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classificationCPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y02P20-52
classificationIPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-05
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-78
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P41-00
filingDate 1991-11-22-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_986abec0c75476c5c324d03507d2b59d
publicationDate 1992-11-27-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-H04341185-A
titleOfInvention New nitrilase
abstract PURPOSE: To provide the subject new nitrilase derived from a bacterial strain belonging to the genus Alkaligenes and capable of enantioselectively hydrolyzing a racemic hydroxynitrile and producing an optically active hydroxycarboxylic acid useful as an industrical raw material. n CONSTITUTION: A nitrilase derived from a bacterial strain belonging to the genus Alkaligenes. Enzymatic action: Catalyze a hydrolysis reaction of a nitrile compound into a carboxylic group and ammonia by acting on a nitrile group of the nitrile compound and catalyze an enantioselective hydrolysis reaction of an α-hydroxynitrile into an optically active α-hydroxycarboxylic acid; Substrate specificity: Capable of acting on n-valeronitrile, acrylonitrile, etc., and showing a high reaction rate especially hydrolysis of chloroacetonitrile, benzylcynide, etc.; Molecular weight: 460000±30000, molecular weight of subunit is 32000±2000; N-terminal amino acid sequence: Sequence of the formula; Temperature stability 10-45°C aty pH 7; pH stability: pH 6.5-8, etc. The above- mentioned enzyme is recommendably collected from a culture medium of Alkaligenes faecalis ATCC-8750 or cell bodies thereof. n COPYRIGHT: (C)1992,JPO&Japio
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