Mechanistic insights into the structure-dependant and strain-specific utilization of wheat arabinoxylan by Bifidobacterium longum

被引:25
|
作者
Song, Ang-Xin [1 ]
Li, Long-Qing [1 ]
Yin, Jun-Yi [2 ]
Chiou, Jia-Chi [1 ]
Wu, Jian-Yong [1 ]
机构
[1] Hong Kong Polytech Univ, Food Safety & Technol Res Ctr, Dept Appl Biol & Chem Technol, Hung Hom,Kowloon, Hong Kong, Peoples R China
[2] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China
关键词
Bifidobacteria; Arabinoxylan; Molecular weight; Degradation mechanism; Strain-specific; Structure-dependence; Genomic analysis; INTESTINAL MICROBIOTA; GENOME SEQUENCE; OLIGOSACCHARIDES; FERMENTATION; DEGRADATION; PURIFICATION; HYDROLYSIS; ULTRASOUND; H-1-NMR; COLON;
D O I
10.1016/j.carbpol.2020.116886
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Arabinoxylan (AX), an important dietary fiber from cereal grains, is mainly metabolised in the large intestine by gut bacteria, especially bifidobacteria. This study investigated the uptake and metabolism of wheat AX by a Bifidobacterium longum strain that could grow well with AX as the sole carbon source. The bacterial growth rate showed a significant correlation to the molecular weight (MW) of AX and its acid hydrolysates. Assessment of the key AX degrading enzymes suggested that the uptake and consumption of AX involved extracellular cleavage of xylan backbone and intracellular degradation of both the backbone and the arabinose substitution. The preference for native or partially hydrolysed AX with single substitutions and a sufficiently high MW suggested the structure-dependant uptake by the bacterial cells. Genetic analysis of B. longum showed the lack of beta-xylosidase, suggesting the existence of unknown enzymes or dual/multiple-specific enzymes for hydrolysis of the nonreducing end of xylan backbone.
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页数:9
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