Purification and characterization of cocoonase from the silkworm Bombyx mori

Hisayoshi Fukumori, Satoshi Teshiba, Yuichi Shigeoka, Kohji Yamamoto, Yutaka Banno, Yoichi Aso

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10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)202-211
Number of pages10
JournalBioscience, Biotechnology and Biochemistry
Issue number2
Publication statusPublished - 2014

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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