ArticleScientific reports2025
The role of N185D substitution in enhancing activity of BaqA∆C α-amylase.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
α-Amylases are endoenzymes capable of degrading starch into branched and linear oligosaccharides. Since starch-processing industries rely on starch-rich mashes, exploring amylases that can efficiently hydrolyse highly concentrated raw starch is crucial. BaqA from Bacillus aquimaris MKSC 6.2 is particularly promising as it hydrolyses raw starch into simple sugars without preheating, offering potential energy and cost savings for industrial applications. This study investigates the functional role of a specific residue within Conserved Sequence Region (CSR) V of BaqAΔC (a truncated BaqA lacking 34 amino acids from the C terminus), predicted to influence catalytic activity, product specificity, and substrate binding. A BaqA∆CN185D mutant was generated through site-directed mutagenesis and expressed in Escherichia coli ArcticExpress (DE3). Compared with BaqAΔC, the mutant displayed higher specific activity (7.6 ± 0.2 vs. 5.8 ± 0.4 U/mg) and a greater degree of hydrolysis (2.18% vs. 1.41%). Futhermore, BaqAΔCN185D showed a significantly lower K
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