Two Novel α- l -Arabinofuranosidases from Bifidobacterium longum subsp. longum Belonging to Glycoside Hydrolase Family 43 Cooperatively Degrade Arabinan
Author(s) -
Masahiro Komeno,
Honoka Hayamizu,
Kiyotaka Fujita,
Hisashi Ashida
Publication year - 2019
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.02582-18
Subject(s) - bifidobacterium longum , glycoside hydrolase , enzyme , biology , gene cluster , biochemistry , extracellular , bifidobacterium , actinomycetaceae , gene , chemistry , fermentation , lactobacillus
We identified two novel α-l -arabinofuranosidases, BlArafC and BlArafB, fromB. longum subsp.longum JCM 1217, both of which are predicted to be extracellular membrane-bound enzymes. The former specifically acts on α1,2/3-l -arabinofuranosyl linkages, while the latter acts on the α1,5-l -arabinofuranosyl linkage. These enzymes cooperatively degrade arabinan and are required for the efficient growth of bifidobacteria in arabinan-containing medium. The genes encoding these enzymes are located side by side in a gene cluster involved in metabolic pathways for plant-derived polysaccharides, which may confer adaptability in adult intestines.
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