Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1186/1754-6834-4-50 http://hdl.handle.net/11449/20011 |
Resumo: | Background: Lignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource. However, saccharification and the production of bioproducts derived from plant cell wall biomass are complex and lengthy processes. The understanding of termite gut biology and feeding strategies may improve the current state of biomass conversion technology and bioproduct production.Results: The study herein shows comprehensive functional characterization of crude body extracts from Coptotermes gestroi along with global proteomic analysis of the termite's digestome, targeting the identification of glycoside hydrolases and accessory proteins responsible for plant biomass conversion. The crude protein extract from C. gestroi was enzymatically efficient over a broad pH range on a series of natural polysaccharides, formed by glucose-, xylose-, mannan- and/or arabinose-containing polymers, linked by various types of glycosidic bonds, as well as ramification types. Our proteomic approach successfully identified a large number of relevant polypeptides in the C. gestroi digestome. A total of 55 different proteins were identified and classified into 29 CAZy families. Based on the total number of peptides identified, the majority of components found in the C. gestroi digestome were cellulose-degrading enzymes. Xylanolytic enzymes, mannan-hydrolytic enzymes, pectinases and starch-degrading and debranching enzymes were also identified. Our strategy enabled validation of liquid chromatography with tandem mass spectrometry recognized proteins, by enzymatic functional assays and by following the degradation products of specific 8-amino-1,3,6-pyrenetrisulfonic acid labeled oligosaccharides through capillary zone electrophoresis.Conclusions: Here we describe the first global study on the enzymatic repertoire involved in plant polysaccharide degradation by the lower termite C. gestroi. The biochemical characterization of whole body termite extracts evidenced their ability to cleave all types of glycosidic bonds present in plant polysaccharides. The comprehensive proteomic analysis, revealed a complete collection of hydrolytic enzymes including cellulases (GH1, GH3, GH5, GH7, GH9 and CBM 6), hemicellulases (GH2, GH10, GH11, GH16, GH43 and CBM 27) and pectinases (GH28 and GH29). |
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Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroiBackground: Lignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource. However, saccharification and the production of bioproducts derived from plant cell wall biomass are complex and lengthy processes. The understanding of termite gut biology and feeding strategies may improve the current state of biomass conversion technology and bioproduct production.Results: The study herein shows comprehensive functional characterization of crude body extracts from Coptotermes gestroi along with global proteomic analysis of the termite's digestome, targeting the identification of glycoside hydrolases and accessory proteins responsible for plant biomass conversion. The crude protein extract from C. gestroi was enzymatically efficient over a broad pH range on a series of natural polysaccharides, formed by glucose-, xylose-, mannan- and/or arabinose-containing polymers, linked by various types of glycosidic bonds, as well as ramification types. Our proteomic approach successfully identified a large number of relevant polypeptides in the C. gestroi digestome. A total of 55 different proteins were identified and classified into 29 CAZy families. Based on the total number of peptides identified, the majority of components found in the C. gestroi digestome were cellulose-degrading enzymes. Xylanolytic enzymes, mannan-hydrolytic enzymes, pectinases and starch-degrading and debranching enzymes were also identified. Our strategy enabled validation of liquid chromatography with tandem mass spectrometry recognized proteins, by enzymatic functional assays and by following the degradation products of specific 8-amino-1,3,6-pyrenetrisulfonic acid labeled oligosaccharides through capillary zone electrophoresis.Conclusions: Here we describe the first global study on the enzymatic repertoire involved in plant polysaccharide degradation by the lower termite C. gestroi. The biochemical characterization of whole body termite extracts evidenced their ability to cleave all types of glycosidic bonds present in plant polysaccharides. The comprehensive proteomic analysis, revealed a complete collection of hydrolytic enzymes including cellulases (GH1, GH3, GH5, GH7, GH9 and CBM 6), hemicellulases (GH2, GH10, GH11, GH16, GH43 and CBM 27) and pectinases (GH28 and GH29).Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Univ Estadual Campinas, Genet Evolut & Bioagents Dept, LGE, Campinas, SP, BrazilCNPEM, Lab Nacl Cencia & Tecnol Bioetanol CTBE, Campinas, SP, BrazilUniv Estadual Campinas, Hematol & Hemotherapy Ctr, Campinas, SP, BrazilUniv Estadual Paulista UNESP, Inst Biocencias, Dept Biol, Rio Claro, BrazilCNPEM, Lab Nacl Biociencias LNBio, Campinas, SP, BrazilUniv Estadual Paulista UNESP, Inst Biocencias, Dept Biol, Rio Claro, BrazilFAPESP: 08/50114-4FAPESP: 08/58037-9FAPESP: 06/59086-8FAPESP: 10/11469-1Biomed Central Ltd.Universidade Estadual de Campinas (UNICAMP)CNPEMUniversidade Estadual Paulista (Unesp)Franco Cairo, Joao Paulo L.Leonardo, Flavia C.Alvarez, Thabata M.Ribeiro, Daniela A.Buechli, FernandaCosta-Leonardo, Ana M. [UNESP]Carazzolle, Marcelo F.Costa, Fernando F.Paes Leme, Adriana F.Pereira, Goncalo A. G.Squina, Fabio M.2014-05-20T13:55:54Z2014-05-20T13:55:54Z2011-11-14info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10application/pdfhttp://dx.doi.org/10.1186/1754-6834-4-50Biotechnology For Biofuels. London: Biomed Central Ltd., v. 4, p. 10, 2011.1754-6834http://hdl.handle.net/11449/2001110.1186/1754-6834-4-50WOS:000300718400001WOS000300718400001.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiotechnology for Biofuels5.4971,899info:eu-repo/semantics/openAccess2023-12-01T06:18:53Zoai:repositorio.unesp.br:11449/20011Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-01T06:18:53Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi |
title |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi |
spellingShingle |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi Franco Cairo, Joao Paulo L. |
title_short |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi |
title_full |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi |
title_fullStr |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi |
title_full_unstemmed |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi |
title_sort |
Functional characterization and target discovery of glycoside hydrolases from the digestome of the lower termite Coptotermes gestroi |
author |
Franco Cairo, Joao Paulo L. |
author_facet |
Franco Cairo, Joao Paulo L. Leonardo, Flavia C. Alvarez, Thabata M. Ribeiro, Daniela A. Buechli, Fernanda Costa-Leonardo, Ana M. [UNESP] Carazzolle, Marcelo F. Costa, Fernando F. Paes Leme, Adriana F. Pereira, Goncalo A. G. Squina, Fabio M. |
author_role |
author |
author2 |
Leonardo, Flavia C. Alvarez, Thabata M. Ribeiro, Daniela A. Buechli, Fernanda Costa-Leonardo, Ana M. [UNESP] Carazzolle, Marcelo F. Costa, Fernando F. Paes Leme, Adriana F. Pereira, Goncalo A. G. Squina, Fabio M. |
author2_role |
author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual de Campinas (UNICAMP) CNPEM Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Franco Cairo, Joao Paulo L. Leonardo, Flavia C. Alvarez, Thabata M. Ribeiro, Daniela A. Buechli, Fernanda Costa-Leonardo, Ana M. [UNESP] Carazzolle, Marcelo F. Costa, Fernando F. Paes Leme, Adriana F. Pereira, Goncalo A. G. Squina, Fabio M. |
description |
Background: Lignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource. However, saccharification and the production of bioproducts derived from plant cell wall biomass are complex and lengthy processes. The understanding of termite gut biology and feeding strategies may improve the current state of biomass conversion technology and bioproduct production.Results: The study herein shows comprehensive functional characterization of crude body extracts from Coptotermes gestroi along with global proteomic analysis of the termite's digestome, targeting the identification of glycoside hydrolases and accessory proteins responsible for plant biomass conversion. The crude protein extract from C. gestroi was enzymatically efficient over a broad pH range on a series of natural polysaccharides, formed by glucose-, xylose-, mannan- and/or arabinose-containing polymers, linked by various types of glycosidic bonds, as well as ramification types. Our proteomic approach successfully identified a large number of relevant polypeptides in the C. gestroi digestome. A total of 55 different proteins were identified and classified into 29 CAZy families. Based on the total number of peptides identified, the majority of components found in the C. gestroi digestome were cellulose-degrading enzymes. Xylanolytic enzymes, mannan-hydrolytic enzymes, pectinases and starch-degrading and debranching enzymes were also identified. Our strategy enabled validation of liquid chromatography with tandem mass spectrometry recognized proteins, by enzymatic functional assays and by following the degradation products of specific 8-amino-1,3,6-pyrenetrisulfonic acid labeled oligosaccharides through capillary zone electrophoresis.Conclusions: Here we describe the first global study on the enzymatic repertoire involved in plant polysaccharide degradation by the lower termite C. gestroi. The biochemical characterization of whole body termite extracts evidenced their ability to cleave all types of glycosidic bonds present in plant polysaccharides. The comprehensive proteomic analysis, revealed a complete collection of hydrolytic enzymes including cellulases (GH1, GH3, GH5, GH7, GH9 and CBM 6), hemicellulases (GH2, GH10, GH11, GH16, GH43 and CBM 27) and pectinases (GH28 and GH29). |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-11-14 2014-05-20T13:55:54Z 2014-05-20T13:55:54Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1186/1754-6834-4-50 Biotechnology For Biofuels. London: Biomed Central Ltd., v. 4, p. 10, 2011. 1754-6834 http://hdl.handle.net/11449/20011 10.1186/1754-6834-4-50 WOS:000300718400001 WOS000300718400001.pdf |
url |
http://dx.doi.org/10.1186/1754-6834-4-50 http://hdl.handle.net/11449/20011 |
identifier_str_mv |
Biotechnology For Biofuels. London: Biomed Central Ltd., v. 4, p. 10, 2011. 1754-6834 10.1186/1754-6834-4-50 WOS:000300718400001 WOS000300718400001.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biotechnology for Biofuels 5.497 1,899 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
10 application/pdf |
dc.publisher.none.fl_str_mv |
Biomed Central Ltd. |
publisher.none.fl_str_mv |
Biomed Central Ltd. |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1799965137453449216 |