作者: H.K. Manonmani , A.A.M. Kunhi
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摘要: α-Amylase gene from Bacillus laterosporus P3 was cloned and expressed in Escherichia coli HB101 DH5α. Up to 92% of the product secreted into medium by recombinant E. coli. The crude enzyme showed improved functionality terms activity at a wider pH range higher temperature, as compared donor strain. due absence contaminating protease which co-produced Sub-cloning α-amylase using promoter-probe vector, pKT240 DH5α indicated presence promoter B. fragment.