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Article

Mutagenesis for improvement of activity and thermostability of amylomaltase from Corynebacterium glutamicum.

International journal of biological macromolecules - 1 May 2016

Nimpiboon Pitchanan, Kaulpiboon Jarunee, Krusong Kuakarun, Nakamura Shigeyoshi, Kidokoro Shun-ichi, Pongsawasdi Piamsook

Abstract excerpt

This work aims to improve thermostability of amylomaltase from a mesophilic Corynebacterium glutamicum (CgAM) by random and site-directed mutagenesis. From error prone PCR, a mutated CgAM with higher thermostability at 50 °C compared to the wild-type was selected and sequenced. The result showed that the mutant contains a single mutation of A406V. Site-directed mutagenesis was then performed to construct A406V...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 26875536
DOI: 10.1016/j.ijbiomac.2016.02.022

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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