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

Simple item page
dc.contributor.authorPontonio, Erica
dc.contributor.authorMahony, Jennifer
dc.contributor.authorDi Cagno, Raffaella
dc.contributor.authorO'Connell Motherway, Mary
dc.contributor.authorLugli, Gabriele A.
dc.contributor.authorO'Callaghan, Amy
dc.contributor.authorDe Angelis, Maria
dc.contributor.authorVentura, Marco
dc.contributor.authorGobbetti, Marco
dc.contributor.authorvan Sinderen, Douwe
dc.contributor.funderScience Foundation Ireland
dc.date.accessioned2017-06-22T13:55:54Z
dc.date.available2017-06-22T13:55:54Z
dc.date.issued2016-05-03
dc.description.abstractBackground: 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.sponsorshipScience Foundation Ireland (Irish Government’s National Development Plan (12/RC/2273; 13/IA/1953).en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid72
dc.identifier.citationPontonio, 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-zen
dc.identifier.doi10.1186/s12934-016-0473-z
dc.identifier.endpage12
dc.identifier.issn1475-2859
dc.identifier.journaltitleMicrobial Cell Factoriesen
dc.identifier.startpage1
dc.identifier.urihttps://hdl.handle.net/10468/4177
dc.identifier.volume15
dc.language.isoenen
dc.publisherBioMed Centralen
dc.relation.urihttps://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.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectXylo-oligosaccharidesen
dc.subjectSourdoughen
dc.subjectPrebioticen
dc.subjectGut microbiotaen
dc.subjectFunctional foodsen
dc.subjectProbioticen
dc.titleCloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814Ten
dc.typeArticle (peer-reviewed)en
Files
Original bundle
Now showing 1 - 2 of 2
Thumbnail Image
Name:
3038.pdf
Size:
1.28 MB
Format:
Adobe Portable Document Format
Description:
Published Version
Download
Thumbnail Image
Name:
3038-1.pdf
Size:
46.62 KB
Format:
Adobe Portable Document Format
Description:
Supplementary File 1
Download
Collections
Microbiology - Journal Articles
APC Microbiome Ireland - Journal Articles