RRC ID 33114
著者 Fukumori H, Teshiba S, Shigeoka Y, Yamamoto K, Banno Y, Aso Y.
タイトル Purification and characterization of cocoonase from the silkworm Bombyx mori.
ジャーナル 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.
巻・号 78(2)
ページ 202-11
公開日 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
引用数 3
WOS 分野 FOOD SCIENCE & TECHNOLOGY BIOTECHNOLOGY & APPLIED MICROBIOLOGY CHEMISTRY, APPLIED BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
カイコ p50