Enhanced secreting expression and improved properties of a recombinant alkaline endoglucanase cloned in <Emphasis Type="Italic">Escherichia coli</Emphasis> |
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Authors: | Sen-Lin Liu Wei-Zhao Chen Gang Liu Miao Xing |
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Institution: | (1) Shenzhen Key Laboratory for Microbial Gene Engineering, College of Life Science, Shenzhen University, Shenzhen, 518060, People’s Republic of China |
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Abstract: | An alkaline endoglucanase from Bacillus akibai III-3A was successfully expressed in Escherichia coli in active form, and secretion was greatly enhanced by addition of 5 g/l ethylenediamine tetraacetic acid (EDTA) to the culture
medium at the induction time of 12 h. Under the optimal culture conditions, extracellular and total endoglucanase activities
were 18.5 and 31.2 U/ml, respectively. Both the recombinant and native enzymes exhibited similar properties with respect to
broad pH stability, good thermostability, and resistibility to various metal ions and reagents examined. However, unlike the
native endoglucanase that was partly inhibited by sodium dodecyl sulfate (SDS), the recombinant enzyme had good resistibility
to SDS, being very stable in the commercial detergents, and no decrease in residual activity was observed in 0.2% (w/v) laundry
detergent, indicating that it was suitable for application in detergents industry. |
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