| Autor: |
Xiu-Lan Chen, Cai-Yun Shun, Yu-Zhong Zhang, Pei-Ji Gao |
| Předmět: |
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| Zdroj: |
Biotechnology Letters; Oct2003, Vol. 25 Issue 20, p1763-1767, 5p |
| Abstrakt: |
A protease, MCP-01, produced by a deep-sea psychrotrophic strain of Pseudoaltermonas sp. SM9913 was purified and its autolysis reaction at 20 °C–50 °C was monitored by capillary electrophoresis. Capillary electrophoresis provides a rapid assay because the degree and state of autolysis of protease MCP-01 could be observed within 6 min. The autolysis rate increased as the temperature rose in the tested range. After 30 min incubation at 30 °C, 77% of MCP-01 autolyzed into peptides. However, its activity for the hydrolysis of casein was reduced by only 4%. The rate of loss of activity of MCP-01 was thus slower than that of autolysis of MCP-01 at 30 °C. Similar results were obtained when MCP-01 was incubated at 20 °C, 40 °C and 50 °C. Large peptides produced by autolysis of MCP-01 therefore still have catalytic activity. When these large peptides autolyzed further into smaller peptides, the enzyme conformation that retained its catalytic activity was destroyed and activity was lost. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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