DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s amendment, reply and IDS filed October 15, 2025 have been received and entered into the record. Claims 1 – 6 are pending; claims 2 and 4 – 6 are withdrawn; claims 1 and 3 have been considered on the merits. All arguments have been fully considered.
Election/Restrictions
Applicant's election with traverse of group I, claims 1 and 3 in the reply filed on July 24, 2025 is maintained.
Applicant requests newly amended claim 4 to be examined with the elected group. Specifically, applicant argues that amended claim 4 now requires the product of claim 1 and therefore shares the same and unspecified special technical feature as the elected invention.
Initially, the election requirement was deemed proper and made final in the previous office action. Notwithstanding, even if the amended claim of group III newly shares the newly recited technical feature of a recombinant enzyme having a particular sequence expressed in a host system, claim 4 (group III) still falls outside the categories of invention permitted as it is drawn to a second use of the product. Note that elected group I includes a product and a method of using the product (paragraph 10.12, 10.15 of PCT International Search and Preliminary Examination Guidelines). Further, regarding the newly recited technical feature of a recombinant enzyme with a particular sequence expressed in a host system, the enzyme sequence, it’s function and expression in a host is known in the prior art as evidenced by the rejections made previously and below. In this regard, the groups to not share a special technical feature that makes a contribution over the prior art. Moreover, the groups continue to lack unity of invention.
The requirement is still deemed proper and is therefore made FINAL.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on October 15, 2025 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(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.
Claims 1 and 3 are rejected under 35 U.S.C. 102a1 as being anticipated by UNIPROT Deposit R7ZW08_9BACT (deposited 07.24.2013).
Regarding claim 1, UNIPROT teaches an isolated enzyme preparation comprising N-acylglucosamine 2-epimerase that matches 100% to applicant’s SEQ ID NO: 1 and 3 (per search results previously provided). The enzyme is obtained from the same microbial source as applicant (Lunatimonas lonarensis, Figures, 0028). Although the reference does not indicate the enzyme is for catalyzing an epimerization reaction of a saccharide, the enzymes are the same as evidenced by the 100% sequence match. Therefore, the enzyme of the prior art must also exhibit the same functions as that claimed. Moreover, the intended use of the claimed composition does not patentably distinguish the composition, per se, since such undisclosed use is inherent in the reference composition. In order to be limiting, the intended use must create a structural difference between the claimed composition and the composition of the prior art. In the instant case, the intended use fails to create a structural difference, thus, the intended use is not limiting. Please note that when applicant claims a composition in terms of function, and the composition of the prior art appears to be the same, the Examiner may make rejections under both 35 U.S.C 102 and 103 (MPEP 2112).
In addition, although the reference does not teach the enzyme is obtained by expression in a heterologous host system, this limitation is interpreted as a product by process type limitation. The patentability of a product does not depend on its method of production. If the claimed product is the same or obvious from a product in the prior art (i.e. the product disclosed in the cited reference), then the claim is unpatentable even though the reference product was made by a different process. When the prior art discloses a product which reasonably appears to be identical with or slightly different than the claimed product-by-process, rejections under 35 U.S.C 102 and/or 35 U.S.C 103 are proper (MPEP 2113).
Regarding claim 3, since N-acylglucosamine 2-epimerase is defined as an enzyme that catalyzes N-acyl-D-glucosamine (a saccharide) into N-acyl-D-mannosamine (epimerization reaction product), or produces epimerization reaction products of a saccharide by catalyzing an epimerization reaction of a saccharide substrate to obtain an epimerization reaction product thereof, the reference intrinsically teaches the claimed method by definition.
Therefore, the reference anticipates the claimed subject matter.
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.
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.
Claims 1 and 3 are rejected under 35 U.S.C. 103 as being unpatentable over UNIPROT Deposit R7ZW08_9BACT (deposited 07.24.2013) in view of Cui et al. (2018).
Regarding claim 1, UNIPROT teaches an isolated enzyme preparation comprising N-acylglucosamine 2-epimerase that matches 100% to applicant’s SEQ ID NO: 1 and 3 (per search results previously provided). The enzyme is obtained from the same microbial source as applicant (Lunatimonas lonarensis, Figures, 0028). Although the reference does not indicate the enzyme is for catalyzing an epimerization reaction of a saccharide, the enzymes are the same as evidenced by the 100% sequence match. Therefore, the enzyme of the prior art must also exhibit the same functions as that claimed. Moreover, the intended use of the claimed composition does not patentably distinguish the composition, per se, since such undisclosed use is inherent in the reference composition. In order to be limiting, the intended use must create a structural difference between the claimed composition and the composition of the prior art. In the instant case, the intended use fails to create a structural difference, thus, the intended use is not limiting. Please note that when applicant claims a composition in terms of function, and the composition of the prior art appears to be the same, the Examiner may make rejections under both 35 U.S.C 102 and 103 (MPEP 2112).
In addition, although the reference does not teach the enzyme is obtained by expression in a heterologous host system, this limitation is interpreted as a product by process type limitation. The patentability of a product does not depend on its method of production. If the claimed product is the same or obvious from a product in the prior art (i.e. the product disclosed in the cited reference), then the claim is unpatentable even though the reference product was made by a different process. When the prior art discloses a product which reasonably appears to be identical with or slightly different than the claimed product-by-process, rejections under 35 U.S.C 102 and/or 35 U.S.C 103 are proper (MPEP 2113).
Notwithstanding, at the time the claims were filed, the practice of expressing enzymes in heterologous host systems was well known in the art. In support, Cui teaches methods of protein expression in Bacillus subtilis (also used by applicant, p.7) are well known due to its heterologous overproduction of recombinant enzymes which can be practiced on large scale and provides a universal platform to produce high value enzymes (abstract, p.145 left col.). Specifically, Cui teaches B. subtilis are superior due to this ability, its ease of genetic manipulation and genetically well characterized system (p.145, left col.). As such, at the time the claims were filed, one of ordinary skill in the art would have been motivated by routine practice, as evidenced by Cui, to express and obtain a desired enzyme in a heterologous host system for the well known advantages of higher yield thereof and with a reasonable expectation for successfully obtaining a recombinant enzyme preparation.
Regarding claim 3, since N-acylglucosamine 2-epimerase is defined as an enzyme that catalyzes N-acyl-D-glucosamine (a saccharide) into N-acyl-D-mannosamine (epimerization reaction product), or produces epimerization reaction products of a saccharide by catalyzing an epimerization reaction of a saccharide substrate to obtain an epimerization reaction product thereof, the reference intrinsically teaches the claimed method by definition.
Thus, the invention as a whole is prima facie obvious over the references, especially in the absence of evidence to the contrary.
Response to Arguments
Applicant argues that the enzyme of the prior art is found in a natural microorganism, is not recombinant and is not expressed in a heterologous host system; that the claimed recombinant enzyme exhibits unexpected, unpredictable properties and advantages over the prior to include reduced byproduct formation (fructose) by contaminating enzymes since a recombinant enzyme is purer; and increased reaction speed due to high yield of the enzyme, higher enzyme titer and faster reaction rates. Applicant further argues that while the UNIPROT deposit discloses N-acylglucoseamine-2-epimerase, the reference fails to teach the enzyme acts on unmodified glucose, mannose, talose or galactose; that applicant newly discovered that the enzyme can unexpectedly catalyze epimerization of the various hexoses; and that the claimed enzyme exhibits advantages over other catalytic enzymes from Melioribacter roseus such as faster reaction time (reply, page 7).
Regarding the argument that the enzyme of the prior art is found in nature while the claimed enzyme is recombinant, it is iterated that since the enzymes are obtained from the same source and have the same sequence, they are interpreted as the same enzyme. Despite the recitation of “recombinant,” the sequence is not modified in any way compared to the natural enzyme. Moreover, the claimed enzyme preparation does not require any changes to the enzyme and does not require any other components in the preparation (e.g., a host cell, per se). It is iterated that the limitations requiring the enzyme to be expressed in a heterologous host system are interpreted as a process by which to obtain the enzyme that does not appear to change or modify the enzyme in any way, as evidenced by its 100% match to the sequence of the prior art.
Regarding applicant’s assertion of unexpected results, applicant has failed to provide any objective evidence of any unexpected or superior results, but has only provided attorney arguments. Arguments presented by applicant cannot take the place of evidence in the record (MPEP 2145 I). Applicant has failed to provide a comparison between the claimed invention and that of the prior art. Further, it is unclear what composition is alleged to exhibit the unexpected results, e.g., the enzyme having SEQ ID NO:1 or 3, one that shares 90% identity thereto or one that is modified by “one or several” amino acid substitutions, insertions, deletions or additions. In this regard, the arguments do not appear commensurate in scope with the claimed invention. Still further, it is unclear if applicant asserts that the enzyme preparation itself exhibits the alleged unexpected results (e.g., the product) or if the manner of expression in a heterologous host system results in the alleged unexpected results (e.g., the process by which it is obtained). Please note that applicant has neither argued nor evidenced that the process of expressing the sequence in a heterologous host system and obtaining the enzyme therefrom imparts any structural or functional difference in the resulting enzyme.
Regarding the argued unexpected results of reduced byproducts as a result of a pure recombinant enzyme and increased reaction rates due to higher enzyme yields, it is initially reiterated that the enzyme preparations are the same as evidenced by the same enzyme being isolated and obtained from the same source with the same sequence. Thus, "Products of identical chemical composition can not have mutually exclusive properties" (MPEP 2112.01 II). In addition, as stated above, it was known in the art that recombinant enzymes obtained from heterologous host systems result in higher yields of enzyme. In this regard, the argued result is not unexpected but rather predicted by the prior art. Moreover, the argued purity, yield and reaction rates are not limitations recited in the claims. As such, the arguments are not commensurate in scope with the claimed invention.
Regarding the argument that UNIPROT does not teach the enzyme acts on unmodified glucose, mannose, talose or galactose, it is iterated that the enzymes are the same as evidenced by their name, source and sequence match. In this regard, it is maintained that the enzyme preparation of the prior art must also inherently act on the claimed substrates. "[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer." Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable (MPEP 2112 I).
Regarding the argument that the claimed enzyme exhibits advantages over other catalytic enzymes from Melioribacter roseus, it is noted that the comparison is not commensurate in scope with the claimed subject matter. While cellobiose 2-epimerase (CE) is an epimerase, the enzyme is classified as EC 5.1.3.11 while the claimed N-acylglucoseamine-2-epimerase is classified as EC 5.1.3.8. The enzymes have different substrates (cellobiose and N-acyl-D-glucosamine, respectively), different reaction products (D-glucosyl-D-mannose and N-acyl-D-mannosamine respectively), and are two among thousands of “catalytic enzymes” and 25 different classifications of epimerases that act on carbohydrates. Moreover, the argued unexpected advantages of the claimed enzyme have not been objectively substantiated.
Thus, the invention as a whole is prima facie obvious over the references, especially in the absence of evidence to the contrary.
No claims are allowed.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to RUTH A DAVIS whose telephone number is (571)272-0915. The examiner can normally be reached Monday - Friday (8am - 4pm).
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Fereydoun Sajjadi can be reached at 571-272-3311. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/RUTH A DAVIS/Primary Examiner, Art Unit 1699