http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-110540980-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-815 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-6454 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/C12R1-84 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-19 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P7-64 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-20 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-55 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-81 |
| filingDate | 2019-09-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2021-06-11-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2021-06-11-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-110540980-B |
| titleOfInvention | Streptomyces marinus lipase mutant and application thereof |
| abstract | The invention discloses a marine streptomyces lipase mutant and application thereof, belongs to the technical field of genetic engineering and enzyme engineering, and aims to design and construct an enzyme mutant library based on enzyme protein structural analysis, screen and obtain a lipase mutant preferring a partial glyceride substrate, and construct and obtain a pichia pastoris engineering bacterium for efficiently expressing the mutant, thereby laying a foundation for the wide application of the mutant. Compared with wild lipase, the Streptomyces marinus lipase mutant provided by the invention has the advantages that the partial glyceride rich in n-3 fatty acid is synthesized by high-efficiency catalysis, the partial glyceride content in the catalytic product is 86.48% (wherein 49.01% PUFA-DAG, 37.47% PUFA-MAG) under the optimal reaction condition, and the partial glyceride content is increased by about 23 times compared with the wild lipase (3.8% PUFA-DAG). |
| priorityDate | 2019-09-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 200.