, or an oil recovery unit.
Poet Research fails to explicitly disclose a liquid enzyme formulation comprising a buffering agent, a stabilizer, and a preservative wherein the pH of the enzyme formulation is about pH 6.0-8.0.
Slupska teaches liquid formulations of alpha amylase [§0498]. The invention provides detergent compositions comprising one or more polypeptides of the invention, for example, amylases and/or glucoamylases of the invention, such as alpha amylases and the detergent compositions can be a one and two part aqueous composition, comprising a buffering agent, a stabilizer, and a preservative [§0710], The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C ... Exemplary assay conditions to test for amylase activity, e.g., to determine if a polypeptide of the invention retains activity under particular conditions, include (MPB: Methylparaben); [§0713], 20% Sucrose (a stabilizer), 0.1 % MPB (methyl paraben preservative) in PBS (phosphate buffer and NaCl stabilizer)), wherein the pH of the enzyme formulation is about pH 6.0-8.0 [§0015], The invention also provides an enzymatic liquefaction process using at least one polypeptide of the invention comprising adjusting the pH of a granular polysaccharide, oligosaccharide or starch slurry to the pH optimum of an enzyme of the invention (e.g., a glucoamylase or an amylase of the invention) to be utilized, e.g., between 6.0 and 6.5; [§0499], The enzyme can be chosen to provide optimum activity and stability for any given set of utility conditions. In one aspect, the polypeptides of the present invention are active in the pH ranges of from about 4 to about 12 and in the temperature range of from about 20°C. to about 95°C.
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of using conditions optimal for preserving enzymatic activity as taught by Slupska [§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C. was selected as the storage buffer of choice.
Regarding Claim 2, Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research fails to explicitly disclose wherein the pH of the liquid enzyme formulation is about pH 6.3-6.7. Slupska teaches a pH of a liquid enzyme formulation is about pH 6.3-6.7 [§0015], The invention also provides an enzymatic liquefaction process using at least one polypeptide of the invention comprising adjusting the pH of a granular polysaccharide, oligosaccharide or starch slurry to the pH optimum of an enzyme of the invention (e.g., a glucoamylase or an amylase of the invention) to be utilized, e.g., between 6.0 and 6.5; [0499], The enzyme can be chosen to provide optimum activity and stability for any given set of utility conditions. In one aspect, the polypeptides of the present invention are active in the pH ranges of from about 4 to about 12 and in the temperature range of from about 20° C. to about 95° C).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of using conditions optimal for preserving enzymatic activity as taught by Slupska [§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C. was selected as the storage buffer of choice).
Regarding Claim 3, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research fails to explicitly disclose wherein the stabilizer comprises sucrose, sorbitol, mannitol, glycerol, trehalose, sodium chloride, sodium sulfate, or any combination thereof.
Slupska teaches a stabilizer comprises sucrose and sodium chloride [§0713], 20% Sucrose, 0.1% MPB in PBS.
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of using conditions optimal for preserving enzymatic activity as taught by Slupska (§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C. was selected as the storage buffer of choice).
Regarding Claim 4, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research fails to explicitly disclose wherein the buffering agent comprises: sodium citrate, potassium citrate, citric acid, sodium acetate, acetic acid, sodium phosphate, potassium phosphate. or any combination thereof.
Slupska teaches a buffering agent comprises sodium phosphate [§0713], 20% Sucrose, 0.1 % MPB in PBS).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of using conditions optimal for preserving enzymatic activity as taught by Slupska [§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C was selected as the storage buffer of choice).
Regarding Claim 5, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research further discloses wherein the alpha-amylase retains activity at a temperature of 4•.40• C [§0041], The stillage composition used to obtain oil may itself be obtained from an ethanol fermentation production process. In one embodiment, the fermentation process can be carried out without creating a hot slurry (i.e., without cooking). In some embodiments, fermentation can be carried out without a liquefaction step. The fermentation process may be carried out with a saccharification step of the starch composition with an enzyme composition to form a saccharified composition (e.g., without cooking). In some embodiments, the enzyme composition used for saccharification can include an alpha amylase and glucoamylase added at a pH from 3 to 6 or al a pH from 4 to 5. In some embodiments the enzyme composition that may be used for saccharification may be added at a temperature from 25°C to 40°C).
Poet Research fails lo explicitly disclose wherein the alpha-amylase retains at least 90% of its activity.
Slupska teaches storage of a liquid formulation of alpha-amylase at temperatures of 4° or 37° degrees Celsius where greater than 90% of enzyme activity is retained at 37° C as compared to 4° C [§0710], The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C was selected as the storage buffer of choice; Figure 16. see MBP acetate at 37° and 4° C for instance).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of choosing conditions that best preserve enzyme activity as taught by Slupska.
Regarding Claim 6, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research further discloses wherein the alpha-amylase retains activity at a temperature of 25° -30° C [§0041 ]. The stillage composition used to obtain oil may itself be obtained from an ethanol fermentation production process. In one embodiment, the fermentation process can be carried out without creating a hot slurry (i.e., without cooking). In some embodiments, fermentation can be carried out without a liquefaction step. The fermentation process may be carried out with a saccharification step of the starch composition with an enzyme composition to form a saccharified composition (e.g., without cooking). In some embodiments, the enzyme composition used for saccharification can include an alpha amylase and glucoamylase added at a pH from 3 to 6 or at a pH from 4 to 5. In some embodiments the enzyme composition that may be used for saccharification may be added at a temperature from 25°C to 40°C).
Poet Research fails to explicitly disclose wherein the alpha-amylase retains at least 90% of its activity.
Slupska teaches storage of a liquid formulation of alpha-amylase at temperatures of 4° or 37°C where greater than 90% of enzyme activity is retained at 37° C as compared to 4°C [§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C was selected as the storage buffer of choice; Figure 16, see MBP acetate at 37° and 4° C for instance.
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of choosing conditions that best preserve enzyme activity as taught by Slupska.
Regarding Claim 10, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research fails to explicitly disclose wherein the preservative comprises: potassium sorbate, sodium sorbate, sorbic acid, sodium benzoate, benzoic acid, methyl paraben, calcium propionate, sodium propionate, ammonium propionate, propionic acid, or any combination thereof
Slupska teaches a preservative comprises methyl paraben [§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below for particular conditions, that include (MPB: Methylparaben).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of using conditions optimal for preserving enzymatic activity as taught by Slupska [§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C. was selected as the storage buffer of choice.
Regarding Claim 11, modified Poet Research discloses the liquid enzyme formulation of Claims 1. Poet Research fails to explicitly disclose said formulation further comprising at least two preservatives.
Slupska teaches enzyme formulations comprising at least two preservatives [§0631], These additional components include, but are not limited to, one or more of the following preservatives [see §0710]. The activities of the purified enzymes were compared in different storage buffers, as listed below for particular conditions, include (MPB: Methylparaben).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of using conditions optimal for preserving enzymatic activity as taught by Slupska [§0710]. The activities of the purified enzymes were compared in different storage buffers, as listed, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C. was selected as the storage buffer of choice.
Regarding Claim 13, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research further discloses comprising a second enzyme [§0041]. In some embodiments, the enzyme composition used for saccharification can include an alpha amylase and glucoamylase added at a pH from 3 to 6 or at a pH from 4 to 5. In some embodiments the enzyme composition that may be used for saccharification may be added at a temperature from 25°C to 40°C.
Regarding Claim 14, modified Poet Research discloses the liquid enzyme formulation of Claim 13. Poet Research further discloses wherein the second enzyme is selected from the group consisting of a second alpha-amylase, a beta-amylase, a glucoamylase, a protease, a phytase, a pullulanase, a cellulase, a cellobiohydrolase, a betaglucosidase, an endoglucanase, a mannanase, a xylanase, a lipase, a phospholipase, and any combination thereof [§0041], In some embodiments, the enzyme composition used for saccharification can include an alpha amylase and glucoamylase added at a pH from 3 to 6 or at a pH from 4 to 5. In some embodiments the enzyme composition that may be used for saccharification may be added at a temperature from 25°C to 40°C.
Regarding Claim 15, modified Poet Research discloses the method of claim 1. Poet Research further discloses wherein a liquid enzyme formulation having at least one enzyme is added to a first stillage composition to form a second stillage composition , wherein the one or more alpha amylase enzymes are added to the first stillage composition in an amount from 0.001 to 0.01 grams/100 grams of solids of the first stillage composition; and obtaining oil from the second stillage composition [§0002], adding one or more alpha amylase enzymes to a first stillage composition to form a second stillage composition, wherein the one or more alpha amylase enzymes are added to the first stillage composition in an amount from 0.001 to 0.05 grams/100 grams of solids of the first stillage composition; and obtaining oil from the second stillage composition.
Regarding Claim 16, modified Poet Research discloses the method of claim 15, wherein the first stillage composition comprises whole stillage, thin stillage, wet cake and/or syrup. [§0004], wherein one or more alpha amylase enzymes are added to the whole stillage, thin still age, wet cake and /or syrup in an amount from 0.001 to 0.05 grams/100 grams of solids of the whole still age, thin stillage, wet cake and/or syrup).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Slupska for the purpose of using conditions optimal for preserving enzymatic activity as taught by Slupska [§0710], and do so with a reasonable expectation of success. One of ordinary skill in the art would have been motivated in view of the importance to market an aqueous enzyme composition, wherein, the enzyme is stabile so that it will retain its functional activity for prolonged periods of time (e.g. shelf-life or storage)).
The activities of the purified enzymes were compared in different storage buffers, as listed, after 1 week of incubation at 37° C. The buffer with the lowest loss of activity compared to the activity of the same enzyme kept at +4° C. was selected as the storage buffer of choice
Claims 7-9 is/are rejected under 35 U.S.C. 103 as being unpatentable over Poet Research (WO2017/059083 A1), Inc. (hereinafter Poet Research) in view of Slupska et al. (US 2011/0039308 A1) (hereinafter Slupska) and Hunt, Jr. et al. (US 2014/0073036A1)(hereinafter Hunt).
Regarding Claim 7, modified Poet Research discloses the liquid enzyme formulation of Claims 1. Poet Research fails to explicitly disclose wherein the alpha-amylase retains at least 90% of its activity for 1 year.
Hunt teaches liquid formulations of amylase which retain at least 90% activity for at least 1 year [§0037], According to an embodiment of the invention the compositions include a surfactant stabilizing agent and a mixture of enzymes ... the mixture of enzymes includes a combination of two or more of the following enzymes: protease, amylase, lipase, gluconase, cellulase and/or peroxidase. In a preferred aspect, the combination of enzymes includes a protease, a lipase and/or an amylase; [0036], In certain embodiments the liquid formulations according to embodiments of the invention are stable for at least 1 year. As referred to herein, compositional stability means that the enzymes in the liquid stable enzyme composition retain at least about 80% of its initial enzyme activity at ambient temperature, preferably at least about 90% of its initial enzyme activity, preferably at least about 95% of its initial enzyme activity, and most preferably 100% of its initial enzyme activity).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Hunt for the purpose of providing enzyme compositions with extended shelf-life as taught by Hunt [§0003], and do so with a reasonable expectation of success. One of ordinary skill in the art would have been motivated in view of the importance to market an aqueous enzyme composition, wherein the enzyme is stabile so that it will retain its functional activity for prolonged periods of time (e.g. shelf-life or storage)).
Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Poet Research (WO2017/059083 A1), Inc. (hereinafter Poet Research) in view of Slupska et al. (US 2011/0039308 A1) (hereinafter Slupska) and Gerendash (US 2003/0013172 A1).
Regarding Claim 12, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research fails to explicitly disclose wherein the alpha-amylase comprises an amino acid sequence having at least 8 0%, 8 1%, 8 2 %, 8 3 %, 8 4 %, 8 5 %, 8 6 %, 87%, 88%, 89%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one of the amino acid sequences set forth in SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, SEQ ID NO:13, and SEQ ID NO:14.
Gerendash teaches an alpha-amylase comprising a sequence 100% identical to SEQ ID NO: 1 of the instant application (Abstract). The invention relates to alpha amylases and to polynucleotides encoding the alpha amylases [§0146], the isolated nucleic acids of one of the SEQ ID NO:I nucleic acid sequences, and sequences substantially identical thereto, may be used to prepare one of the polypeptides of a SEQ ID N0: 2 amino acid sequence, and sequences substantially identical thereto; See SEQ ID NO: 2 in Fig. 7).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology at the time of the invention to modify Poet Research with the teaching of Gerendash for the purpose of providing an enzyme with multiple commercial uses as taught by Gerendash [§0003]. Amylases are of considerable commercial value, being used in the initial stages (liquefaction) of starch processing; in corn wet milling; in alcohol production; as cleaning agents in detergent matrices; in the textile industry for starch desizing; in baking applications; in the beverage industry; in oilfields in drilling processes; in inking of recycled paper; and in animal feed).
Regarding Claim 8, modified Poet Research discloses the liquid enzyme formulation of Claim 1. Poet Research fails to explicitly disclose wherein the alpha-amylase has a shelf life of at least 1 year.
Hunt teaches an amylase has a shelf life of at least 1 year [§0037]. According to an embodiment of the invention the compositions include a surfactant stabilizing agent and a mixture of enzymes ... the mixture of enzymes includes a combination of two or more of the following enzymes: protease, amylase, lipase, gluconase, cellulase and/or peroxidase. In a preferred aspect, the combination of enzymes includes a protease, a lipase and/or an amylase; [§0036]. In certain embodiments the liquid formulations according to embodiments of the invention are stable for at least 1 year. As referred to herein, compositional stability means that the enzymes in the liquid stable enzyme composition retain at least about 80% of its initial enzyme activity at ambient temperature, preferably at least about 90% of its initial enzyme activity, preferably at least about 95% of its initial enzyme activity, and most preferably 100% of its initial enzyme activity).
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology to modify Poet Research with the teaching of Hunt for the purpose of providing enzyme compositions with extended shelf-life as taught by Hunt [§0003], and do so with a reasonable expectation of success. One of ordinary skill in the art would have been motivated in view of the importance to market an aqueous enzyme composition, the enzyme must be stabilized so that it will retain its functional activity for prolonged periods of time (e.g. shelf-life or storage)).
Regarding Claim 9, modified Poet Research discloses the liquid enzyme formulation of Claim 8. Poet Research fails to explicitly disclose wherein the alpha-amylase has a shelf life of at least 1 year at 25oC.
Hunt teaches an amylase has a shelf life of at least 1 year at 25°C [§0037]. According to an embodiment of the invention the compositions include a surfactant stabilizing agent and a mixture of enzymes ... the mixture of enzymes includes a combination of two or more of the following enzymes: protease, amylase, lipase, gluconase, cellulase and/or peroxidase. In a preferred aspect, the combination of enzymes includes a protease, a lipase and/or an amylase [§0036]. In certain embodiments the liquid formulations according to embodiments of the invention are stable for at least 1 year. As referred to herein, compositional stability means that the enzymes in the liquid stable enzyme composition retain at least about 80% of its initial enzyme activity at ambient temperature, preferably at least about 90% of its initial enzyme activity, preferably at least about 95% of its initial enzyme activity, and most preferably 100% of its initial enzyme activity [§0115], ambient temperature refers to the temperature of the surroundings of the liquid stabilized enzyme composition under normal conditions for storage or transportation. Although the compositions may be stored and transported at temperatures in the range of about -10° F. to about 100° F., ambient temperatures preferably refers to room temperatures of about 72° F. or 25° C. [§0127]
It would have been obvious before the effective filing date of the claimed invention for one of ordinary skill in the art of enzymology/biotechnology to modify Poet Research with the teaching of Hunt for the purpose of providing enzyme compositions with extended shelf-life as taught by Hunt [§0003], and do so with a reasonable expectation of success. One of ordinary skill in the art would have been motivated in view of the importance to market an aqueous enzyme composition, wherein the enzyme is stabile so that it will retain its functional activity for prolonged periods of time (e.g. shelf-life or storage)).
9. 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 1-16 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 12,110,531. Although the claims at issue are not identical, they are not patentably distinct from each other.
Instant claims are drawn to:
1. A method for increasing the oil yield in an ethanol production process comprising: adding a liquid enzyme formulation having at least one enzyme titrated from a pH of 8.0 to 10.5, a buffering agent, a stabilizer, and a preservative wherein the pH of the enzyme formulation is about pH 6.0-8.0 to a beer, a distillation, a whole stillage, a centrifugation, a thin stillage, an evaporator, a syrup, or an oil recovery unit.
2. The liquid enzyme formulation of claim 1, wherein the pH of the liquid enzyme formulation is about pH 6.3-6.7.
3. The liquid enzyme formulation of claim 1, wherein the stabilizer comprises sucrose, sorbitol, mannitol, glycerol, trehalose, sodium chloride, sodium sulfate, or any combination thereof.
4. The liquid enzyme formulation of claim 1, wherein the buffering agent comprises: sodium citrate, potassium citrate, citric acid, sodium acetate, acetic acid, sodium phosphate, potassium phosphate, or any combination thereof.
5. The liquid enzyme formulation of claim 1, wherein the alpha-amylase retains at least 90% of its activity at a temperature of 4-40° C.
6. The liquid enzyme formulation of claim 1, wherein the alpha-amylase retains at least 90% of its activity at a temperature of 25-30° C.
7. The liquid enzyme formulation of claim 1, wherein the alpha-amylase retains at least 90% of its activity for 1 year.
8. The liquid enzyme formulation of claim 1, wherein the alpha-amylase that has a shelf life of at least 1 year.
9. The liquid enzyme formulation of claim 8, wherein the alpha-amylase has a shelf life of at least 1 year at 25° C.
10. The liquid enzyme formulation of claim 1, wherein the preservative comprises: potassium sorbate, sodium sorbate, sorbic acid, sodium benzoate, benzoic acid, methyl paraben, calcium propionate, sodium propionate, ammonium propionate, propionic acid, or any combination thereof.
11. The liquid enzyme formulation of claim 1, further comprising at least two preservatives.
12. The liquid enzyme formulation of claim 1, wherein the alpha-amylase comprises an amino acid sequence having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one of the amino acid sequences set forth in SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, SEQ ID NO:13, and SEQ ID NO:14.
13. The liquid enzyme formulation of claim 1, further comprising a second enzyme.
14. The liquid enzyme formulation of claim 13, wherein the second enzyme is selected from the group consisting of a second alpha-amylase, a beta-amylase, a glucoamylase, a protease, a phytase, a pullulanase, a cellulase, a cellobiohydrolase, a beta-glucosidase, an endoglucanase, a mannanase, a xylanase, a lipase, a phospholipase, and any combination thereof.
15. The method of claim 1, wherein a liquid enzyme formulation having at least one enzyme is added to a first stillage composition to form a second stillage composition, wherein the one or more alpha amylase enzymes are added to the first stillage composition in an amount from 0.001 to 0.01 grams/100 grams of solids of the first stillage composition; and obtaining oil from the second stillage composition.
16. The method of claim 15, wherein the first stillage composition comprises whole stillage, thin stillage, wet cake and/or syrup.
Claims of US Patent 12,110,531 are drawn to as follows.
1. A method for increasing the oil yield in an ethanol production process comprising: adding a liquid enzyme formulation having an alpha-amylase titrated from a pH of 8.0 to 10.5, a buffering agent, a stabilizer, and a preservative wherein the pH of the enzyme formulation is about pH 6.0-8.0 to a beer, a distillation, a whole stillage, a centrifugation, a thin stillage, an evaporator, a syrup, or an oil recovery unit, and wherein the alpha-amylase comprises an amino acid sequence having at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to one of the amino acid sequences set forth in SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9, SEQ ID NO:10, SEQ ID NO:11, SEQ ID NO:12, SEQ ID NO:13, and SEQ ID NO:14.
2. The liquid enzyme formulation of claim 1, wherein the pH of the liquid enzyme formulation is about pH 6.3-6.7.
3. The liquid enzyme formulation of claim 1, wherein the stabilizer comprises sucrose, sorbitol, mannitol, glycerol, trehalose, sodium chloride, sodium sulfate, or any combination thereof.
4. The liquid enzyme formulation of claim 1, wherein the buffering agent comprises: sodium citrate, potassium citrate, citric acid, sodium acetate, acetic acid, sodium phosphate, potassium phosphate, or any combination thereof.
5. The liquid enzyme formulation of claim 1, wherein the alpha-amylase retains at least 90% of its activity at a temperature of 4-40° C.
6. The liquid enzyme formulation of claim 1, wherein the alpha-amylase retains at least 90% of its activity at a temperature of 25-30° C.
7. The liquid enzyme formulation of claim 1, wherein the alpha-amylase retains at least 90% of its activity for 1 year.
8. The liquid enzyme formulation of claim 1, wherein the alpha-amylase has a shelf life of at least 1 year.
9. The liquid enzyme formulation of claim 8, wherein the alpha-amylase has a shelf life of at least 1 year at 25° C.
10. The liquid enzyme formulation of claim 1, wherein the preservative comprises: potassium sorbate, sodium sorbate, sorbic acid, sodium benzoate, benzoic acid, methyl paraben, calcium propionate, sodium propionate, ammonium propionate, propionic acid, or any combination thereof.
11. The liquid enzyme formulation of claim 1, further comprising at least two preservatives.
12. The liquid enzyme formulation of claim 1, further comprising a second enzyme.
13. The liquid enzyme formulation of claim 12, wherein the second enzyme is selected from the group consisting of a second alpha-amylase, a beta-amylase, a glucoamylase, a protease, a phytase, a pullulanase, a cellulase, a cellobiohydrolase, a beta-glucosidase, an endoglucanase, a mannanase, a xylanase, a lipase, a phospholipase, and any combination thereof.
14. The method of claim 1, wherein a liquid enzyme formulation having at least one enzyme is added to a first stillage composition to form a second stillage composition, wherein the one or more alpha amylase enzymes are added to the first stillage composition in an amount from 0.001 to 0.01 grams/100 grams of solids of the first stillage composition; and obtaining oil from the second stillage composition.
15. The method of claim 14, wherein the first stillage composition comprises whole stillage, thin stillage, wet cake and/or syrup.
Given the fact pattern of the instant case as well as the patent the species claims of the patent anticipates the instant genus claims.
10. No claim is allowed.
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to TEKCHAND SAIDHA whose telephone number is (571)272-0940. The examiner can normally be reached on M-F 8.00-5.30. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert B Mondesi can be reached on 408 918 7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/TEKCHAND SAIDHA/
Primary Examiner, Art Unit 1652
Recombinant Enzymes, Hoteling
Telephone: (571) 272-0940
Fax: (571) 273-0940