http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-110438097-B

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classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-74
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0071
classificationIPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-125
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-74
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-53
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-02
filingDate 2019-08-14-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2020-12-29-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationDate 2020-12-29-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CN-110438097-B
titleOfInvention L-isoleucine hydroxylase mutant with improved heat stability and enzyme activity
abstract The invention discloses an L-isoleucine hydroxylase mutant with improved thermal stability and enzyme activity, in particular to an L-isoleucine hydroxylase mutant with improved thermal stability and enzyme activity and application thereof in production of 4-hydroxyisoleucine, belonging to the technical field of genetic engineering. The method for improving the thermal stability can be used for modifying other hydroxylases and provides theoretical guidance for producing other hydroxylated amino acids with high added values. The specific enzyme activity of the L-isoleucine hydroxylase produced by using the bacillus subtilis engineering bacteria can reach 2.4 +/-0.08U/mg, 5 batches of whole cells are repeated, continuous conversion is carried out for 45 hours, 856.91mM (126.1g/L) 4-HIL can be obtained, and after 5 batches, the conversion capacity of the L-isoleucine hydroxylase is still 84.1% of that of the first conversion.
priorityDate 2019-08-14-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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