http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-105602913-B

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classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P17-12
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0006
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y101-01184
classificationIPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-53
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filingDate 2016-03-09-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2019-02-01-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationDate 2019-02-01-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CN-105602913-B
titleOfInvention Recombinant carbonyl reductase mutant ReCR-Mut, encoding gene, engineering bacteria and application
abstract The invention discloses a recombinant carbonyl reductase mutant ReCR-Mut, an encoding gene, an engineering bacterium and an application thereof. The mutant ReCR-Mut is the amino acid sequence shown in SEQ ID NO. Mutated to phenylalanine; mutant ReCR-Mut has higher enzymatic activity and catalytic efficiency than wild-type ReCR; specific enzyme activity of mutant ReCR-Mut reducing N-Boc-3-piperidone It is 1.42 times that of wild-type ReCR, and the k cat /K m value of mutant ReCR-Mut to N-Boc-3-piperidone is 1.37 times that of wild-type; Alcohol is used as co-substrate and organic phase, and NAD + is used as coenzyme to synthesize optically pure (S)-N-Boc-3-piperidinol efficiently and asymmetrically; in the preferred two-phase system, 300g/LN-Boc-3-piperidol The asymmetric reduction reaction of the pyridone was catalyzed by the whole cell method for 12 hours, the product ee value of the product (S)-N-Boc-3-piperidinol was >99%, and the yield was 93.9%; and the wild-type carbonyl reductase ReCR Compared with the biocatalyst, the product yield increased by 11.9%.
priorityDate 2016-03-09-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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