http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-105255849-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-88 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y401-01015 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P13-005 |
| 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/C12N9-88 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-77 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-60 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P13-00 |
| filingDate | 2015-11-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2018-12-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2018-12-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-105255849-B |
| titleOfInvention | The glutamate decarboxylase mutation construction and its application that a kind of enzyme activity improves |
| abstract | The invention discloses glutamic acid decarboxylase enzyme mutants and its construction method that a kind of enzyme activity improves, belong to genetic engineering field.On the basis of mutant of the invention is the amino acid shown in SEQ ID N0.1, the 172nd tyrosine is mutated into cysteine.The mutant that the present invention obtains is in expression in escherichia coli, rear enzyme activity is 28.6U/mL to shake flask fermentation for 24 hours, and mutation enzyme activity improves 81%, and substrate affinity reduces by 53% compared with protoenzyme, specific enzyme activity simultaneously improves 83%, and the half-life period of enzyme is extended to for 24 hours by 16h at 35 DEG C.In the expression in escherichia coli recombinase, and the γ-aminobutyric acid of 283.8g/L can be obtained in resting cell glutamic acid 18h；The recombinase is expressed in glutamic acid rod bacterium, and the γ-aminobutyric acid of 126.7g/L can be obtained in resting cell glutamic acid 18h.Present invention demonstrates that 172 amino acids residues have larger impact to the catalytic action of enzyme and stability, certain basis is provided to the research of the catalytic mechanism of the enzyme, and improve the commercial application potentiality of the enzyme. |
| priorityDate | 2015-11-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 37.