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Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T)
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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855831/ https://www.ncbi.nlm.nih.gov/pubmed/27142164 http://dx.doi.org/10.1186/s12934-016-0473-z |
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author | Pontonio, Erica Mahony, Jennifer Di Cagno, Raffaella O’Connell Motherway, Mary Lugli, Gabriele Andrea O’Callaghan, Amy De Angelis, Maria Ventura, Marco Gobbetti, Marco van Sinderen, Douwe |
author_facet | Pontonio, Erica Mahony, Jennifer Di Cagno, Raffaella O’Connell Motherway, Mary Lugli, Gabriele Andrea O’Callaghan, Amy De Angelis, Maria Ventura, Marco Gobbetti, Marco van Sinderen, Douwe |
author_sort | Pontonio, Erica |
collection | PubMed |
description | 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 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. 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 15814(T) was also measured under sourdough conditions. CONCLUSIONS: 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12934-016-0473-z) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4855831 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-48558312016-05-05 Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T) Pontonio, Erica Mahony, Jennifer Di Cagno, Raffaella O’Connell Motherway, Mary Lugli, Gabriele Andrea O’Callaghan, Amy De Angelis, Maria Ventura, Marco Gobbetti, Marco van Sinderen, Douwe Microb Cell Fact Research 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 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. 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 15814(T) was also measured under sourdough conditions. CONCLUSIONS: 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12934-016-0473-z) contains supplementary material, which is available to authorized users. BioMed Central 2016-05-03 /pmc/articles/PMC4855831/ /pubmed/27142164 http://dx.doi.org/10.1186/s12934-016-0473-z Text en © Pontonio et al. 2016 Open AccessThis 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. |
spellingShingle | Research Pontonio, Erica Mahony, Jennifer Di Cagno, Raffaella O’Connell Motherway, Mary Lugli, Gabriele Andrea O’Callaghan, Amy De Angelis, Maria Ventura, Marco Gobbetti, Marco van Sinderen, Douwe Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T) |
title | Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T) |
title_full | Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T) |
title_fullStr | Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T) |
title_full_unstemmed | Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T) |
title_short | Cloning, expression and characterization of a β-d-xylosidase from Lactobacillus rossiae DSM 15814(T) |
title_sort | cloning, expression and characterization of a β-d-xylosidase from lactobacillus rossiae dsm 15814(t) |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855831/ https://www.ncbi.nlm.nih.gov/pubmed/27142164 http://dx.doi.org/10.1186/s12934-016-0473-z |
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