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Sasaki et al. Microbiome Res Rep 2023;2:12 Microbiome Research
DOI: 10.20517/mrr.2023.08
Reports

Original Article Open Access

Assimilation of arabinogalactan side chains with
novel 3-O-β-L-arabinopyranosyl-α-L-

arabinofuranosidase in Bifidobacterium
pseudocatenulatum

1
1
3
3
1,2
Yuki Sasaki , Makoto Yanagita , Mimika Hashiguchi , Ayako Horigome , Jin-Zhong Xiao , Toshitaka
3
1
Odamaki , Kanefumi Kitahara , Kiyotaka Fujita 1
1
Faculty of Agriculture, Kagoshima University, Kagoshima, Kagoshima 890-0065, Japan.
2
Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
3
Next Generation Science Institute, Morinaga Milk Industry Co. Ltd., Zama, Kanagawa 252-8583, Japan.
Correspondence to: Prof. Kiyotaka Fujita. Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto,
Kagoshima 890-0065, Japan. E-mail: k4022897@kadai.jp
How to cite this article: Sasaki Y, Yanagita M, Hashiguchi M, Horigome A, Xiao JZ, Odamaki T, Kitahara K, Fujita K. Assimilation
of arabinogalactan side chains with novel 3-O-β-L-arabinopyranosyl-α-L-arabinofuranosidase in Bifidobacterium
pseudocatenulatum. Microbiome Res Rep 2023;2:12. https://dx.doi.org/10.20517/mrr.2023.08
Received: 24 Jan 2023 First Decision:2 Mar 2023 Revised: 19 Mar 2023 Accepted: 6 Apr 2023 Published: 19 Apr 2023
Academic Editor: Francesca Turroni Copy Editor: Yanbing Bai Production Editor: Yanbing Bai

Abstract
Aim: Dietary plant fibers affect gut microbiota composition; however, the underlying microbial degradation
pathways are not fully understood. We previously discovered 3-O-α-D-galactosyl-α-L-arabinofuranosidase
(GAfase), a glycoside hydrolase family 39 enzyme involved in the assimilation of side chains of arabinogalactan
protein (AGP), from Bifidobacterium longum subsp. longum (B. longum) JCM7052. Although GAfase homologs are
not highly prevalent in the Bifidobacterium genus, several Bifidobacterium strains possess the homologs. To explore
the differences in substrate specificity among the homologs, a homolog of B. longum GAfase in Bifidobacterium
pseudocatenulatum MCC10289 (MCC10289_0425) was characterized.
Methods: Gum arabic, larch, wheat AGP, and sugar beet arabinan were used to determine the substrate specificity
of the MCC10289_0425 protein. An amino acid replacement was introduced into GAfase to identify a critical
residue that governs the differentiation of substrate specificity. The growth of several Bifidobacterium strains on β-
L-arabinopyranosyl disaccharide and larch AGP was examined.

© The Author(s) 2023. Open Access This article is licensed under a Creative Commons Attribution 4.0
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