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Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum

BACKGROUND: Tannases are tannin-degrading enzymes that have been described in fungi and bacteria as an adaptative mechanism to overcome the stress conditions associated with the presence of these phenolic compounds. RESULTS: We have identified and expressed in E. coli a tannase from the oral microbi...

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Autores principales: Tomás-Cortázar, Julen, Plaza-Vinuesa, Laura, de las Rivas, Blanca, Lavín, José Luis, Barriales, Diego, Abecia, Leticia, Mancheño, José Miguel, Aransay, Ana M., Muñoz, Rosario, Anguita, Juan, Rodríguez, Héctor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5828091/
https://www.ncbi.nlm.nih.gov/pubmed/29482557
http://dx.doi.org/10.1186/s12934-018-0880-4
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author Tomás-Cortázar, Julen
Plaza-Vinuesa, Laura
de las Rivas, Blanca
Lavín, José Luis
Barriales, Diego
Abecia, Leticia
Mancheño, José Miguel
Aransay, Ana M.
Muñoz, Rosario
Anguita, Juan
Rodríguez, Héctor
author_facet Tomás-Cortázar, Julen
Plaza-Vinuesa, Laura
de las Rivas, Blanca
Lavín, José Luis
Barriales, Diego
Abecia, Leticia
Mancheño, José Miguel
Aransay, Ana M.
Muñoz, Rosario
Anguita, Juan
Rodríguez, Héctor
author_sort Tomás-Cortázar, Julen
collection PubMed
description BACKGROUND: Tannases are tannin-degrading enzymes that have been described in fungi and bacteria as an adaptative mechanism to overcome the stress conditions associated with the presence of these phenolic compounds. RESULTS: We have identified and expressed in E. coli a tannase from the oral microbiota member Fusobacterium nucleatum subs. polymorphum (TanB(Fnp)). TanB(Fnp) is the first tannase identified in an oral pathogen. Sequence analyses revealed that it is closely related to other bacterial tannases. The enzyme exhibits biochemical properties that make it an interesting target for industrial use. TanB(Fnp) has one of the highest specific activities of all bacterial tannases described to date and shows optimal biochemical properties such as a high thermal stability: the enzyme keeps 100% of its activity after prolonged incubations at different temperatures up to 45 °C. TanB(Fnp) also shows a wide temperature range of activity, maintaining above 80% of its maximum activity between 22 and 55 °C. The use of a panel of 27 esters of phenolic acids demonstrated activity of TanB(Fnp) only against esters of gallic and protocatechuic acid, including tannic acid, gallocatechin gallate and epigallocatechin gallate. Overall, TanB(Fnp) possesses biochemical properties that make the enzyme potentially useful in biotechnological applications. CONCLUSIONS: We have identified and characterized a metabolic enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum. The biochemical properties of TanB(Fnp) suggest that it has a major role in the breakdown of complex food tannins during oral processing. Our results also provide some clues regarding its possible participation on bacterial survival in the oral cavity. Furthermore, the characteristics of this enzyme make it of potential interest for industrial use. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12934-018-0880-4) contains supplementary material, which is available to authorized users.
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spelling pubmed-58280912018-02-28 Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum Tomás-Cortázar, Julen Plaza-Vinuesa, Laura de las Rivas, Blanca Lavín, José Luis Barriales, Diego Abecia, Leticia Mancheño, José Miguel Aransay, Ana M. Muñoz, Rosario Anguita, Juan Rodríguez, Héctor Microb Cell Fact Research BACKGROUND: Tannases are tannin-degrading enzymes that have been described in fungi and bacteria as an adaptative mechanism to overcome the stress conditions associated with the presence of these phenolic compounds. RESULTS: We have identified and expressed in E. coli a tannase from the oral microbiota member Fusobacterium nucleatum subs. polymorphum (TanB(Fnp)). TanB(Fnp) is the first tannase identified in an oral pathogen. Sequence analyses revealed that it is closely related to other bacterial tannases. The enzyme exhibits biochemical properties that make it an interesting target for industrial use. TanB(Fnp) has one of the highest specific activities of all bacterial tannases described to date and shows optimal biochemical properties such as a high thermal stability: the enzyme keeps 100% of its activity after prolonged incubations at different temperatures up to 45 °C. TanB(Fnp) also shows a wide temperature range of activity, maintaining above 80% of its maximum activity between 22 and 55 °C. The use of a panel of 27 esters of phenolic acids demonstrated activity of TanB(Fnp) only against esters of gallic and protocatechuic acid, including tannic acid, gallocatechin gallate and epigallocatechin gallate. Overall, TanB(Fnp) possesses biochemical properties that make the enzyme potentially useful in biotechnological applications. CONCLUSIONS: We have identified and characterized a metabolic enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum. The biochemical properties of TanB(Fnp) suggest that it has a major role in the breakdown of complex food tannins during oral processing. Our results also provide some clues regarding its possible participation on bacterial survival in the oral cavity. Furthermore, the characteristics of this enzyme make it of potential interest for industrial use. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12934-018-0880-4) contains supplementary material, which is available to authorized users. BioMed Central 2018-02-26 /pmc/articles/PMC5828091/ /pubmed/29482557 http://dx.doi.org/10.1186/s12934-018-0880-4 Text en © The Author(s) 2018 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
Tomás-Cortázar, Julen
Plaza-Vinuesa, Laura
de las Rivas, Blanca
Lavín, José Luis
Barriales, Diego
Abecia, Leticia
Mancheño, José Miguel
Aransay, Ana M.
Muñoz, Rosario
Anguita, Juan
Rodríguez, Héctor
Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum
title Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum
title_full Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum
title_fullStr Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum
title_full_unstemmed Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum
title_short Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum
title_sort identification of a highly active tannase enzyme from the oral pathogen fusobacterium nucleatum subsp. polymorphum
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5828091/
https://www.ncbi.nlm.nih.gov/pubmed/29482557
http://dx.doi.org/10.1186/s12934-018-0880-4
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