| 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
|
| Resource |
| Silkworms |
p50 |
