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 response to restriction letter of 1/17/26 is acknowledged. Applicant elected Group III, claims 9-15 and Group C (namely SEQ ID NO:3) with traverse.
Applicant further elected species (a) and explains that he/she has submitted a preliminary amendment to introduce dependent claims 16-19 and hence, said claims should be examined together with the elected invention.
He/she further traverses the species election requirement and mentions that the species are referred to as compositions of Groups IA, Group IB, Group IC in the last office action but it is unclear what the groups are referring to in the context of the office action.
With respect to rejoinder of claims 16-19, said claims are hereby rejoined with the elected invention.
Regarding applicant’ confusion with respect to species election, it should be noted that said species election requirement was directed only to composition claims 2-8 and original claims 16-19 (see the previous office action) and the method claims 9-15 were excluded from species election requirement. Also, the idea behind species election requirement is based on the language of claim 7, which refers to a one or more enzyme of “psicose production pathway”, “mannitol production pathway”, “tagatose production pathway” etc.
Since each of said pathways are made of many enzymes and each pathway has different enzymes, it deemed necessary to require species election.
Finally, applicant can always leave a telephonic message for the examiner if she happens to be unavailable when applicant calls. She usually responds to phone messages within 24 hours.
DETAILED ACTION
Claims 9-19 are under examination on the merits. Claims 1-8 remain withdrawn as drawn to non-elected invention.
Specification
The disclosure is objected to for reciting hyperlink language (see for example page 15, line 17). Applicant is advised to delete hyperlink language everywhere in the disclosure, in compliance with 37 CFR section 1/57(d).
Claim Rejections - 35 USC § 112
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.
Claim 10 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. In claim 10, it is unknown what “product” is referred to.
Claim 15 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. Dependent claim 15 is totally confusing because in its base claim 14, sucrose is a substrate but in claim 15, the “sugar produced” is also “sucrose”. Appropriate clarification is required.
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.
Claim(s) 9-13, 16-17 are rejected under 35 U.S.C. 103 as being unpatentable over Godl et al., “Godl” (US2009/0318372, 12/2009) further in view of Weinstock et al., “Weinstock” (UniProt Database, accession No.U1STY0, 11/2013).
Godl in its claim 17 recites the following:
A method of producing a mixture containing α-D-glucosylglycerol and fructose comprising the steps: providing a sucrose phosphorylase (EC 2.4.1.7); incubating said sucrose phosphorylase (SPase) with a mixture comprising sucrose and glycerol as glucosyl acceptor; and isolating and/or purifying the α-D-glucosylglycerol and fructose mixture.
In [0027], according to said publication, the SPase is preferably recombinantly produced as a full-length protein or a catalytically active fragment thereof or a fusion protein. However, it is of course also possible to use SPase directly from the organism which naturally produces said SPase. Methods for the recombinant production of SPase are known to the person skilled in the art (e.g. Sambrook J. et al. Molecular cloning: a laboratory manual. ISBN 0-87969-309-6).
In [0032], Godl teaches that SPase may be employed in the incubation step as either a cell-free enzyme, which may but need not be partially purified, a whole-cell system pre-treated physically or chemically for improved permeability of the cell membrane (permeabilization) and mechanical stability (wherein such cell will be free of buffers and allows for sucrose and glycerol to pass through its membrane), encapsulated catalyst in which said free enzyme or whole-cell system are entrapped, preferably in gel-like structures, or immobilized on a carrier.
In [0079], Godl recites that recombinant SPase may be produced in E.coli.
Said reference does refer to some exemplary sources of said sucrose phosphorylase but fails to mention utilizing instant SEQ ID NO:3 or 80% or higher homologs thereof.
Weinstock teaches about a recombinant sucrose phosphorylase from Alloscardovia omnicolens, having 94.2% identity to instant SEQ IOD NO:3.
Before the effective filing of this application, it would have been obvious to one of ordinary skill in the art to start with the method of Godl and substitute its sucrose phosphorylase(s) with that of Weinstock’s.
One of ordinary skill in the art is motivated to substitute the sucrose phosphorylase(s) of Godl with that of Weinstock’s because the prior art teaches that said enzyme is commercially available, highly efficient in catalysis and its structure is fully known ( at 2.6 Aº resolution) so that one of ordinary skill can improve its thermal stability and even its catalytic efficiency by site directed mutagenesis, thereby improving yields of highly pure fructose, rendering this invention obvious.
One of ordinary skill in the art has a reasonable expectation of success in substituting the sucrose phosphorylase of Godl with the one from Weinstock’s because such procedures were routine in the prior art before the effective filing of this application.
Claim(s) 14-15, 18-19 are rejected under 35 U.S.C. 103 as being unpatentable over Sun et al., “Sun” (US2021/0254031, 8/2021) further in view of Weinstock (cited above).
Sun claims a method of producing allulose (psicose) as following:
Claim 9. A method for producing allulose, comprising fermenting single or combined glucose, fructose, sucrose, or using Allulose1, Allulose2, Allulose3, Allulose4, Allulose5, or fermenting single or combined glucose, fructose, sucrose, or glycerol using Allulose6, wherein Allulose1, Allulose2, Allulose3, Allulose4, Allulose5, or Allulose6 are constructed by the method of claim 5, wherein said claim recites the following:
Claim 5. A method for construction of a recombinant Corynebacterium glutamicum strain for producing allulose, comprising at least one of the following steps: (1) amplifying the allulose 6-phosphate 3-epimerase (P6PE) gene and the allulose 6-phosphate phosphatase (P6PP) gene derived from Escherichia coli and constructing them into the expression vector pEC-XK99E to obtain a recombinant expression vector pEC-P6PE-P6PP, and converting the recombinant expression vector pEC-P6PE-P6PP into wild-type Corynebacterium glutamicum ATCC13032 to obtain a recombinant strain Allulose1;
(2) using Corynebacterium glutamicum ATCC13032 as the starting strain, reducing the expression level of fructose 6-phosphate kinase gene to obtain a recombinant strain Allulose2;
(3) constructing the recombinant expression vector pEC-P6PE-P6PP bearing the allulose 6-phosphate 3-epimerase and allulose 6-phosphate phosphatase genes into the recombinant strain Allulose2 to obtain a recombinant strain Allulose3;
(4) amplifying the glucokinase gene and glucose 6-phosphate isomerase gene derived from Corynebacterium glutamicum and constructing them into the expression vector pXMJ19 to obtain a recombinant plasmid pXMJ19-GlK-PGI, converting the recombinant plasmid pXMJ19-GlK-PGI into the recombinant strain Allulose3 to obtain a recombinant strain Allulose4;
(5) amplifying the fructose permease gene from Zymomonas mobilis and the fructokinase gene derived from Escherichia coli or Enterococcus faecalis, and constructing them into the expression vector pEC-P6PE-P6PP to obtain a recombinant vector pEC-P6PE-P6PP-FK-GLF, constructing the recombinant plasmid pEC-P6PE-P6PP-FK-GLF and the optional pXMJ19-GLK-PGI into the recombinant strain Alluose2 to obtain a recombinant strain Alluose5;
(6) amplifying the glycerol permease gene derived from Escherichia coli, the glycerol dehydrogenase gene from Klebsiella pneumoniae, and the dihydroxyacetone kinase gene from Citrobacter freundii, and constructing them into the recombinant plasmid pXMJ19-GlK-PGI to obtain a recombinant plasmid pXMJ19-GlK-PGI-GlpF-DhaD-DhaK, converting the recombinant plasmid pXMJ19-GlK-PGI-GlpF-DhaD-DhaK and pEC-P6PE-P6PP-FK-GlF at the same time into the recombinant strain Allulose2 to obtain a recombinant strain Allulose 6.
In [0177], according to Sun, to establish an extracellular multienzyme system for converting sucrose into allulose. The key enzymes include: (1) sucrose phosphorylase (EC: 2.4.1.7), which catalyzes the conversion of sucrose to glucose 1-phosphate and fructose, etc.
Said reference however, does not mention utilizing instant SEQ ID NO:3 or 80% or higher homologs thereof.
Weinstock teaches about a recombinant sucrose phosphorylase from Alloscardovia omnicolens, having 94.2% identity to instant SEQ IOD NO:3.
Before the effective filing of this invention, it would have been obvious to one of ordinary skill in the art to start with the allulose production method of Sun and prepare its fructose substrate utilizing Weinstock’s enzyme.
One of ordinary skill in the art is motivated in preparing fructose substrate of Sun to be used in its allulose preparation method, utilizing the enzyme of Weinstock , because as mentioned above, said SPase enzyme is commercially available, is highly efficient in catalysis and its structure is fully known ( at 2.6 Aº resolution) so that one of ordinary skill can improve its thermal stability and even its catalytic efficiency by site directed mutagenesis, thereby improving yields of highly pure fructose, and thereby allulose, rendering this invention obvious.
Finally, one of ordinary skill in the art has a reasonable expectation of success in preparing fructose substrate of Sun to be used in Sun’s allulose preparation method, utilizing the enzyme of Weinstock because such procedures were routine in the prior art before the effective filing of this application.
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARYAM MONSHIPOURI whose telephone number is (571)272-0932. The examiner can normally be reached full-flex.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melenie L Gordon can be reached at 571-272-8037. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/MARYAM MONSHIPOURI/Primary Examiner, Art Unit 1651