http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-108841805-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y301-01003 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-20 |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 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/C12N9-20 |
| filingDate | 2018-06-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2021-07-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2021-07-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-108841805-B |
| titleOfInvention | Lipase mutant with improved heat stability |
| abstract | A lipase mutant with improved thermal stability belongs to the technical field of enzyme genetic engineering. The invention discloses a lipase mutant with improved thermostability, which is obtained by taking Aspergillus oryzae (Aspergillus oryzae) lipase as a parent through site-directed mutagenesis technology. In the amino acid sequence of this mutant, the amino acid mutations involved are: gly57Glu/Leu156 Cys. The temperature (T) at which the mutant loses 50 percent of enzyme activity after being kept for 10min at different temperatures is used 50％ 10 ) And a half-life (t) at 50 ℃ 50 1/2 ) The expression shows that the mutant has improved heat stability, higher practical application value and wide market prospect. |
| priorityDate | 2018-06-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 221.