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2000
Volume 12, Issue 4
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Protease MCP-01 is similar to other cold-adapted enzymes in that it is a cold-adapted serine protease having high specific activity and low thermostability at low and moderate temperature. Its thermolability and self-autolysis has resulted in difficulties in its purification, preservation and research on its structure and function. The disaccharide trehalose is known to effectively stabilize proteins. Its prevention effect on the autolysis of cold-adapted protease MCP-01 was monitored by capillary electrophoresis. In the absence of trehalose, protease MCP-01 autolyzed rapidly at 35°C. However, when trehalose was added, autolysis was remarkably prevented and the loss of activity reduced. MCP-01 may be a useful model for basic research on the interaction of protein and trehalose.

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/content/journals/ppl/10.2174/0929866053765626
2005-05-01
2025-10-15
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  • Article Type:
    Review Article
Keyword(s): autolysis; cold-adapted protease; trehalose
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