http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-109486794-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-2442 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y302-01014 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-75 |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-125 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-42 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-56 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-75 |
| filingDate | 2018-12-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2020-06-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2020-06-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-109486794-B |
| titleOfInvention | Chitinase mutant with improved enzyme activity |
| abstract | The invention discloses a chitinase mutant with improved enzyme activity, and belongs to the technical field of genetic engineering and enzyme engineering. According to the invention, the 43 th cysteine, the 273 rd phenylalanine and the 336 th glutamic acid near the catalytic structural domain of the chitinase molecule are mutated into aspartic acid, the 273 th phenylalanine and the 336 th glutamic acid are mutated into arginine through a site-specific mutation mode, so that the enzyme activity of the bacterial strain for expressing the chitinase is obviously improved, wherein the enzyme activities of the single mutant strains F273W and E336R are respectively improved by 1.37 times and 1.22 times compared with that of the original bacterial strain. The enzyme production capability and the catalytic efficiency of the modified strain are improved, and the content of chitooligosaccharide in the purified mutant is detected by HPLC, so that the sugar production of the F273W mutant is 1.65g/L after catalyzing for 3h, wherein the GlcNAc is 0.12g/L, (GlcNAc) 2 1.53g/L, which is increased by 49.7 percent compared with the wild strain. |
| priorityDate | 2018-12-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 369.