http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-111979218-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-80 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y305-01041 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-80 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-55 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 |
| filingDate | 2020-07-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2023-01-20-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2023-01-20-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-111979218-B |
| titleOfInvention | A mutant of chitin deacetylase from Arthrobacter sp. AW19M34-1 |
| abstract | The invention discloses a mutant of Arthrobacter sp.AW19M34‑1 chitin deacetylase, in which the amino acid sequence of the marine bacterium Arthrobacter sp.AW19M34‑1 chitin deacetylase is mutated as follows: 172-position lysine K mutation It is glutamic acid E, glutamic acid E at position 200 is mutated to tyrosine Y, serine S at position 201 is mutated to tryptophan W, and the codon optimized sequence of Arthrobacter sp.AW19M34‑1 chitin deacetylase gene is as follows As shown in Appendix 1, the amino acid sequence of the marine bacterium Arthrobacter sp. The catalytic activity of the chitin deacetylase increases, while other catalytic properties of the enzyme remain basically unchanged. The activity of the mutant enzyme to catalyze deacetylation of crystal chitin is 2.57 times that of the wild-type enzyme, which has higher economic and social value and is worthy of promotion. |
| priorityDate | 2020-07-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 214.