Purification and characterization of a cysteine-like protease from the body wall of the sea cucumber <Emphasis Type="Italic">Stichopus japonicus</Emphasis> |
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Authors: | H Qi X P Dong L N Cong Y Gao L Liu T Mikiro B W Zhu |
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Institution: | (1) College of Bio & Food Technology, Dalian Institute of Light Industry, Qinggongyuan No.1, Ganjingzi District, Dalian, 116034, P.R. China;(2) Department of Biological Resources Chemistry, Faculty of Agriculture, Okayama University, Okayama 700-8530, Japan |
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Abstract: | The sea cucumber (Stichopus japonicus) is able to undergo autolysis in response to a variety of environmental and mechanical cues. Within the framework of a long-term
study of this phenomenon we have purified a protease from the body wall of the sea cucumber by means of ion-exchange chromatography
with DE-52 cellulose and gel filtration chromatography with Sephadex G-100. The final enzyme preparation was nearly homogeneous
on polyacrylamide gel electrophoresis, and its molecular weight was estimated to be approximately 35.5 kDa. The purified enzyme
exhibited a maximum activity for the hydrolysis of casein at pH 7.0 and 50°C and a remarkable stability at pH 4.0–7.0 and
40–60°C. Based on the inhibition and activation profiles obtained with numerous specific protease inhibitors and an activator,
the protease purified from the body wall of the sea cucumber was defined to be a cysteine-like protease. |
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Keywords: | Characterization Proteases Purification Sea cucumber (Stichopus japonicus) |
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