http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2017044510-A1
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_540796ea8bfe796adeb9fe82c83d6445 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-2417 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y302-01001 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-28 |
| filingDate | 2015-04-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_1269de799a7155e9fd7d024c50ffb7f9 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_893b8928fdd4a7843e8bfcedc6c8afde http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_d911514d0498538b8f7af159a986f536 |
| publicationDate | 2017-02-16-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | US-2017044510-A1 |
| titleOfInvention | Cold-active alpha-amylase |
| abstract | There is provided a novel cold-active alpha-amylase identified by a functional metagenomic approach expressed in E. coli and purified to homogeneity. Functional, biochemical analysis has documented that the alpha-amylase is cold-adapted with a temperature optimum at 10° C. to 20° C. and that the enzyme is active over a broad pH range. Sequence analysis has indicated that the alpha-amylase is related to Clostridia, and has revealed classical characteristics of cold-adapted enzymes. |
| priorityDate | 2014-04-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 96.