The role of N185D substitution in enhancing activity of BaqA∆C α-amylase.

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 exp

SUBMITTER: Hanif MA 

PROVIDER: S-EPMC12695923 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature