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Article

Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance.

Applied and environmental microbiology - 1 Aug 2003

Kim Young-Wan, Choi Ji-Hye, Kim Jung-Wan, Park Cheonseok, Kim Jung-Woo, Cha Hyunju, Lee Soo-Bok, Oh Byoung-Ha, Moon Tae-Wha, Park Kwan-Hwa

Abstract excerpt

The thermostability of maltogenic amylase from Thermus sp. strain IM6501 (ThMA) was improved greatly by random mutagenesis using DNA shuffling. Four rounds of DNA shuffling and subsequent recombination of the mutations produced the highly thermostable mutant enzyme ThMA-DM, which had a total of seven individual mutations. The seven amino acid substitutions in ThMA-DM were identified as R26Q, S169N, I333V, M375T,...

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Identifiers

PMID: 12902281
DOI: 10.1128/AEM.69.8.4866-4874.2003
PMCID: PMC169122

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Source receipt: pubmed, retrieved 7 Sept 2026.

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