http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-109777788-B
Outgoing Links
| Predicate | Object |
|---|---|
| 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/C12P13-04 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-06 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-53 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 |
| filingDate | 2019-03-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2020-12-01-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2020-12-01-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-109777788-B |
| titleOfInvention | Leucine dehydrogenase mutant and application thereof |
| abstract | The invention discloses a leucine dehydrogenase mutant and application thereof, belonging to the technical field of biological engineering. On the basis of the leucine dehydrogenase amino acid sequence shown in SEQ ID NO.1, the 47 th amino acid residue M is mutated into V, and the 109 th amino acid residue N is mutated into I to obtain a leucine dehydrogenase mutant (the mutation points are M47V and N109I), the amino acid sequence of the mutant is shown in SEQ ID NO.3, and the leucine dehydrogenase enzyme activity of recombinant bacteria E.coli BL21-pET28a-BtLDH007 unit bacteria expressing the mutant reaches 170.9U/g; the yield of the L-2-aminobutyric acid produced by taking 2-ketobutyric acid as a substrate reaches up to 77.6g/L, and the conversion rate is 96.0%. |
| priorityDate | 2019-03-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 268.