http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-113481183-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_cc4e13141d402ceb885f368dfa042348 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-20 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y301-01003 |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-20 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-55 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 |
| filingDate | 2021-06-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_16b386d5fc9d983f0eb0e84e5d2c1004 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_cd48394baeb99a168f2c937f28e2d5bb http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1c2298cabb6e8dc72c2e307c16f808e7 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_c5af392b9eacecb62651026b321dfac8 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_4d5d8c53dc42f58104921c2c6a0d295c http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_963f335b95f4741699783e87ad59b4fa |
| publicationDate | 2021-10-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-113481183-A |
| titleOfInvention | A marine microbial lipase chimera and its construction method and application |
| abstract | The invention belongs to the field of enzyme engineering, and discloses a marine microorganism lipase chimera and a construction method and application thereof. The amino acid sequence of the lipase chimera is shown in SEQ NO. 1, and the gene nucleotide sequence encoding the lipase chimera is as follows: shown in SEQ NO.2. The construction method is as follows: (1) PCR amplifies the first 160 amino acid peptides of the N-terminal of GMGL; (2) The amino acid peptides of step (1) are replaced by the corresponding peptides of CoMGL in a seamless cloning manner to obtain a recombinant plasmid; (3) ) The successfully sequenced recombinant plasmid was transformed into BL21(DE3) competent cells for heterologous expression and purification to obtain lipase chimera 160. The specific enzyme activity of the modified chimera 160 under the optimum conditions is 741.8 U/mg, which is 4.9 times that of wild-type CoMGL and 2.7 times that of wild-type GMGL; the optimum reaction temperature is 70 °C, which has good industrial application prospects. . |
| priorityDate | 2021-06-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 315.