Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814T

Microbial Cell Factories

Research

Maria De Angelis¹  Raffaella Di Cagno¹  Erica Pontonio¹  Marco Gobbetti¹  Gabriele Andrea Lugli²  Marco Ventura²  Jennifer Mahony³  Mary O’Connell Motherway⁴  Amy O’Callaghan⁴  Douwe van Sinderen⁴ 

[1] Department of Soil, Plant and Food Science, University of Bari Aldo Moro, Via G. Amendola 165/A, 70126, Bari, Italy;Laboratory of Probiogenomics, Department of Life Sciences, University of Parma, Parma, Italy;School of Microbiology, University College Cork, Cork, Ireland;School of Microbiology, University College Cork, Cork, Ireland;Alimentary Pharmabiotic Centre, University College Cork, Cork, Ireland;

关键词: Xylo-oligosaccharides;    Sourdough;    Prebiotic;    Gut microbiota;    Functional foods;    Probiotic;   

DOI  :  10.1186/s12934-016-0473-z

 received in 2016-02-10, accepted in 2016-04-24,  发布年份 2016

来源: Springer

【 摘 要 】

BackgroundAmong the oligosaccharides that may positively affect the gut microbiota, xylo-oligosaccharides (XOS) and arabinoxylan oligosaccharides (AXOS) possess promising functional properties. Ingestion of XOS has been reported to contribute to anti-oxidant, anti-bacterial, immune-modulatory and anti-diabetic activities. Because of the structural complexity and chemical heterogeneity, complete degradation of xylan-containing plant polymers requires the synergistic activity of several enzymes. Endo-xylanases and β-d-xylosidases, collectively termed xylanases, represent the two key enzymes responsible for the sequential hydrolysis of xylan. Xylanase cocktails are used on an industrial scale for biotechnological purposes. Lactobacillus rossiae DSM 15814T can utilize an extensive set of carbon sources, an ability that is likely to contribute to its adaptive ability. In this study, the capacity of this strain to utilize XOS, xylan, d-xylose and l-arabinose was investigated.ResultsGenomic and transcriptomic analyses revealed the presence of two gene clusters, designated xyl and ara, encoding proteins predicted to be responsible for XOS uptake and hydrolysis and d-xylose utilization, and l-arabinose metabolism, respectively. The deduced amino acid sequence of one of the genes of the xyl gene cluster, LROS_1108 (designated here as xylA), shows high similarity to (predicted) β-d-xylosidases encoded by various lactic acid bacteria, and belongs to glycosyl hydrolase family 43. Heterologously expressed XylA was shown to completely hydrolyse XOS to xylose and showed optimal activity at pH 6.0 and 40 °C. Furthermore, β-d-xylosidase activity of L. rossiae DSM 15814T was also measured under sourdough conditions.ConclusionsThis study highlights the ability of L. rossiae DSM 15814T to utilize XOS, which is a very useful trait when selecting starters with specific metabolic performances for sourdough fermentation or as probiotics.

【 授权许可】

CC BY   
© Pontonio et al. 2016