Bacterial tannases: classification and biochemical properties
Tannin acyl hydrolases, also known as tannases, are a group of enzymes critical for the transformation of tannins. The study of these enzymes, which initially evolved in different organisms to detoxify and/or use these plant metabolites, has nowadays become relevant in microbial enzymology research due to their relevant role in food tannin transformation. Microorganisms, particularly bacteria, are major sources of tannase. Cloning and heterologous expression of bacterial tannase genes and structural studies have been performed in the last few years. However, a systematic compilation of the information related to all recombinant tannases, their classification, and characteristics is missing. In this review, we explore the diversity of heterologously produced bacterial tannases, describing their substrate specificity and biochemical characterization. Moreover, a new classification based on sequence similarity analysis is proposed. Finally, putative tannases have been identified in silico for each group of tannases taking advantage of the use of the "tannase" distinctive features previously proposed.
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Format: | artículo biblioteca |
Language: | English |
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Springer Nature
2019
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Subjects: | Esterase, Feruloyl esterase, Gallic acid, Hydrolyzable tannins, |
Online Access: | http://hdl.handle.net/10261/203317 http://dx.doi.org/10.13039/501100010198 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100000780 |
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dig-ictan-es-10261-2033172021-06-30T07:49:08Z Bacterial tannases: classification and biochemical properties Rivas, Blanca de las Rodríguez, Héctor Anguita, Juan Muñoz, Rosario Ministerio de Economía, Industria y Competitividad (España) Ministerio de Economía y Competitividad (España) European Commission Esterase Feruloyl esterase Gallic acid Hydrolyzable tannins Tannin acyl hydrolases, also known as tannases, are a group of enzymes critical for the transformation of tannins. The study of these enzymes, which initially evolved in different organisms to detoxify and/or use these plant metabolites, has nowadays become relevant in microbial enzymology research due to their relevant role in food tannin transformation. Microorganisms, particularly bacteria, are major sources of tannase. Cloning and heterologous expression of bacterial tannase genes and structural studies have been performed in the last few years. However, a systematic compilation of the information related to all recombinant tannases, their classification, and characteristics is missing. In this review, we explore the diversity of heterologously produced bacterial tannases, describing their substrate specificity and biochemical characterization. Moreover, a new classification based on sequence similarity analysis is proposed. Finally, putative tannases have been identified in silico for each group of tannases taking advantage of the use of the "tannase" distinctive features previously proposed. This work was financially supported by grants AGL2014-52911-R and SAF2015-73549-JIN from the Spanish Ministry of Economy and Competitiveness/FEDR-MINEICO. Peer reviewed 2020-03-10T07:47:48Z 2020-03-10T07:47:48Z 2019 artículo http://purl.org/coar/resource_type/c_6501 Applied Microbiology and Biotechnology 103: 603-623 (2019) 0175-7598 http://hdl.handle.net/10261/203317 10.1007/s00253-018-9519-y 1432-0614 http://dx.doi.org/10.13039/501100010198 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100000780 30460533 en #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2014-52911-R info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2015-73549-JIN Postprint https://doi.org/10.1007/s00253-018-9519-y Sí open Springer Nature |
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Esterase Feruloyl esterase Gallic acid Hydrolyzable tannins Esterase Feruloyl esterase Gallic acid Hydrolyzable tannins |
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Esterase Feruloyl esterase Gallic acid Hydrolyzable tannins Esterase Feruloyl esterase Gallic acid Hydrolyzable tannins Rivas, Blanca de las Rodríguez, Héctor Anguita, Juan Muñoz, Rosario Bacterial tannases: classification and biochemical properties |
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Tannin acyl hydrolases, also known as tannases, are a group of enzymes critical for the transformation of tannins. The study of these enzymes, which initially evolved in different organisms to detoxify and/or use these plant metabolites, has nowadays become relevant in microbial enzymology research due to their relevant role in food tannin transformation. Microorganisms, particularly bacteria, are major sources of tannase. Cloning and heterologous expression of bacterial tannase genes and structural studies have been performed in the last few years. However, a systematic compilation of the information related to all recombinant tannases, their classification, and characteristics is missing. In this review, we explore the diversity of heterologously produced bacterial tannases, describing their substrate specificity and biochemical characterization. Moreover, a new classification based on sequence similarity analysis is proposed. Finally, putative tannases have been identified in silico for each group of tannases taking advantage of the use of the "tannase" distinctive features previously proposed. |
author2 |
Ministerio de Economía, Industria y Competitividad (España) |
author_facet |
Ministerio de Economía, Industria y Competitividad (España) Rivas, Blanca de las Rodríguez, Héctor Anguita, Juan Muñoz, Rosario |
format |
artículo |
topic_facet |
Esterase Feruloyl esterase Gallic acid Hydrolyzable tannins |
author |
Rivas, Blanca de las Rodríguez, Héctor Anguita, Juan Muñoz, Rosario |
author_sort |
Rivas, Blanca de las |
title |
Bacterial tannases: classification and biochemical properties |
title_short |
Bacterial tannases: classification and biochemical properties |
title_full |
Bacterial tannases: classification and biochemical properties |
title_fullStr |
Bacterial tannases: classification and biochemical properties |
title_full_unstemmed |
Bacterial tannases: classification and biochemical properties |
title_sort |
bacterial tannases: classification and biochemical properties |
publisher |
Springer Nature |
publishDate |
2019 |
url |
http://hdl.handle.net/10261/203317 http://dx.doi.org/10.13039/501100010198 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100000780 |
work_keys_str_mv |
AT rivasblancadelas bacterialtannasesclassificationandbiochemicalproperties AT rodriguezhector bacterialtannasesclassificationandbiochemicalproperties AT anguitajuan bacterialtannasesclassificationandbiochemicalproperties AT munozrosario bacterialtannasesclassificationandbiochemicalproperties |
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1777670636110348288 |