Two α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum are involved in arabinoxylan utilization.
Sign Up to like & getrecommendations! Published in 2022 at "Applied microbiology and biotechnology"
DOI: 10.1007/s00253-022-11845-x
Abstract: Arabinoxylan (AX) and arabinoxylooligosaccharides (AXOs) are carbohydrate sources utilized by Bifidobacterium longum subsp. longum. However, their degradation pathways are poorly understood. In this study, we characterized two genes, BLLJ_1850 and BLLJ_1851, in the hemicellulose-degrading gene… read more here.
Keywords: longum; subsp longum; longum subsp; gh43 ... See more keywords
GH43 endo-arabinanase from Bacillus licheniformis: Structure, activity and unexpected synergistic effect on cellulose enzymatic hydrolysis.
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DOI: 10.1016/j.ijbiomac.2018.05.157
Abstract: The hydrolysis of the plant biomass provides many interesting opportunities for the generation of building blocks for the green chemistry industrial applications. An important progress has been made for the hydrolysis of the cellulosic component… read more here.
Keywords: arabinanase bacillus; gh43; bacillus licheniformis; hydrolysis ... See more keywords
Mechanism of Cooperative Degradation of Gum Arabic Arabinogalactan Protein by Bifidobacterium longum Surface Enzymes
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DOI: 10.1128/aem.02187-21
Abstract: Terminal galactose residues of the side chain of gum arabic arabinogalactan protein (AGP) are mainly substituted by α1,3/α1,4-linked Araf and β1,6-linked α-l-Rhap-(1→4)-β-d-GlcpA residues. This study found a multidomain BlArafE with GH43_22 and GH43_34 catalytic domains… read more here.
Keywords: arabic agp; arabic arabinogalactan; gum arabic; longum ... See more keywords