http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-107603937-B
Outgoing Links
Predicate | Object |
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classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19 |
classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-57 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P13-08 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-48 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 |
filingDate | 2017-10-11-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
grantDate | 2020-10-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationDate | 2020-10-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | CN-107603937-B |
titleOfInvention | Recombinant escherichia coli for expressing lysine aminopeptidase and construction method thereof |
abstract | The invention discloses a recombinant escherichia coli for expressing lysine aminopeptidase and a construction method thereof, belonging to the fields of biological engineering technology and genetic engineering. The invention clones the aminopeptidase gene of wild pseudomonas aeruginosa and successfully expresses the recombinant lysine aminopeptidase in escherichia coli for the first time. After optimization of the shake flask, the highest enzyme activity in the cells reaches 3.47 U.mL ‑1 1.37 times of the original value before optimization. The specific site of the lysine aminopeptidase coding gene is subjected to directional mutation by using a full plasmid PCR technology, and the mutant lysine aminopeptidase with the thermal stability improved by about 10% is obtained by deleting a PA structural domain positioned in an inactive center. Provides a basis for further researching the characteristics, the structure and the function relationship and the like of the lysine aminopeptidase. |
priorityDate | 2017-05-18-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 38.