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( Salimi,Ali ),( Fatemeh Yousefi ),( Marzieh Ghollasi ),( Sara Daneshjou ),( Hesam Tavoli ),( Sirous Ghobadi ),( Khosro Khajch ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.8
Previously, an extracellular a-amylase (BKA) had been purified from the culture of Bacillus sp. KR8104. Subsequently, the crystal structure of the active enzyme revealed a 422 amino acids polypeptide. In this study, the bka was cloned into E. coli, which encoded a polypeptide of 659 amino acids including two additional fragments: one 44 residues N-terminal fragment and another 193 residues C-terminal fragment. In order to investigate the role of the C-terminal fragment, two constructs with and without this region [BKAΔ(N44) and BKAΔ(N44C193)] were designed and expressed in E. coli BL21. The optimum pH, thermal stability, and the end-products of starch hydrolysis were found to be similar in both constructs. The Km and Vmax values for BKAΔ (N44) were lower than BKAΔ (N44C193), using either starch or ethylidene-blocked 4-nitrophenylmaltoheptaoside as a substrate.