Type

Journal Article

Authors

Douwe van Sinderen
Marco Gobbetti
Marco Ventura
Maria de Angelis
Amy O'Callaghan
Gabriele Andrea Lugli
Mary O'Connell Motherway
Raffaella Di Cagno
Jennifer Mahony
Erica Pontonio

Subjects

Microbiology

Topics
expression lactobacillus prebiotic functional properties lactic acid bacteria gut microbiota anti bacterial xylo oligosaccharides probiotic sourdough functional foods cloning amino acid sequence

Cloning, expression and characterization of a β-D-xylosidase from Lactobacillus rossiae DSM 15814(T). (2016)

Abstract Among 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 15814(T) 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. Genomic 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 15814(T) was also measured under sourdough conditions. This study highlights the ability of L. rossiae DSM 15814(T) to utilize XOS, which is a very useful trait when selecting starters with specific metabolic performances for sourdough fermentation or as probiotics.
Collections Ireland -> University College Cork -> APC Microbiome Institute
Ireland -> University College Cork -> PubMed
Ireland -> University College Cork -> College of Science, Engineering and Food Science
Ireland -> University College Cork -> APC Microbiome Institute- Journal Articles
Ireland -> University College Cork -> Microbiology
Ireland -> University College Cork -> Research Institutes and Centres
Ireland -> University College Cork -> Microbiology - Journal Articles

Full list of authors on original publication

Douwe van Sinderen, Marco Gobbetti, Marco Ventura, Maria de Angelis, Amy O'Callaghan, Gabriele Andrea Lugli, Mary O'Connell Motherway, Raffaella Di Cagno, Jennifer Mahony, Erica Pontonio

Experts in our system

1
Douwe van Sinderen
University College Cork
 
2
Marco Gobbetti
University College Cork
 
3
Marco Ventura
University College Cork
Total Publications: 31
 
4
Maria de Angelis
University College Cork
 
5
Amy O'Callaghan
University College Cork
Total Publications: 6
 
6
Gabriele A. Lugli
University College Cork
Total Publications: 17
 
7
Mary O'Connell Motherway
University College Cork
Total Publications: 16
 
8
Raffaella Di Cagno
University College Cork
 
9
Jennifer Mahony
University College Cork
Total Publications: 71
 
10
Erica Pontonio
University College Cork