http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-113215130-B

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Predicate Object
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-16
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y301-04003
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-55
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-16
filingDate 2021-05-11-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2022-12-06-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationDate 2022-12-06-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CN-113215130-B
titleOfInvention Phospholipase C mutant, preparation method and application thereof
abstract The invention provides a phospholipase C mutant, a preparation method and application thereof. The amino acid sequence of the mutant is shown in SEQ ID NO:1. The mutant is a mutation of the 96th phenylalanine F from Bacillus cereus HSL3 wild-type phospholipase C to arginine R; the 153rd glutamine Q is mutated into proline Sour P. Compared with the wild-type recombinant PLC, the thermal stability of this mutant has been significantly improved, and the optimal reaction temperature has been increased from 80°C to 90°C, which is the highest reaction temperature reported so far; 56 % about enzyme activity. The kcat and kcat/Km of the mutant were 5.64 times and 2.37 times that of the wild type, respectively, and the adaptability to the substrate was also improved. Homology modeling analysis showed that the mutation resulted in a decrease in the proportion of random coils and inhibited the activity of a specific loop, thereby significantly improving the thermostability and activity of the mutant.
priorityDate 2021-05-11-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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