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

doi:10.1016/j.foodchem.2014.02.105

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 journal › Article › peer-review

40 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 language	English
Pages (from-to)	192-199
Number of pages	8
Journal	Food Chemistry
Volume	158
DOIs	https://doi.org/10.1016/j.foodchem.2014.02.105
Publication status	Published - Sept 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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10.1016/j.foodchem.2014.02.105

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Zhou, D. Y., Chang, X. N., Bao, S. S., Song, L., Zhu, B. W., Dong, X. P., Zong, Y., Li, D. M., Zhang, M. M., Liu, Y. X., & Murata, Y. (2014). Purification and partial characterisation of a cathepsin L-like proteinase from sea cucumber (Stichopus japonicus) and its tissue distribution in body wall. Food Chemistry, 158, 192-199. https://doi.org/10.1016/j.foodchem.2014.02.105

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

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.",

keywords = "Autolysis, Body wall, Cathepsin L-like proteinase, Immunohistochemistry, Sea cucumber (Stichopus japonicus)",

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

note = "Funding Information: This work was supported financially by “ The National Natural Science Foundation of China (Grant Nos. 30901124 and 31000754 )” and “Organization Project for National Engineering Research Center of Seafood funded by Ministry of Science and Technology of the People{\textquoteright}s Republic of China (2012FU125X03)”.",

year = "2014",

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doi = "10.1016/j.foodchem.2014.02.105",

language = "English",

volume = "158",

pages = "192--199",

journal = "Food Chemistry",

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T1 - Purification and partial characterisation of a cathepsin L-like proteinase from sea cucumber (Stichopus japonicus) and its tissue distribution in body wall

AU - Zhou, Da Yong

AU - Chang, Xian Na

AU - Bao, Sha Sha

AU - Song, Liang

AU - Zhu, Bei Wei

AU - Dong, Xiu Ping

AU - Zong, Yuan

AU - Li, Dong Mei

AU - Zhang, Mao Mao

AU - Liu, Yu Xin

AU - Murata, Yoshiyuki

N1 - Funding Information: This work was supported financially by “ The National Natural Science Foundation of China (Grant Nos. 30901124 and 31000754 )” and “Organization Project for National Engineering Research Center of Seafood funded by Ministry of Science and Technology of the People’s Republic of China (2012FU125X03)”.

PY - 2014/9/1

Y1 - 2014/9/1

N2 - 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.

AB - 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.

KW - Autolysis

KW - Body wall

KW - Cathepsin L-like proteinase

KW - Immunohistochemistry

KW - Sea cucumber (Stichopus japonicus)

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JO - Food Chemistry

JF - Food Chemistry

ER -

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

Abstract

Keywords

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