The Bifidobacterium adolescentis BAD_1527 gene encodes GH43_22 α-L-arabinofuranosidase of AXH-m type
Walid Fathallah, Vladimír Puchart

TL;DR
A gene in Bifidobacterium adolescentis encodes an enzyme that specifically breaks down certain plant sugars, but not others.
Contribution
The study clarifies the specific enzymatic activity of the BAD_1527 gene product as an α-L-arabinofuranosidase with AXH-m specificity.
Findings
The BAD_1527 gene product releases xylose only from artificial substrates, not natural ones.
The enzyme efficiently debranches arabinoxylan and branched arabinan but not doubly arabinosylated residues.
L-Arabinose is the only sugar released from natural substrates by the enzyme.
Abstract
Bifidobacterium adolescentis gene BAD_1527 has previously been suggested to code for a β-xylosidase (Kobayashi et al., Mar Drugs 18:174, 2020). Our detailed investigation of the substrate specificity of the GH43_22 protein using a wide spectrum of natural and artificial substrates showed that the enzyme hydrolyzed neither linear xylooligosaccharides nor glucuronoxylan. Xylose was released only from the artificial 4-nitrophenyl β-D-xylopyranoside (1.58 mU/mg). The corresponding α-L-arabinofuranoside was by three orders of magnitude better substrate (2.17 U/mg). Arabinose was the only monosaccharide liberated from arabinoxylan and α-1,3- or α-1,2-singly arabinosylated xylooligosaccharides. Moreover, the enzyme efficiently debranched sugar beet arabinan and singly arabinosylated α-1,5-L-arabinooligosaccharides, although short linear α-1,5-L-arabinooligosaccharides were also slowly…
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Taxonomy
TopicsMicrobial Metabolites in Food Biotechnology · Enzyme Production and Characterization · Digestive system and related health
