http://rdf.ncbi.nlm.nih.gov/pubchem/patent/KR-100689339-B1
Outgoing Links
| Predicate | Object |
|---|---|
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N2500-60 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N2523-00 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-6405 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-50 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-64 |
| filingDate | 2005-07-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2007-03-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate | 2007-03-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | KR-100689339-B1 |
| titleOfInvention | Novel Proteolytic Enzymes Derived from In Situal Suspension and Its Manufacturing Method |
| abstract | The present invention relates to a method for producing proteolytic enzymes from the medicinal herb, which is an herbal medicine. As a result of extracting, isolating, purifying and analyzing the sperm coenzyme, the molecular weight of the gyreum protease was about 18,000 Daltons (daltons) in molecular weight and isoelectric point pI. The optimum pH was 8.97, and the optimum temperature was 50 ° C. Metal ions did not significantly affect the in situ proteolytic enzyme activity of the present invention, Mn 2 + , CU 2 + , Ca 2 + , Zn 2 + ions increased the enzyme activity, but the results of the substrate specificity The relative activity of collagen protein was high.n n n n Salinity, proteolytic enzymes, extraction, separation, purification, biochemical properties |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-104940236-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-104940236-B |
| priorityDate | 2005-07-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 297.