Improving the Thermostability of Raw-Starch-Digesting Amylase from a Cytophaga sp. by Site-Directed Mutagenesis

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...

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Vydáno v:	Appl Environ Microbiol
Hlavní autoři:	Shiau, Rong-Jen, Hung, Hui-Chen, Jeang, Chii-Ling
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 2003
Témata:	Enzymology and Protein Engineering
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC154812/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12676725/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/AEM.69.4.2383-2385.2003
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