Probing the function of C-terminal region of recombinant α-amylase BmaN1 from NL3.

The α-amylase BmaN1 from NL3 is a member of GH13_45 subfamily that has a conserved C-terminal region of approximately 30 residues. This region features a motif of five aromatic amino acids predicted to play a role in starch binding. This study aimed to unravel the role of the C-terminal region in starch hydrolysis.

Comparative biochemical analysis of full-length and truncated BaqA α-amylases from MKSC 6.2.

BaqA is a raw starch degrading α-amylase produced by the marine bacterium MKSC 6.2, associated with soft corals. This α-amylase belongs to a new subfamily Glycoside Hydrolases (GH) 13_45 which has several unique characteristics, namely, a pair of tryptophan residues Trp201 and Trp202, a distinct LPDIx signature in the Conserved Sequence Region-V (CSR-V), and an elongated C-terminus containing five aromatic residues.