Improving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis.
نویسندگان
چکیده
A heat-stable raw-starch-digesting amylase (RSDA) was generated through PCR-based site-directed mutagenesis. At 65 degrees C, the half-life of this mutant RSDA, which, compared with the wild-type RSDA, lacks amino acids R178 and G179, was increased 20-fold. While the wild type was inactivated completely at pH 3.0, the mutant RSDA still retained 41% of its enzymatic activity. The enhancement of RSDA thermostability was demonstrated to be via a Ca(2+)-independent mechanism.
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ورودعنوان ژورنال:
- Applied and environmental microbiology
دوره 69 4 شماره
صفحات -
تاریخ انتشار 2003