http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-112646799-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y402-02 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P19-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P19-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-88 |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-60 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-66 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/C12P19-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P19-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 |
| filingDate | 2021-01-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2022-01-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2022-01-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-112646799-B |
| titleOfInvention | Ulva lactuca polysaccharide lyase mutant and application thereof |
| abstract | The invention provides an ulva polysaccharide lyase mutant and application thereof, belonging to the field of genetic engineering. The activity of the enzyme provides a degradation function in ulvan. The ulva polysaccharide lyase mutant is characterized in that on the basis of the amino acid sequence of wild ulva polysaccharide lyase, the 35 th position of the mutant is mutated from Asn to Pro, the optimum temperature and the optimum pH of the mutant and the wild enzyme are both 40 ℃ and 9.0, and the specific activity of the mutant is about 1.35 times that of the wild enzyme. Under the optimal reaction condition, the catalytic efficiency of the mutant is improved by about 2 times compared with that of the wild type. When ulva powder is used as a substrate, the content of reducing sugar produced by the catalytic reaction of the mutant enzyme is 1.27 times that of a wild degradation substrate, so that the mutant enzyme is obviously improved in enzyme activity and can be used for reducing the economic cost of industrial application. |
| priorityDate | 2021-01-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 315.