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The Bifidobacterium adolescentis BAD_1527 gene encodes GH43_22 α-L-arabinofuranosidase of AXH-m type.

Authors :
Fathallah, Walid
Puchart, Vladimír
Source :
AMB Express. 7/20/2024, Vol. 14 Issue 1, p1-9. 9p.
Publication Year :
2024

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 degraded. On the other hand, debranched arabinan, arabinogalactan as well as 2,3-doubly arabinosylated main chain residues of arabinan and arabinoxylan did not serve as substrates. Thus, the enzyme encoded by the BAD_1527 gene is a typical α-L-arabinofuranosidase of AXH-m specificity. Key points: BAD_1527 gene encodes a protein releasing xylose from NPX, but not natural substrates L-Arabinose is released from natural substrates, similarly to other GH43_22 members The enzyme debranches arabinoxylan, branched arabinan and derived oligosaccharides [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
21910855
Volume :
14
Issue :
1
Database :
Academic Search Index
Journal :
AMB Express
Publication Type :
Academic Journal
Accession number :
178530290
Full Text :
https://doi.org/10.1186/s13568-024-01738-9