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Gotoh et al. Microbiome Res Rep 2023;2:20 Microbiome Research
DOI: 10.20517/mrr.2023.14
Reports

Original Article Open Access

Substrate recognition mode of a glycoside
hydrolase family 42 β-galactosidase from

Bifidobacterium longum subspecies infantis
(BiBga42A) revealed by crystallographic and

mutational analyses

1,2
3
2
4,5
4
Aina Gotoh , Masafumi Hidaka , Haruko Sakurama , Mamoru Nishimoto , Motomitsu Kitaoka , Mikiyasu
1
6
Sakanaka , Shinya Fushinobu , Takane Katayama 1,2
1
Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
2
Ishikawa Prefectural University, Nonoichi, Ishikawa 921-8836, Japan.
3
Graduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 980-8572, Japan.
4
Institute of Food Research, National Agriculture and Food Research Organization, Tsukuba, Ibaraki 305-8642, Japan.
5
Faculty of Agriculture, Niigata University, Niigata 950-2102, Japan.
6
Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
Correspondence to: Takane Katayama, Graduate School of Biostudies, Kyoto University, Kitashirakawa Sakyo-ku, Kyoto 606-
8502, Japan. E-mail: takane@lif.kyoto-u.ac.jp; Shinya Fushinobu, Department of Biotechnology, The University of Tokyo, Hongo
Bunkyo-ku, Tokyo 113-8657, Japan. E-mail: asfushi@mail.ecc.u-tokyo.ac.jp
How to cite this article: Gotoh A, Hidaka M, Sakurama H, Nishimoto M, Kitaoka M, Sakanaka M, Fushinobu S, Katayama T.
Substrate recognition mode of a glycoside hydrolase family 42 β-galactosidase from Bifidobacterium longum subspecies infantis
(BiBga42A) revealed by crystallographic and mutational analyses. Microbiome Res Rep 2023;2:20.
https://dx.doi.org/10.20517/mrr.2023.14
Received: 21 Feb 2023 First Decision: Ap 19 2023 Revised: May 2 2023 Accepted: May 9 2023 Published: 26 May 2023
Academic Editor: Christian Milani Copy Editor: Dong-Li Li Production Editor: Dong-Li Li
Abstract
Aim: Bifidobacterium longum subsp. infantis uses a glycoside hydrolase (GH) family 42 β-galactosidase (BiBga42A)
for hydrolyzing lacto-N-tetraose (LNT), which is the most abundant core structure of human milk oligosaccharides
(HMOs). As such, BiBga42A represents one of the pivotal enzymes underpinning the symbiosis between
bifidobacteria and breastfed infants. Despite its importance, the structural basis underlying LNT hydrolysis by Bi
Bga42A is not understood. Moreover, no substrate-complexed structures are available to date for GH42 family
members.

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