Author： Manonmani H.K. Kunhi A.A.M.
Publisher： Springer Publishing Company
ISSN： 0959-3993
Source： World Journal of Microbiology and Biotechnology, Vol.15, Iss.4, 1999-08, pp. : 475-480
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Abstract
α-Amylase gene from Bacillus laterosporus P_3 was cloned and expressed in Escherichia coli HB101 and DH5α. Up to 92% of the cloned gene product was secreted into the medium by the recombinant E. coli. The recombinant crude enzyme showed improved functionality in terms of activity at a wider pH range and at higher temperature, as compared to the crude enzyme from the donor strain. The improved functionality of the cloned enzyme was due to the absence of a contaminating protease which was co-produced in the donor strain. Sub-cloning of the α-amylase gene using the promoter-probe vector, pKT240 in E. coli DH5α indicated the presence of a promoter of B. laterosporus P_3 in the cloned fragment.
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