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Article

Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions.

Bioresource technology - 1 Jan 2011

Ben Mabrouk Sameh, Aghajari Nushin, Ben Ali Mamdouh, Ben Messaoud Ezzedine, Juy Michel, Haser Richard, Bejar Samir

Abstract excerpt

Based on sequence alignments and homology modeling, Gly 312 and Lys 436 of the maltogenic amylase from Bacillus sp. US149 (MAUS149) were selected as targets for site-directed mutagenesis to improve the thermostability of the enzyme. Variants of MAUS149 with amino acid substitutions G312A, K436R and G312A-K436R had substrate specificities, kinetic parameters and pH optima similar to those of the wild-type enzyme;...

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PMID: 20855205
DOI: 10.1016/j.biortech.2010.08.082

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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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