Two α-l-arabinofuranosidases from Bifidobacterium longum subsp. longum are involved in arabinoxylan utilization
Author:
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
https://link.springer.com/content/pdf/10.1007/s00253-022-11845-x.pdf
Reference25 articles.
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2. Arboleya S, Bottacini F, O’Connell-Motherway M, Ryan CA, Ross RP, van Sinderen D, Stanton C (2018) Gene-trait matching across the Bifidobacterium longum pan-genome reveals considerable diversity in carbohydrate catabolism among human infant strains. BMC Genomics 19:33. https://doi.org/10.1186/s12864-017-4388-9
3. Ashida H, Maki R, Ozawa H, Tani Y, Kiyohara M, Fujita M, Imamura A, Ishida H, Kiso M, Yamamoto K (2008) Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. Glycobiology 18:727–734. https://doi.org/10.1093/glycob/cwn053
4. Fujita K, Kitahara K, Suganuma T (2012) Functional analysis of degradative enzymes for hydroxyproline-linked β-l-arabinofuranosides in Bifidobacterium longum. Trends Glycosci Glycotechnol 24:215–224. https://doi.org/10.4052/tigg.24.215
5. Fujita K, Oura F, Nagamine N, Katayama T, Hiratake J, Sakata K, Kumagai H, Yamamoto K (2005) Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J Biol Chem 280:37415–37422. https://doi.org/10.1074/jbc.M506874200
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