| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_cb351a5a4e03ee3773bd0df5dbae9ac3 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07B2200-07
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07C33-26
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-686 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0004
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-52
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0008
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07C29-143
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0006
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-641
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y304-2207
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-04
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-22
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y101-01184 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P7-22
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-02 |
| filingDate |
2017-11-21-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_750f5b1271bf3395db0e7361b6fd8132
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_2c22aabb9c48edd69411ef614a96f855 |
| publicationDate |
2018-11-07-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
EP-3399030-A1 |
| titleOfInvention |
Carbonyl reductase oligomer and use thereof in synthesis of chiral alcohol |
| abstract |
Disclosed are methods for the synthesis of chiral alcohols by Sortase A-mediated oxidoreductase oligomers, which relates to the field of biocatalysis. In the present disclosure, oxidoreductase oligomers were used as biocatalysts for chiral alcohol preparation. Compared to wild-type enzymes, the oxidoreductase oligomers significantly improved catalytic activity and thermal stability. The sortase A-mediated oxidoreductase oligomers had 6 - 8 folds improvement in specific activity over that of the wild-type enzymes. The oligomers displayed a T m value 6 - 12 °C higher than that of the wild-type, suggesting the sortase A-mediated oxidoreductase oligomers significantly improved thermostability of the enzymes. The oxidoreductase oligomers catalyzed asymmetric transformation to produce ( S )-1-phenyl-1,2-ethanediol or ( R )-1-phenethyl alcohol within 3 - 6 hr, with an optical purity of 98%-100% and a yield of 98%-99%. |
| priorityDate |
2016-12-30-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |