http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-103114049-B
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_33a62710796e131599043055d399597f |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-645 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-84 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-19 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-34 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-30 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-81 |
| filingDate | 2013-01-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2015-04-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_aba665726231dea1a141716622a65682 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5d8a622a5c80d1c2559a279c62cfe264 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_03c33b8f9b51b78b8e62cfd703616602 |
| publicationDate | 2015-04-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-103114049-B |
| titleOfInvention | Recombined pichia pastoris strain for commonly expressing glucamylase and alpha-amylase and construction method thereof as well as mixed enzyme preparation |
| abstract | The invention provides a recombined pichia pastoris strain for commonly expressing glucamylase and alpha-amylase and a construction method of the recombined pichia pastoris strain as well as a mixed enzyme preparation prepared from the recombined pichia pastoris strain. The recombined pichia pastoris strain contains glucamylase genes from tiny mold funli and alpha-amylase genes at the same time; and gene sequences are respectively shown as SEQ ID NO.1 and SEQ ID NO.2. According to the mixed enzyme preparation prepared from the recombined strain, the saccharifying enzyme activity is improved by 79% when being compared with that of a strain which only carries the glucamylase genes, and the starch liquefacation enzyme activity is improved by 183% when being compared with that of a strain which only carries the alpha-amylase genes. The optimum operation temperatures and the optimum operation pH (Potential of Hydrogen) of the two enzymes are close; and the two enzymes have the synergistic promoting effect in a starch hydrolytic process, so that the application potential and advantages are great. |
| priorityDate | 2013-01-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 73.