Hydrolysis of Arabinoxylo-oligosaccharides by α-L-Arabinofuranosidases and β-D-Xylosidase from Bifidobacterium dentium.

ABSTRACT: Two α-L-arabinofuranosidases (BfdABF1 and BfdABF3) and a β-D-xylosidase (BfdXYL2) genes were cloned from Bifidobacterium dentium ATCC 27679, and functionally expressed in E. coli BL21(DE3). BfdABF1 showed the highest activity in 50 mM sodium acetate buffer at pH 5.0 and 25°C. This exo-enzyme could hydrolyze p-nitrophenyl arabinofuranoside, arabino-oligosaccharides (AOS), arabinoxylo-oligosaccharides (AXOS) such as 3²-α-L-arabinofuranosyl-xylobiose (A³X), and 2³-α-Larabinofuranosyl-xylotriose (A²XX), whereas hardly hydrolyzed polymeric substrates such as debranched arabinan and arabinoxylans. BfdABF1 is a typical exo-ABF with the higher specific activity on the oligomeric substrates than the polymers. It prefers

SUBMITTER: Lee MJ 

PROVIDER: S-EPMC9628843 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature