http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-108048430-B
Outgoing Links
Predicate | Object |
---|---|
classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-815 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-2437 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y302-01004 |
classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-84 |
classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-42 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-19 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-81 |
filingDate | 2018-01-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
grantDate | 2021-03-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationDate | 2021-03-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | CN-108048430-B |
titleOfInvention | Endoglucanase NfEG12A mutant and coding gene and application thereof |
abstract | The invention relates to the technical field of agricultural biology, in particular to an endoglucanase NfEG12A mutant and a coding gene and application thereof. The mutant is characterized in that the amino acid Y at the 7 th site and/or the 111 th site of the endoglucanase NfEG12A with the amino acid sequence shown as SEQ ID No.1 is mutated into W. The mutant has the optimum temperature and the optimum pH which are consistent with those of wild enzymes and are 65 ℃ and 5.0, the catalytic efficiency of the mutant on beta-1, 3-1, 4-glucan and xyloglucan is respectively improved by 0.5-0.8 times, and the mutant has good heat resistance and pH tolerance, so the mutant has very considerable application prospect in industry. |
priorityDate | 2018-01-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 240.