| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_8d0fc2b70675ee19bd5fc464f5ae9061 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y402-01001 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-88 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12M1-40
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P7-62 |
| filingDate |
2013-05-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0dca84ae9aef47b2b80f455c3e1ca853 |
| publicationDate |
2014-12-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
KR-20140139787-A |
| titleOfInvention |
Novel carbonic anhydrase from Persephonella marina EX-H1 and use thereof |
| abstract |
The present invention relates to a novel carbonic anhydrase derived from Persephonella marina EX-H1 and its use. The novel carbonic anhydrase isolated from marine microalgae has excellent carbon dioxide hydration activity and thermal stability, Can be used for immobilization, can be used not only for the production of bicarbonate compounds but also as a catalyst for the synthesis of useful metabolites, thereby increasing the synthesis yield. In addition, by removing the N-terminal signal peptide of the carbonic anhydrase, the water-soluble expression rate and enzyme activity can be increased. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2022181939-A1
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-10927364-B2
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2018017792-A1
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-11773386-B2
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-20210120388-A
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-20220121652-A |
| priorityDate |
2013-05-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |