DETAILED ACTION
Claims 1, 10, and 14-15 are amended.
New claims 22-28 have been added.
Claims 16-19, and 28 are withdrawn.
Claims 20-21 are cancelled.
Claims 1-19, and 22-28 are pending.
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 .
Election/Restrictions
Newly submitted claim 28 is directed to an invention that is independent or distinct from the invention originally claimed for the following reasons: newly Claim 28 is dependent upon a withdrawn method claim (claim 17), and comprises method steps of using the recombinant host cell of claim 1. The method steps are not included as part of the recombinant host cell of claim 1. Because claim 28 is dependent upon withdrawn claim 17, claim 28 is drawn to an unelected group and is withdrawn based on applicant’s previous election. Claim 28 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 12/04/2024.
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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
(previous rejection, withdrawn) Claim 10 was previously rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point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.
(previous rejection, withdrawn) Claim 14 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and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.
Applicants Arguments: Applicant has amended claims 10 and 14 to overcome this rejection.
Response to arguments: The examiner acknowledges the amendments made to claims 10 and 14. The previous 112b rejection of claims 10 and 14 is withdrawn.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
(previous rejection, withdrawn) Claims 1-7, 9-12, and 14-15 were previously rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Argyros, US 20140295516 A1 (see form PTO-892).
Regarding claims 1 and 14, Argyros teaches a recombinant S. cerevisiae host cell comprising a heterologous polynucleotide encoding a sugar transporter, wherein the transporter has a mature polypeptide sequence with at least 80% sequence identity to SEQ ID NO: 387 (Argyros, claims 1-3, claim 12) ; and wherein the cell comprises an active pentose fermentation pathway (Argyros, [98]). A sequence search found that SEQ ID NO:15 from Argyros, US 20140295516 A1, is a 92.8% identity match for instant SEQ ID NO: 387. The search results and alignment are shown below:
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701
1227
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188
826
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Regarding claim 2, Argyros teaches that the recombinant host cell comprises an active xylose fermentation pathway (Argyros, claim 14).
Regarding claim 3, Argyros teaches that the recombinant host cell comprises the active xylose fermentation genes: a heterologous xylose isomerase (Argyros, claim 8), a heterologous xylulokinase (Argyros, claim 18; [18]).
Regarding claim 4, Argyros teaches that the cell comprises the active xylose fermentation pathway genes: a heterologous xylulokinase (Argyros, claim 18; [18]).
Regarding claim 5, Argyros teaches that the recombinant host cell comprises an active arabinose fermentation pathway (Argyros, claim 14; [10]; [16])
Regarding claim 6, Argyros teaches that the recombinant host cell comprises the active arabinose fermentation pathway genes: heterologous L-arabinose isomerase (Argyros, claim 1, [44]), heterologous L-ribulokinase (Argyros, claim 1, [44]), heterologous L-ribulose-5-P4-epimerase (Argyros, claim 1, [44]).
Regarding claim 7, Argyros teaches that the recombinant host cell comprises the active arabinose fermentation genes: heterologous xylulokinase (Argyros, claim 18, [18]).
Regarding claim 9, Argyros teaches that the recombinant host cell is capable of higher anaerobic growth rate on pentose compared to the same cell without the heterologous polynucleotide encoding a sugar transporter (Argyros, [60]; [79]; [32-34]).
Regarding claim 10, Argyros teaches that the recombinant host cell is capable of higher pentose consumption compared to the same cell without the heterologous polynucleotide encoding a sugar transporter at 48 hours of fermentation (Argyros, [31-34]). Additionally, Argyros teaches that the recombinant host cell is capable of consuming arabinose as the sole carbon source, whereas the same cell without the heterologous polynucleotide encoding a sugar transporter did not consume any arabinose in the same environment (Argyros, [204]). Although, Argyros does not explicitly disclose that the recombinant host cell is capable of higher pentose consumption than the unmodified cell at about or after 120 hours, the recombinant host cell taught by Argyros is substantially identical in composition and structure to the recombinant host cell of claim 10. According to MPEP 2112.01(I): When the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Therefore, based on the teachings of Argyros, and because the recombinant host cell taught by Argyros is substantially identical to that of claim 10, it is presumed that the recombinant host cell taught by Argyros is capable of higher pentose consumption than the unmodified cell at about or after 120 hours.
Regarding claim 11, Argyros teaches that the recombinant host cell is capable of higher ethanol production compared to the same cell without the heterologous polynucleotide encoding a sugar transporter under the same conditions (Argyros, [32-34]).
Regarding claim 12, Argyros teaches that the recombinant host cell is capable of higher ethanol production compared to the same cell without the heterologous polynucleotide encoding a sugar transporter under the same conditions (Argyros, [32-34]).
Regarding claim 15, Argyros teaches a composition comprising the recombinant host cell and one or more naturally and/or non-naturally occurring components such as gums (i.e., YP medium containing agar) (Argyros, [205]).
Applicants arguments: Applicant Argues that claim 1 has been amended, and that Argyros no longer anticipates claims 1-7, 9-12, and 14-15.
Response to applicants arguments: The examiner agrees with applicants arguments that amended claim 1 is no longer anticipated by Argyros. Accordingly, the previous rejection of claims 1-7, 9-12, and 14-15 is withdrawn.
(new rejection) Claims 1-7, 9-12, 14-15, 22-23 and 25-27 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Argyros, US 20170191088 A1 (see form PTO-892 notice of references cited) and evidenced by Uniprot ID A1C8W7_ASPCL1 (see form PTO-892 notice of references cited).
Regarding claim 1, Argyros teaches a recombinant eukaryotic host cell comprising a AraT sugar transporter. Argyros teaches the AraT sugar transporter is derived from Aspergillus clavatus (ACLA_044740). Argyros teaches that the host cell comprises a pentose fermentation pathway (Argyros, [79]; [86]; [184]).
Regarding claim 2, Argyros teaches the host cell comprises an active xylose fermentation pathway (Argyros, [184]).
Regarding claims 3 and 4, Argyros teaches that the host cell comprises heterologous polynucleotides encoding xylose isomerase, a xylulokinase, xylitol dehydrogenase, and a xylose reductase (Argyros, claims 8, 13; [15]; [48])
Regarding claim 5, Argyros teaches that the host cell comprises an active arabinose fermentation pathway (Argyros, claim 7).
Regarding claim 6, Argyros teaches that the host cell comprises heterologous polynucleotides encoding an L-arabinose isomerase, an L-ribulokinase, and an L-ribulose-5-epimerase (Argyros, claims 1, 5; [44]).
Regarding claim 7, Argyros teaches that the host cell comprises heterologous polynucleotides encoding a xylulokinase, xylitol dehydrogenase, and an L-xylose reductase (Argyros, claims 8, 13; [15]; [44]; [48]).
Regarding claim 8, Argyros does not teach claim 8. See if the substrates used in their embodiments would be beneficial for amylase enzymes
Regarding claims 9 and 10, Argyrose teaches that the recombinant host cell is capable of higher consumption and growth on arabinose (a pentose sugar) compared to the same cell without the heterologous polynucleotide encoding a sugar transporter (Argyrose, [206]; fig. 7).
Regarding claim 11, Argyros teaches that the recombinant host cell is capable of producing higher ethanol titers compared to the same cell without the heterologous polynucleotide encoding a sugar transporter (Argyros, [82], [206]; fig. 7).
Regarding claim 12, Argyros teaches that the recombinant host cell comprises a heterologous polynucleotide encoding a transketolase and transaldolase (Argyros, claim 13).
Regarding claims 14 and 22, Argyros teaches that the recombinant host cell is an S. cerevisiae cell (Argyros, claim 12).
Regarding claim 15, Argyros teaches a composition comprising the recombinant host cell and one or more naturally and/or non-naturally occurring components such as gums (i.e., YMA, which is a form of medium containing agar gel) (Argyros, [201]).
Regarding claim 23, Argyros teaches that the heterologous polynucleotide encoding a sugar transporter is operably linked to a foreign promoter (i.e., exogenous, or surrogate promoter) (Argyros, [41]).
Regarding claims 1, and 25-27, Argyros does not explicitly disclose the amino acid sequence of the mature sugar transporter. However, Argyros teaches the recombinant eukaryotic host cell comprising a AraT sugar transporter (Argyros, claim 1). Argyros teaches the AraT sugar transporter is derived from Aspergillus clavatus (ACLA_044740) (Argyros, [51]).
A sequence search of SEQ ID NO: 387 provided the following result from Uniprot:
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952
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67
912
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434
824
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441
851
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As shown above, the amino acid sequence of Uniprot ID A1C8W7_ASPCL is encoded by open reading frame ACLA_04470 from Aspergillus clavatus. The citation of Uniprot serves as evidence that the sequence of the sugar transporter taught by Argyros inherently comprises the amino acid sequence of instant SEQ ID NO: 387 (see MPEP 2112 III-IV for Requirements of Rejection Based on Inherency). Both Argyros and Uniprot cite the same open reading frame from Aspergillus clavatus as being the coding sequence for the sugar transporter, AraT. Therefore, it appears inherent that the teachings of Argyros anticipate claims 1-7, 9-12, 14-15, 22-23, and 25-27.
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.
(previous rejection, withdrawn) Claim 8 was previously rejected under 35 U.S.C. 103 as being unpatentable over Argyros, US 20140295516 A1, as applied to claims 1-7, 9-12, and 14-15 above, and further in view of Purkan2 (see form PTO-892).
The teachings of Argyros, as they apply to claim 1, are shown above.
Argyros does not teach that the recombinant host cell of instant claim 1 further comprises a heterologous polynucleotide encoding a glucoamylase, alpha- amylase, phospholipase, trehalase, protease, or pullulanase.
Purkan teaches an S. cerevisiae cell that comprises a heterologous polynucleotide encoding a glucoamylase (Purkan, pg. 4, [2]).
It would have been obvious to one of ordinary skill in the art to modify the recombinant host cell taught by Argyros, with the heterologous polynucleotide encoding a glucoamylase taught by Purkan. One would be motivated to combine these teachings because the S. cerevisiae host cell taught by Argyros is intended for use in ethanol production via fermentation of starches (Argyros, [18-24]). However, Argyros teaches the use of external enzymes for the saccharification of starches (Argyros, [76]). The use of an external enzyme is necessary because S. cerevisiae do not produce these enzymes naturally (Purkan, pg. 2, [3]). Modifying an S. cerevisiae host cell to express a heterologous glucoamylase gene allows S. cerevisiae to ferment starch and produce ethanol without the use of an external enzyme (Purkan, pg. 7). Therefore, combining the teachings of Argyros and Purkan may result in a simplified process that includes a simultaneous saccharification/fermentation process without the use of an external enzyme (Argyros, [76]). Furthermore, starch containing biomass is relatively inexpensive, and it would therefore be beneficial to use as a substrate for ethanol production (Purkans, abstract). A person having ordinary skill in the art would have a reasonable expectation of success in combining the above teachings of Argyros and Purkan. The host cell taught by Argyros is an S. cerevisiae cell, and the cell modified to express glucoamylase taught by Purkan is also an S. cerevisiae cell (Purkan, pg. 2, [3]). Additionally, Purkans demonstrates that an S. cerevisiae cell modified with a heterologous glucoamylase encoding polypeptide can successfully convert starch into ethanol (Purkans, pg. 7, [1]). Therefore, it would have been obvious to combine the above teachings of Argyros and Purkans. Accordingly, claim 8 is rejected.
Applicants arguments: Applicant Argues that claim 8 is no longer rendered obvious by the teachings of Argyros and Purkans due to the amendment of independent claim 1 from which claim 8 depends.
Response to applicants arguments: The examiner agrees with applicant that claim 8 is no longer rendered obvious by the combination of Argyros and Purkans. Accordingly, the previous rejection of claim 8 is withdrawn.
(previous rejection, withdrawn) Claim 13 was previously rejected under 35 U.S.C. 103 as being unpatentable over Argyros, US 20140295516 A1, as applied to claims 1-7, 9-12, and 14-15 above, and further in view of Guadalupe-Medina3 (see form PTO-892).
The teachings of Argyros as they apply to claim 1 are shown above.
Argyros does not teach that the recombinant host cell of claim 1 further comprises a disruption to an endogenous gene encoding a glycerol-3-phosphate dehydrogenase (GPD) and/or a disruption to an endogenous gene encoding a glycerol-3-phosphatase (GPP).
Guadalupe-Medina teach an S. cerevisiae cell that comprises a deletion of an endogenous GPD (Guadalupe-Medina, pg. 6, left column).
It would have been obvious to combine the host cell as taught by Argyros and applied to claim 1 with the GPD deletion taught by Guadalupe-Medina. One would be motivated to combine the above teachings because the deletion of GPD offers improved ethanol yield. Guadalupe-Medina teaches that an S. cerevisiae cell comprising a deleted GPD converted sugar into ethanol at increased yields relative to the control strain (Guadalupe-Medina, pg. 6, left column). Additionally, Guadalupe-Medina suggest that GPD deletion S. cerevisiae strain produces less acetic acid, which may be particularly beneficial during simultaneous saccharification and fermentation processes, which is the same process the host cell taught by Argyros is intended to be used for (Argyros, [76]). Argyros also suggests that particular endogenous genes or polynucleotides may be deleted (Argyros, [61-62]). Furthermore, one would have a reasonable expectation of success combining the above teachings of Argyros and Guadalupe-Medina. Both Argyros and Guadalupe-Medina teach an S. cerevisiae strain that can ferment sugars in order to produce ethanol. Additionally, bioethanol production using S. cerevisiae is well known in the art (Guadalupe-Medina, pg. 1, right column), and the skilled artisan would be able to use known techniques to modify the cell taught by Argyros by deleting the GPD gene as taught by Guadalupe-Medina (Guadalupe-Medina, pg. 7, left column). Therefore, it would have been obvious to combine the above teachings of Argyros and Guadalupe-Medina. Accordingly, claim 13 is rejected.
Applicants arguments: Applicant has not provided an argument specifically regarding claim 13.
Examiners response: Although applicant has not made arguments specifically regarding claim 13, it is noted that independent claim 1, from which claim 13 depends, has been amended, and the combination of teachings from Argyros and Guadalupe-Medina no longer renders claim 13 obvious. Accordingly, the previous rejection of claim 13 is withdrawn.
(new rejection) Claims 1-7, 9-12, 14-15, 22-23, and 25-27 are rejected under 35 U.S.C. 103 as being unpatentable over Argyros, US 20170191088 A1 (cited above) and Uniprot ID A1C8W7_ASPCL (cited above).
The rejection of claims 1-7, 9-12, 14-15, 22-23 and 25-27 under 35 U.S.C. 102(a)(1) set forth above are incorporated by reference. Although such claims are stated to be anticipated, the following is further noted.
Regarding claim 1, Argyros teaches a recombinant eukaryotic host cell comprising a AraT sugar transporter. Argyros teaches the AraT sugar transporter is derived from Aspergillus clavatus (ACLA_044740). Argyros teaches that the host cell comprises a pentose fermentation pathway (Argyros, [79]; [86]; [184]).
Regarding claim 2, Argyros teaches the host cell comprises an active xylose fermentation pathway (Argyros, [184]).
Regarding claims 3 and 4, Argyros teaches that the host cell comprises heterologous polynucleotides encoding xylose isomerase, a xylulokinase, xylitol dehydrogenase, and a xylose reductase (Argyros, claims 8, 13; [15]; [48])
Regarding claim 5, Argyros teaches that the host cell comprises an active arabinose fermentation pathway (Argyros, claim 7).
Regarding claim 6, Argyros teaches that the host cell comprises heterologous polynucleotides encoding an L-arabinose isomerase, an L-ribulokinase, and an L-ribulose-5-epimerase (Argyros, claims 1, 5; [44]).
Regarding claim 7, Argyros teaches that the host cell comprises heterologous polynucleotides encoding a xylulokinase, xylitol dehydrogenase, and an L-xylose reductase (Argyros, claims 8, 13; [15]; [44]; [48]).
Regarding claim 8, Argyros does not teach claim 8. See if the substrates used in their embodiments would be beneficial for amylase enzymes
Regarding claims 9 and 10, Argyrose teaches that the recombinant host cell is capable of higher consumption and growth on arabinose (a pentose sugar) compared to the same cell without the heterologous polynucleotide encoding a sugar transporter (Argyrose, [206]; fig. 7).
Regarding claim 11, Argyros teaches that the recombinant host cell is capable of producing higher ethanol titers compared to the same cell without the heterologous polynucleotide encoding a sugar transporter (Argyros, [82], [206]; fig. 7).
Regarding claim 12, Argyros teaches that the recombinant host cell comprises a heterologous polynucleotide encoding a transketolase and transaldolase (Argyros, claim 13).
Regarding claims 14 and 22, Argyros teaches that the recombinant host cell is an S. cerevisiae cell (Argyros, claim 12).
Regarding claim 15, Argyros teaches a composition comprising the recombinant host cell and one or more naturally and/or non-naturally occurring components such as gums (i.e., YMA, which is a form of medium containing agar gel) (Argyros, [201]).
Regarding claim 23, Argyros teaches that the heterologous polynucleotide encoding a sugar transporter is operably linked to a foreign promoter (i.e., exogenous, or surrogate promoter) (Argyros, [41]).
Regarding claims 1, and 25-27, Argyros does not explicitly disclose the amino acid sequence of the mature sugar transporter. However, Argyros teaches the recombinant eukaryotic host cell comprising a AraT sugar transporter (Argyros, claim 1). Argyros teaches the AraT sugar transporter is derived from Aspergillus clavatus (ACLA_044740) (Argyros, [51]).
A sequence search of SEQ ID NO: 387 provided the following result from Uniprot:
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640
952
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67
912
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It would have been obvious at the time of filing for one of ordinary skill in the art to use the above sugar transport amino acid sequence taught by Uniprot as an embodiment in order to practice the invention taught by Argyros. The teachings of Argyros differ from the claimed invention in that Argyros does not disclose the amino acid sequence of the sugar transporter. Argyros teaches that Aspergillus clavatus (ACLA_044740) is an AraT sugar transporter. Uniprot teaches that the above sequence was derived from Aspergillus clavatus open reading frame ACLA_044740. One of ordinary skill in the art could have used as an embodiment the AraT transporter for the sugar transporter with the above amino acid sequence taught by Uniprot, and the results of said embodiment would have been predictable. Therefore, it would have been obvious to one of ordinary skill in the art to make the above substitution to arrive at the invention of claims 1-7, 9-12, 14-15, 22-23 and 25-27.
(new rejection) Claims 1-12, 14-15 and 22-27 are rejected under 35 U.S.C. 103 as being unpatentable over Argyros, US 20170191088 A1 and Uniprot ID A1C8W7_ASPCL as applied to claims 1-7, 9-12, 14-15, 22-23, and 25-27 above, and further in view of Purkan (cited above).
Regarding claims 8 and 24, Argyros does not teach that the S. cerevisiae host cell comprises a heterologous polynucleotide encoding a glucoamylase, alpha-amylase, phospholipase, trehalase, protease, or pullulanase.
Purkan teaches an S. cerevisiae cell that comprises a heterologous polynucleotide encoding a glucoamylase (Purkan, pg. 4, [2]).
It would have been obvious to one of ordinary skill in the art to modify the recombinant host cell taught by Argyros, with the heterologous polynucleotide encoding a glucoamylase taught by Purkan. One would be motivated to combine these teachings because the S. cerevisiae host cell taught by Argyros is intended for use in ethanol production via fermentation of starches (Argyros, [18-24]). However, Argyros teaches the use of external enzymes for the saccharification of starches (Argyros, [76]). The use of an external enzyme is necessary because S. cerevisiae do not produce these enzymes naturally (Purkan, pg. 2, [3]). Modifying an S. cerevisiae host cell to express a heterologous glucoamylase gene allows S. cerevisiae to ferment starch and produce ethanol without the use of an external enzyme (Purkan, pg. 7). Therefore, combining the teachings of Argyros and Purkan may result in a simplified process that includes a simultaneous saccharification/fermentation process without the use of an external enzyme (Argyros, [76]). Furthermore, starch containing biomass is relatively inexpensive, and it would therefore be beneficial to use as a substrate for ethanol production (Purkans, abstract). A person having ordinary skill in the art would have a reasonable expectation of success in combining the above teachings of Argyros and Purkan. The host cell taught by Argyros is an S. cerevisiae cell, and the cell modified to express glucoamylase taught by Purkan is also an S. cerevisiae cell (Purkan, pg. 2, [3]). Additionally, Purkans demonstrates that an S. cerevisiae cell modified with a heterologous glucoamylase encoding polypeptide can successfully convert starch into ethanol (Purkans, pg. 7, [1]). Therefore, it would have been obvious to combine the above teachings of Argyros and Purkans. Accordingly, claims 1-12, 14-15 and 22-27 are rejected.
(new rejection) Claims 1-7, 9-15, 22-23, and 25-27 are rejected under 35 U.S.C. 103 as being unpatentable over Argyros, US 20170191088 A1 and Uniprot ID A1C8W7_ASPCL as applied to claims 1-7, 9-12, 14-15, 22-23, and 25-27 above, and further in view of Guadalupe-Medina (cited above).
Regarding claim 13, Argyros does not teach that the recombinant host cell of claim 1 further comprises a disruption to an endogenous gene encoding a glycerol-3-phosphate dehydrogenase (GPD) and/or a disruption to an endogenous gene encoding a glycerol-3-phosphatase (GPP).
Guadalupe-Medina teach an S. cerevisiae cell that comprises a deletion of an endogenous GPD (Guadalupe-Medina, pg. 6, left column).
It would have been obvious to combine the host cell as taught by Argyros and applied to claim 1 with the GPD deletion taught by Guadalupe-Medina. One would be motivated to combine the above teachings because the deletion of GPD offers improved ethanol yield. Guadalupe-Medina teaches that an S. cerevisiae cell comprising a deleted GPD converted sugar into ethanol at increased yields relative to the control strain (Guadalupe-Medina, pg. 6, left column). Additionally, Guadalupe-Medina suggests that GPD deletion S. cerevisiae strain produces less acetic acid, which may be particularly beneficial during simultaneous saccharification and fermentation processes, which is the same process the host cell taught by Argyros is intended to be used for (Argyros, [76]). Argyros also suggests that particular endogenous genes or polynucleotides may be deleted (Argyros, [61-62]). Furthermore, one would have a reasonable expectation of success combining the above teachings of Argyros and Guadalupe-Medina. Both Argyros and Guadalupe-Medina teach an S. cerevisiae strain that can ferment sugars in order to produce ethanol. Additionally, bioethanol production using S. cerevisiae is well known in the art (Guadalupe-Medina, pg. 1, right column), and the skilled artisan would be able to use known techniques to modify the cell taught by Argyros by deleting the GPD gene as taught by Guadalupe-Medina (Guadalupe-Medina, pg. 7, left column). Therefore, it would have been obvious to combine the above teachings of Argyros and Guadalupe-Medina. Accordingly, claims 1-7, 9-15, 22-23, and 25-27 are rejected.
Response to Arguments
Applicants arguments in the remarks filed 05/20/2025 are acknowledged. However, these arguments are moot in view of the new rejections shown above.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to BENJAMIN HALL EASTON whose telephone number is (703)756-5851. The examiner can normally be reached 10:30AM - 6:30PM EST.
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/BENJAMIN HALL EASTON/Examiner, Art Unit 1652
/ROBERT B MONDESI/Supervisory Patent Examiner, Art Unit 1652
1 A1C8W7_ASPCL. UniProt. (2007, January 23). https://www.uniprot.org/uniprotkb/A1C8W7/entry
2 P. Purkan, A. Baktir, N. N. T. Puspaningsih, M. Ni’mah; Direct conversion of starch to ethanol using recombınant Saccharomyces cerevisiae containing glucoamylase gene. AIP Conf. Proc. 21 September 2017; 1888 (1): 020041. https://doi.org/10.1063/1.5004318
3 Guadalupe-Medina, V., Metz, B., Oud, B., van Der Graaf, C.M., Mans, R., Pronk, J.T. and van Maris, A.J.A. (2014), Laboratory evolution of osmotolerant Gpd– yeast. Microbial Biotechnology, 7: 44-53. https://doi.org/10.1111/1751-7915.12080