Molecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) from Myxococcus sp. Strain V11.

ABSTRACT: A novel multifunctional isoamylase, MIsA from Myxococcus sp. strain V11, was expressed in Escherichia coli BL21(DE3). Sequence alignment revealed that MIsA is a typical isoamylase that belongs to glycoside hydrolase family 13 (GH 13). MIsA can hydrolyze the α-1,6-branches of amylopectin and pullulan, as well as the α-1,4-glucosidic bond in amylose. Additionally, MIsA demonstrates 4-α-D-glucan transferase activity, enabling the transfer of α-1,4-glucan oligosaccharides between molecules, particularly with linear maltooligosaccharides. The K_m, K_cat, and V_max values of the MIsA for amylopectin were 1.22 mM, 40.42 µmol·min^-1·mg^-1, and 4046.31 mM·min^-1. The yields of amylopectin and amylose hydr

SUBMITTER: Feng S 

PROVIDER: S-EPMC11544908 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature