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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 607-611 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  A chimeric enzyme, engineered from two rice α-amylase isozymes, Amy1A and Amy3D, showed unique characteristics in soluble-starch and maltoheptaose hydrolysis. Effects of pH on soluble-starch hydrolysis and the thermostability of the chimeric enzyme were similar to those of the isozyme Amy3D. The previous study revealed that Amy1A shows high activity in soluble-starch hydrolysis and low activity in oligosaccharide degradation, while Amy3D shows low activity in soluble-starch hydrolysis and high activity in oligosaccharide degradation. The chimeric enzyme showed high activities in both soluble-starch hydrolysis and oligosaccharide degradation. These results suggest that protein modules of highly homologous enzymes are interchangeable, and that a novel enzyme with unique characteristics can be obtained by creating a chimeric enzyme.
    Type of Medium: Electronic Resource
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