Purification and partial characterisation of a cathepsin L-like proteinase from sea cucumber (Stichopus japonicus) and its tissue distribution in body wall

Da Yong Zhou, Xian Na Chang, Sha Sha Bao, Liang Song, Bei Wei Zhu, Xiu Ping Dong, Yuan Zong, Dong Mei Li, Mao Mao Zhang, Yu Xin Liu, Yoshiyuki Murata

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

A cathepsin L-like proteinase (CLP) with molecular weight of 30.9 kDa from the gut of sea cucumber (Stichopus japonicas, S. japonicus) was isolated and purified to homogeneity by several chromatographic procedures. The enzyme exhibited optimum activity at pH 5.0-5.5 and 50 C, and showed thermostability up to 40 C. The enzyme activity was completely inhibited by Zn2+, strongly inhibited by Fe2+ and Cu2+, drastically reduced by cysteine proteinase inhibitors, but slightly enhanced by thiol-activating agents. The enzyme efficiently hydrolysed the specific substrate of cathepsin L, but hardly hydrolysed the specific substrates for cathepsin B, cathepsin H and cathepsin K. Immunohistochemical studies indicated that the CLP was more abundant in the epidermis rather than in the dermis of S. japonicus body wall. The distribution of CLP showed positive correlation with autolysis rate. Therefore, the relationship between CLP and autolysis deserved further study.

Original languageEnglish
Pages (from-to)192-199
Number of pages8
JournalFood Chemistry
Volume158
DOIs
Publication statusPublished - Sep 1 2014

Keywords

  • Autolysis
  • Body wall
  • Cathepsin L-like proteinase
  • Immunohistochemistry
  • Sea cucumber (Stichopus japonicus)

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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