Reference - Detail
| RRC ID | 33114 |
|---|---|
| Author | Fukumori H, Teshiba S, Shigeoka Y, Yamamoto K, Banno Y, Aso Y. |
| Title | Purification and characterization of cocoonase from the silkworm Bombyx mori. |
| Journal | Biosci Biotechnol Biochem |
| Abstract |
Cocoonase (CCN) which facilitates the degradation of a cocoon is recognized as a trypsin-like serine protease. In this study, CCN from the silkworm Bombyx mori was purified and comprehensively characterized. Its activity was maximal at about pH 9.8. It was stable above pH 3.4 at 4 °C and below 50 °C at pH 7.5. CuSO₄, FeSO₄, and ZnSO₄ showed inhibitory effects on CCN, but other salts improved activity. Typical trypsin inhibitors inhibited CCN, but the relative inhibitory activities were much lower than those against bovine trypsin. An extract of cocoon shells inhibited trypsin, but it was only slightly inhibitory against CCN. There were significant differences in catalytic efficiencies and substrate specificities as between CCN and bovine trypsin. |
| Volume | 78(2) |
| Pages | 202-11 |
| Published | 2014-1-1 |
| DOI | 10.1080/09168451.2014.878215 |
| PMID | 25036672 |
| MeSH | Animals Bombyx / enzymology* Cattle Enzyme Stability Hydrogen-Ion Concentration Peptide Hydrolases / chemistry Peptide Hydrolases / isolation & purification* Peptide Hydrolases / metabolism* Protease Inhibitors / pharmacology Salts / pharmacology Substrate Specificity |
| IF | 1.516 |
| Times Cited | 3 |
| WOS Category | FOOD SCIENCE & TECHNOLOGY BIOTECHNOLOGY & APPLIED MICROBIOLOGY CHEMISTRY, APPLIED BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Altmetric score |
オルトメトリクス指標項目
|
| The most frequently cited source | X(Twitter) |
| Total number of mentions | 1 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Silkworms | p50 |