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

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dc.contributor.author Pontonio, Erica
dc.contributor.author Mahony, Jennifer
dc.contributor.author Di Cagno, Raffaella
dc.contributor.author O'Connell Motherway, Mary
dc.contributor.author Lugli, Gabriele A.
dc.contributor.author O'Callaghan, Amy
dc.contributor.author De Angelis, Maria
dc.contributor.author Ventura, Marco
dc.contributor.author Gobbetti, Marco
dc.contributor.author van Sinderen, Douwe
dc.date.accessioned 2017-06-22T13:55:54Z
dc.date.available 2017-06-22T13:55:54Z
dc.date.issued 2016-05-03
dc.identifier.citation Pontonio, E., Mahony, J., Di Cagno, R., O’Connell Motherway, M., Lugli, G. A., O’Callaghan, A., De Angelis, M., Ventura, M., Gobbetti, M. and van Sinderen, D. (2016) 'Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814T', Microbial Cell Factories, 15, 72 (12pp). doi: 10.1186/s12934-016-0473-z en
dc.identifier.volume 15
dc.identifier.startpage 1
dc.identifier.endpage 12
dc.identifier.issn 1475-2859
dc.identifier.uri http://hdl.handle.net/10468/4177
dc.identifier.doi 10.1186/s12934-016-0473-z
dc.description.abstract Background: 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 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. Results: 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 15814T was also measured under sourdough conditions. Conclusions: This 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. en
dc.description.sponsorship Science Foundation Ireland (Irish Government’s National Development Plan (12/RC/2273; 13/IA/1953). en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher BioMed Central en
dc.relation.uri https://microbialcellfactories.biomedcentral.com/articles/10.1186/s12934-016-0473-z
dc.rights © 2016, Pontonio et al. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/ en
dc.subject Xylo-oligosaccharides en
dc.subject Sourdough en
dc.subject Prebiotic en
dc.subject Gut microbiota en
dc.subject Functional foods en
dc.subject Probiotic en
dc.title Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814T en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Douwe van Sinderen, Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: d.vansinderen@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Science Foundation Ireland
dc.description.status Peer reviewed en
dc.identifier.journaltitle Microbial Cell Factories en
dc.internal.IRISemailaddress d.vansinderen@ucc.ie en
dc.identifier.articleid 72


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© 2016, Pontonio et al. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. Except where otherwise noted, this item's license is described as © 2016, Pontonio et al. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
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