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 .
Withdrawal of Rejections
The response and amendments filed on 01/22/2026 are acknowledged. Any previously applied minor objections and/or minor rejections (i.e., formal matters), not explicitly restated here for brevity, have been withdrawn necessitated by Applicant’s formality correction and/or amendments. For the purposes of clarity of the record, the reasons for the Examiner’s withdrawal, and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner’s Response to Arguments section.
Briefly, the previous claim rejections under 35 U.S.C. 112(b) for indefiniteness have been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection have been set forth below. The previous claim rejections under 35 U.S.C. 103 for obviousness have been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection have been set forth below.
The following rejections and/or objections are either reiterated or newly applied. They constitute the complete set presently being applied to the instant application.
Claim Objections
Claim 1 is objected to because of the following informalities: the abbreviation “PEI” should be completely spelled out upon first recitation. Appropriate correction is required. This is an objection, not a rejection, because PEI is spelled out in the instant specification to be “polyethyleneimine” (see, e.g., instant specification, pg. 4, line 4).
Claim 2 is objected to because of the following informalities: “or from” that is recited between the bacterial species should not be italicized. Appropriate correction is required. This is an objection, not a rejection, because this appears to be a typographical error.
Claim 2 is objected to because of the following informalities: “Rhodococcus sp. Phi1” should be spelled “Rhodococcus sp. Phil”. Appropriate correction is required. This is an objection, not a rejection, because this appears to be a typographical error.
Claim 3 is objected to because of the following informalities: “Lactate dehydrogenase” should be “lactate dehydrogenase”. Appropriate correction is required. This is an objection, not a rejection, because this appears to be a typographical error.
New Grounds of Rejection Necessitated by Amendments
Claim Rejections - 35 USC § 112(b), Indefiniteness
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-3 are rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites the limitation "the coenzyme ammonium formate dehydrogenase". There is insufficient antecedent basis for this limitation in the claim. No ammonium formate dehydrogenase was previously recited.
Claim 1 recites “wherein when a sum of masses of the main enzyme and the coenzyme is marked as N1, and the mass of the amino resin carrier is marked as N2, then the ratio of N1: N2 is 80[[50]]-200 mg: 1 g”; however, it is unclear if the coenzyme to be included in this sum is the lactate dehydrogenase, or the formate dehydrogenase, or both. For the purposes of applying prior art, the Examiner has interpreted the coenzyme to be both lactate dehydrogenase and formate dehydrogenase.
Claims 2-3 are included in this rejection for depending on independent claim 1 and failing to rectify the noted deficiencies.
Examiner’s Response to Arguments
Regarding Applicant’s arguments regarding the previous 35 U.S.C. 112(b) rejection (remarks, page 8), as discussed above, the previous claim rejections under 35 U.S.C. 112(b) have been withdrawn; however, new grounds of rejection have been set forth above.
New Grounds of Rejection Necessitated by Amendments
Claim Rejections - 35 USC § 103, Obviousness
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claim 1 is rejected under 35 U.S.C. 103 as being unpatentable over Liu (CN 109777813; Date of Publication: May 21, 2019 – previously cited) in view Jackson (Enhanced stability of L-lactate dehydrogenase through immobilization engineering; 2016 – newly cited), Bolivar (Coating of Soluble and Immobilized Enzymes with Ionic Polymers: Full Stabilization of the Quaternary Structure of Multimeric Enzymes; 2009 – newly cited), Hu (CN 110241107; Date of Publication: September 17, 2019 – previously cited), and of Truppo (US 2014/0106413; Date of Publication: April 17, 2014 – newly cited).
Liu’s general disclosure relates to “a method for covalently immobilizing a transaminase-PLP co-immobilized enzyme with a transaminase and a coenzyme pyridoxal (PLP) with an epoxy resin as a carrier, and the co-immobilized transaminase” (see, e.g., Liu, “Invention content”, pg. 2). Moreover, Liu discloses the “transaminase-PLP co-immobilization” for high-efficiency preparation of the co-immobilized transaminase and the coenzyme, and wherein the obtained co-immobilized transaminase has a high recovery rate, good stability, strong tolerance to organic solvents, and low cost (see, e.g., Liu, “Invention content”, pg. 2).
Regarding claim 1 pertaining to the co-immobilized enzymes, Liu teaches a main enzyme (transaminase) and a coenzyme (PLP) (see, e.g., Liu, “Invention content”, pg. 2). Liu teaches covalently immobilizing transaminase on an amino resin carrier that is activated by glutaraldehyde (see, e.g., Liu, “Invention Content”, pg. 2; “Amino Resin Pretreatment” & “Carrier Activation”, pg. 4).
However, Liu does not teach: when the number of the coenzyme is two, one coenzyme is covalently immobilized on the amino resin carrier and the other coenzyme is non-covalently immobilized on the amino resin carrier by PEI ionic interaction (claim 1); or wherein the coenzyme is selected from any one of the combinations: 1) lactate dehydrogenase (LDH) and formate dehydrogenase (FDH); or 2) lactate dehydrogenase and glucose dehydrogenase (GDH), and the LDH is covalently immobilized on the amino resin carrier and the FDH or the GDH is non-covalently immobilized on the amino resin carrier by PEI ionic interaction (claim 1); or wherein the FDH and GDH are sensitive to glutaraldehyde (claim 1); or wherein the amino resin carrier is an amino resin carrier active by glutaraldehyde and the amino resin carrier is with a C2 or C4 linker arm (claim 1); or wherein the mass ratio of the coenzyme lactate dehydrogenase thereof is 5-7:1 (claim 1); or wherein the mass ratio of the transaminase to the coenzyme glucose dehydrogenase thereof if 5-7:1-2 (claim 1); or wherein the sum of the masses of the main enzyme and the coenzyme is marked as N1, and the mass of the amino resin carrier is marked as N2; then the ratio of N1:N2 is 80-200 mg:1g (claim 1).
Jackson’s general disclosure relates to “immobilization of LDH from rabbit muscle in glyoxyl-agarose to have an active and stable preparation which is able to synthesize l-lactic acid. Optimization of various parameters during immobilization allowed the preparation of an active and highly stable immobilized derivative of LDH” (see, e.g., Jackson, abstract). Moreover, Jackson discloses “fine tuning of the immobilization by controlling different parameters such as temperature, immobilization time, and presence of additives to achieve maximum activity and stability, furthermore, the evaluation of its operational stability in the conversion of pyruvate to l-lactic acid” (see, e.g., Jackson, Introduction, pg. 1249).
Regarding claim 1 pertaining to co-immobilization of the co-enzymes, Jackson teaches co-immobilization of LDH and FDH (see, e.g., Jackson, section 2.5). Moreover, Jackson teaches covalent immobilization of LDH to the carrier (see, e.g., Jackson, introduction). Jackson teaches immobilization of 0.15 mg of LDH and 0.2 mg of FDH (see, e.g., Jackson, Section 2.5). Jackson teaches “Co-immobilization of LDH and formate dehydrogenase (FDH) was performed by adding 1 g of support to a 10 mL solution of FDH (0.2 mg of soluble FDH in 0.1 M sodium bicarbonate pH 10.0) at 4 °C for 1.5 h followed by 45 min at 24 °C. The solution was filtered and 10 mL of a solution of LDH was added (0.15 mg of soluble LDH with 300 mM of trehalose in 0.1 M sodium bicarbonate pH 10.0) for 15 min at 24 °C” (see, e.g., Jackson, section 2.5).
Bolivar’s general disclosure relates to “a simple and effective way to avoid the dissociation of multimeric enzymes by coating their surface with a large cationic polymer (e.g., polyethylenimine (PEI)) by ionic exchange. As model enzymes, glutamate dehydrogenase (GDH) from Thermus thermophilus and formate dehydrogenase (FDH) from Pseudomonas sp. were used. Both enzymes are very unstable at acidic pH values due to the rapid dissociation of their subunits (half-life of diluted preparations is few minutes at pH 4 and 25 °C). GDH and FDH were incubated in the presence of PEI yielding an enzyme-PEI composite with full activity. To stabilize the enzyme-polymer composite, a treatment with glutaraldehyde was required. These enzyme-PEI composites can be crosslinked with glutaraldehyde by immobilizing previously the composite onto a weak cationic exchanger. The soluble GDH-PEI composite was much more stable than unmodified GDH at pH 4 and 30 °C (retaining over 90% activity after 24 h incubation) with no effect of the GDH concentration in the inactivation course. The composite could be very strongly, but reversibly, adsorbed on cationic exchangers. Similarly, FDH could be treated with PEI and glutaraldehyde after adsorption on cationic exchangers, This permitted a stabilized FDH preparation. In this way, the coating of the enzymes surfaces with PEI is used as a simple and efficient strategy to prevent enzyme dissociation of multimeric enzymes. These composites can be used as a soluble catalyst or reversibly immobilized onto a cationic exchanger (e.g., CM-agarose)” (see, e.g., Bolivar, abstract).
Regarding claim 1 pertaining to non-covalent immobilization of FDH, Bolivar teaches non-covalent immobilization of FDH onto cationic exchangers by coating the surface of FDH with PEI in order to avoid dissociation of the multimeric enzyme (see, e.g., Bolivar, abstract). Additionally, Bolivar teaches that glutaraldehyde was used to cross-link the PEI-GDH composition in order to increase stability of the enzyme (see, e.g., Bolivar, results); therefore, one of ordinary skill in the art would understand that GDH is sensitive to glutaraldehyde because treatment of GDH with glutaraldehyde increases stability of the enzyme.
Hu’s general disclosure relates to “a method for immobilizing lipase by using amino resin”, wherein “the lipase is immobilized by the amino carrier covalent bonding method, and the amino carrier is activated by a cross-linking agent to obtain an amino carrier with an epoxy group at the end, and the amino group on the surface of the lipase reacts with the epoxy group at the tail of the amino carrier to form Stable covalent bond, so as to achieve the purpose of immobilization” (see, e.g., Hu, English translation, abstract).
Regarding claim 1 pertaining to the C2 linker arm, Hu teaches the amino resin carrier LC-1000EA, which has a C2 linker arm length (see, e.g., Hu, English translation, “Contents of the Invention”, pg. 3).
Regarding claim 1 pertaining to the mass of the amino resin carrier, Hu teaches that the mass of the activated resin carrier is 0.5-1.25g (see, e.g., Hu, English translation, “Contents of the Invention”, pg. 3). This mass taught by Hu overlaps with the claimed amino resin carrier mass of 1 g (see, e.g., MPEP 2144.05(I)).
Truppo’s general disclosure relates to “immobilized transaminases comprising a recombinant transaminase physically attached to a resin by ether hydrophobic interactions or covalent bonds. The immobilized transaminases described herein include recombinant transaminases that are capable of converting 4-oxo-4-[3-(trifluoromethyl)-5,6-dihydro[1,2,4]triazolo[4,3-a]pyrazin-7(8- H)-yl]-1-(2,4,5-trifluorophenyl)butan-2-one to (2R)-4-oxo-4-[3-(trifluoromethyl)-5,6-dihydro[1,2,4]triazolo[4,3-a]pyrazi- n-7(8H)-yl]-1-(2,4,5-trifluorophenyl)butan-2-amine in the presence of an amino group donor to levels measurable by an analysis technique. In certain embodiments the immobilized transaminases described herein are used to make (2R)-4-oxo-4-[3-(trifluoromethyl)-5,6-dihydro[1,2,4]triazolo[4,3-a]pyrazi- n-7(8H)-yl]-1-(2,4,5-trifluorophenyl)butan-2-amine” (see, e.g., Truppo, [0007]).
Regarding claim 1 pertaining to the mass ratio of transaminase, Truppo teaches “A 25 g/L solution of SEQ ID NO: 110 in 100 mM potassium phosphate buffer (pH 7.5) with 1 g/L PLP (pyrodoxial-5-phosphate) was made. 1 g of each resin was incubated with 5 mL of enzyme solution in a shaker overnight at room temperature” (see, e.g., Truppo, [0131]). One of ordinary skill in the art would be able to calculate that this comes out to 250 mg/mL of transaminase that is immobilized onto the resin.
It would have been first obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Liu’s co-immobilized transaminase and PLP enzymes, wherein PLP is substituted for LDH and FDH coenzymes, as taught by Jackson. One would have been motivated to do so because Jackson teaches that LDH and FDH can be co-immobilized in order to synthesize L-lactic acid (see, e.g., Jackson, section 2.12, pg. 1250). Moreover, Jackson teaches that immobilization of LDH can be fine-tuned by controlling for different parameters, such as temperature, immobilization time, and presence of additives to achieve maximum activity and stability (see, e.g., Jackson, Introduction, pg. 1249). Moreover, Liu teaches the preparation of a co-immobilized enzyme complex comprising transaminase as the main enzyme and PLP as the coenzyme, wherein the enzymes are covalently immobilized (see, e.g., Liu, “Invention content”, pg. 2). Therefore, based on the teachings of Liu and Jackson, it would have been obvious to co-immobilize transaminase with LDH and FDH because this would allow for the production of downstream products, such as L-lactic acid, and this allows for stabilization during the immobilization process. One would have expected success because Liu and Jackson both teach immobilization of enzymes.
It would have been secondly obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Liu’s immobilized covalently-immobilized transaminase, wherein another enzyme, FDH is non-covalently co-immobilized onto the resin, as taught by Bolivar. One would have been motivated to do so because Bolivar teaches FDH is “very unstable at acidic pH values due to the rapid dissociation of their subunits (half-life of diluted preparations is few minutes at pH 4 and 25 °C). GDH and FDH were incubated in the presence of PEI yielding an enzyme-PEI composite with full activity” (see, e.g., Bolivar, abstract). Furthermore, Bolivar teaches PEI is used as a simple and efficient strategy to prevent enzyme dissociation of multimeric enzymes (see, e.g., Bolivar, abstract). Moreover, Liu teaches that covalent immobilization results in high-efficiency, high recovery rate, good stability, strong tolerance to organic solvents, and low cost (see, e.g., Liu, “Invention Content”, pg. 2).Therefore, based on the teaching of Liu and Bolivar, it would have been obvious to combine covalent and non-covalent immobilization of enzymes since they both stabilize the enzymes for immobilization. One would have expected success because Liu and Bolivar both teach immobilization of enzymes.
It would have been thirdly obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce Liu’s co-immobilized enzyme, wherein the enzymes are immobilized using an amino resin carrier with a C2 linker arm, as taught by Hu. One would have been motivated to do so because Hu teaches that the amino resin carrier with the C2 linker arm showed good stability and catalytic performance (see, e.g., Hu, English translation, “Contents of the Invention”, pg. 3). Moreover, Liu teaches methods for producing co-immobilized transaminase and coenzymes, wherein Liu employs covalent immobilization technology because of the good stability of the co-immobilized transaminase (see, e.g., Liu, “Invention content”, pg. 3). Therefore, based on the teachings of Liu and Hu, it would have been obvious to co-immobilize enzymes using an activated amino resin carrier with a C2 linker arm because it would increase the stability of the co-immobilized transaminase and co-enzyme in addition to the increased stability provided by the covalent immobilization methods, as taught by Liu. One would have expected success because Liu and Hu teach immobilization methods.
Regarding claim 1 pertaining to the mass ratios, those working in the biological and/or pharmaceutical arts would understand that adjustments of particular working conditions, such as concentrations or amounts that pertain to ratios, is deemed a matter of judicious selection and routine optimization, which is within the purview of the skilled artisan. For example, the mass ratio of the transaminase to the lactate dehydrogenase would be 250mg, as taught by Truppo (see, e.g., Truppo, [0131]), to 0.15 mg, as taught by Jackson (see, e.g., Jackson, Section 2.5). The mass ratio of the transaminase to the formate dehydrogenase would be 250 mg, as taught by Truppo (see, e.g., Truppo, [0131]), to 0.2 mg, as taught by Jackson (see, e.g., Jackson, Section 2.5). The N1:N2 ratio would be 250.35mg to 1 g, wherein the N2 amino resin mass (1 g) is taught by Hu (see, e.g., Hu, English translation, “Contents of the Invention”, pg. 3). Furthermore, Hu teaches that there are many different parameters that influence immobilization and stabilization of enzymes on carriers, and that each physio-chemical tool to immobilize enzymes on solid surfaces needs to be adapted accordingly (see, e.g., Hu, Introduction, pg. 1249). Therefore, one of ordinary skill in the art would reasonably understand that the amount of the main enzyme (transaminase), co-enzymes (LDH and FDH), and amino resin carrier would influence immobilization of the enzymes. This is motivation for one of ordinary skill in the art to practice or test the parameter widely to find those that are functional or optimal which then would be inclusive or cover the steps as instantly claimed. Absent any teaching of criticality by the Applicant concerning amounts of the enzymes and resin, which pertains to the mass ratios, it would be prima facie obvious that one of ordinary skill in the art would recognize these limitations are result effective variables which can be met as a matter of routine optimization.
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Liu, Jackson, Bolivar, Hu, and Truppo as applied to claim 1 above, and further in view of Shin (Comparison of the ω-Transaminases from Different Microorganisms and Application of Production of Chiral Amines; 2001 – previously cited).
The teachings of Liu, Jackson, Bolivar, Hu, and Truppo, herein referred to as modified-Liu-Jackson-Bolivar-Hu-Truppo, are discussed above as it pertains to co-immobilization of enzymes.
However, modified-Liu-Jackson-Bolivar-Hu-Truppo does not teach: wherein the transaminase is derived from B. thuringiensis or Vibrio fluvialis strain JS17 (claim 2).
Shin’s general disclosure pertains to comparing the properties of three ω-Transaminases from different microorganisms, i.e., Klebsiella pneumoniae JS2F, B. thuringiensis JS64, and Vibrio fluvialis strain JS17 (see, e.g., Shin, Introduction, pg. 1782).
Regarding claim 2 pertaining to the transaminase, Shin teaches transaminases derived from B. thuringiensis JS64, and Vibrio fluvialis strain JS17 (see, e.g., Shin, Introduction, pg. 1782).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce modified-Liu-Jackson-Bolivar-Hu-Truppo’s co-immobilized enzyme with transaminase, wherein the transaminase is derived from B. thuringiensis JS64, and Vibrio fluvialis strain JS17, as taught by Shin. One would have been motived to do so because Shin teaches that the transaminases from B. thuringiensis JS64 and Vibrio fluvialis strain JS17 exhibit good transaminase activity, and the Vibrio fluvialis strain JS17 does not rely on nitrogen for induction of the enzyme (see, e.g., Shin, abstract). Moreover, modified-Liu-Jackson-Bolivar-Hu-Truppo teaches that the co-immobilized transaminase has a high recovery rate, good stability, strong tolerance to organic solvents, and low cost (see, e.g., Liu, “Invention content”, pg. 2). Therefore, based on the teachings of modified-Liu-Jackson-Bolivar-Hu-Truppo, it would have been obvious to co-immobilize a transaminase derived from B. thuringiensis or Vibrio fluvialis strain JS17. One would have expected success because modified-Liu-Jackson-Bolivar-Hu-Truppo and Shin both teach transaminase enzymes.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Liu, Jackson, Bolivar, Hu, and Truppo as applied to claim 1 above, and further in view of Bhowmik (Purification and partial characterization of D-(-)-lactate dehydrogenase from Lactobacillus helveticus CNRZ 32; 1993 – previously cited).
Bhowmik’s general disclosure relates to purification and characterization of D-lactate dehydrogenase derived from Lactobacillus helveticus (see, e.g., Bhowmik, abstract).
Regarding claim 3 pertaining to D-lactate dehydrogenase, Bhowmik teaches the D-lactate dehydrogenase derived from Lactobacillus helveticus (see, e.g., Bhowmik, abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention produce modified-Liu-Jackson-Bolivar-Hu-Truppo’s co-immobilized transaminase, lactate dehydrogenase, and formate dehydrogenase enzymes, wherein the lactate dehydrogenase coenzyme is derived from Lactobacillus helveticus, as taught by Bhowmik. One would have been motivated to do so because Bhowmik teaches that the lactate dehydrogenase derived from Lactobacillus helveticus has activity at low pH ranges and the enzyme’s activity is not inhibited by divalent metal cations like other lactate dehydrogenases derived from other Lactobacilli (see, e.g., Bhowmik, Discussion, pgs. 39-40). Moreover, modified-Liu-Jackson-Bolivar-Hu-Truppo teaches co-immobilization of transaminase with lactate dehydrogenase and formate dehydrogenase, wherein lactate dehydrogenase is covalently immobilized (see, e.g., Jackson, section 2.5). Therefore, based on the teachings of modified-Liu-Jackson-Bolivar-Hu-Truppo and Bhowmik, it would have been obvious to co-immobilize a lactate dehydrogenase enzyme derived from Lactobacillus helveticus. One would have expected success because modified-Liu-Jackson-Bolivar-Hu-Truppo and Bhowmik teach immobilization of lactate dehydrogenase.
Examiner’s Response to Arguments
Applicant's arguments filed 01/22/2026 have been fully considered but they are not persuasive.
Regarding Applicant’s arguments pertaining to the teachings of Virgen-Ortiz, Kim, Du, and Delgove (remarks, pages 12-16), these arguments are moot because, as previously discussed, the previous 35 U.S.C. 103 rejection has been withdrawn and new grounds of rejection have been set forth above. Virgen-Ortiz, Kim, Du, and Delgove were not relied upon for the 103 rejection above.
Regarding Applicant’s arguments pertaining to Liu not teaching co-immobilization of TA, LDH, and FDH (remarks, page 13), this argument is not persuasive because Liu was not relied upon in the 103 rejection above for immobilization of LDH and FDH. Instead, Jackson teaches co-immobilization of LDH and FDH (see, e.g., Jackson, section 2.5). Liu was relied upon to teach covalent immobilization of transaminase to an amino resin carrier (see, e.g., Liu, “Invention content”, pg. 2). One would have been motivated to do so because Jackson teaches that LDH and FDH can be co-immobilized in order to synthesize L-lactic acid (see, e.g., Jackson, section 2.12, pg. 1250). Moreover, Jackson teaches that immobilization of LDH can be fine-tuned by controlling for different parameters, such as temperature, immobilization time, and presence of additives to achieve maximum activity and stability (see, e.g., Jackson, Introduction, pg. 1249). Moreover, Liu teaches the preparation of a co-immobilized enzyme complex comprising transaminase as the main enzyme and PLP as the coenzyme, wherein the enzymes are covalently immobilized (see, e.g., Liu, “Invention content”, pg. 2). Therefore, based on the teachings of Liu and Jackson, it would have been obvious to co-immobilize transaminase with LDH and FDH because this would allow for the production of downstream products, such as L-lactic acid, and this allows for stabilization during the immobilization process.
Regarding Applicant’s arguments pertaining to Hu’s disclosure not teaching immobilization of transaminase (remarks, page 16), this argument is not persuasive because Hu was not relied upon to teach this limitation since Liu teaches covalent immobilization of transaminase. Instead, Hu was relied upon to teach the amino resin carrier LC-1000EA, which has a C2 linker arm length (see, e.g., Hu, English translation, “Contents of the Invention”, pg. 3). One would have been motivated to employ a C2 linker arm because Hu teaches that the amino resin carrier with the C2 linker arm showed good stability and catalytic performance (see, e.g., Hu, English translation, “Contents of the Invention”, pg. 3). Moreover, Liu teaches methods for producing co-immobilized transaminase and coenzymes, wherein Liu employs covalent immobilization technology because of the good stability of the co-immobilized transaminase (see, e.g., Liu, “Invention content”, pg. 3). Therefore, based on the teachings of Liu and Hu, it would have been obvious to co-immobilize enzymes using an activated amino resin carrier with a C2 linker arm because it would increase the stability of the co-immobilized transaminase and co-enzyme in addition to the increased stability provided by the covalent immobilization methods, as taught by Liu.
Regarding Applicant’s arguments pertaining to secondary considerations (remarks, pages 17-19), this argument is not persuasive because the results are not commensurate in scope with the claimed invention. More specifically, Applicant is relying on 1 g of co-immobilized TA and LDH being resuspended in 0.1 M PB (pH 7.0-7.5) and PEI solution (final concentration 2%), along with 20 mg of FDH. Followed by incubation at 20-25oC with shaking, filtration, and washing with 0.1 M PB (pH 7.5). Furthermore, Applicant is relying upon the following reactions: “5 mL of 0.1 M phosphate buffer (pH 8.0) is added to a 10 mL reactor, and then 100 mg of the above substrate 1. 80 mg of FDH, and 5 mg of PLP are added. pH is adjusted to 7.5-8.0, then 5 mg of NAD+ and 100 mg of the co-immobilized enzyme (wet, containing 50-80% of water) are added. It is reacted at 30'C for 16-20 hours, and the conversion rate is tested” (see, e.g., instant specification, pg. 21, lines 11-21). For Example 3, Table 7, Applicant is relying on “5 mL of 0.1 M phosphate buffer (pH 8.0) is added to a 10 mL reactor, and then 100 mg of the
above substrate 1, 120 mg of glucose and 5 mg of PLP are added, pH is adjusted to 7.5-8.0, then 5 mg of NAD+ and 100 mg of the co-immobilized enzyme (wet, containing 50-80% of water) are added. It is reacted at 30*C for 16-20 hours, and the conversion rate is tested” (see, e.g., instant specification, pg. 22, lines 5-9). Therefore, Applicant is relying on many factors for the unexpected results, wherein these results are not commensurate in scope with the claimed invention.
Regarding Applicant’s request for rejoinder of claims 8, 10-14, and 16-21 (remarks, page 20-23), this request is denied because claims 1-3 are not allowable.
Conclusion
Claims 1-3 are rejected.
No claims are allowed.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 EST.
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, Sharmila Landau can be reached at (571) 272-0614. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
Prosecution Insights