Improving the Thermostability of Raw-Starch-Digesting Amylase from a Cytophaga sp. by Site-Directed Mutagenesis
2003 ◽
Vol 69
(4)
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pp. 2383-2385
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ABSTRACT A heat-stable raw-starch-digesting amylase (RSDA) was generated through PCR-based site-directed mutagenesis. At 65°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 Ca2+-independent mechanism.
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2019 ◽
Vol 20
(24)
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pp. 6224
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2001 ◽
Vol 12
(10)
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pp. 2012-2018
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2007 ◽
Vol 70
(1)
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pp. 191-195
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1993 ◽
Vol 240
(2)
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pp. 221-230
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