http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-105026558-B
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y101-03004 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N2333-904 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-54 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-54 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0006 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-54 |
| filingDate | 2014-01-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2020-05-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2020-05-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-105026558-B |
| titleOfInvention | Novel glucose oxidase derived from aspergillus niger |
| abstract | Disclosed herein are novel glucose oxidase variants having in addition to the two substitutions T30V and I94V according to SEQ ID No. 1, position S53 in the polypeptide sequence; a137; a173; a332; f414; and at least one further amino acid substitution in any one of V560. The optimized glucose oxidase variants thus show specificity for glucose and a significantly reduced oxygen consumption rate. In another aspect, the present invention provides glucose oxidase variants having significantly reduced oxygen consumption rates and/or increased enzymatic activity for electron mediators other than oxygen. The present invention also provides an assay device with at least one of the GOx variants disclosed herein for improved blood glucose measurement. |
| priorityDate | 2013-01-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 528.