Journal
ARCHIVES OF MICROBIOLOGY
Volume 191, Issue 2, Pages 171-175Publisher
SPRINGER
DOI: 10.1007/s00203-008-0437-8
Keywords
Escherichia coli; Endoglucanase; Fusion protein; Over-expression; Phytase activity
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Phytase and endoglucanase enzymes are being widely used as feed additives in poultry industry. In our earlier studies, the Bacillus phytase, when expressed in Escherichia coli, was found in inclusion bodies, whereas endoglucanase was found in active soluble form. Herein, we report the development of a chimeric gene construct coding for similar to 73 kDa fusion protein and its over-expression in E. coli in soluble form. The novel enzyme exhibited both endoglucanase and phytase activities across broad pH (4.0-8.0) and temperature (25-75A degrees C) ranges. As such, the bi-functional enzyme seems promising and might serve as a potential feed additive for enhanced nutrition uptake in monogastric animals.
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