Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1007/s10482-016-0723-4 http://www.locus.ufv.br/handle/123456789/18806 |
Resumo: | Environments where lignocellulosic biomass is naturally decomposed are sources for discovery of new hydrolytic enzymes that can reduce the high cost of enzymatic cocktails for second-generation ethanol production. Metagenomic analysis was applied to discover genes coding carbohydrate-depleting enzymes from a microbial laboratory subculture using a mix of sugarcane bagasse and cow manure in the thermophilic composting phase. From a fosmid library, 182 clones had the ability to hydrolyse carbohydrate. Sequencing of 30 fosmids resulted in 12 contigs encoding 34 putative carbohydrate-active enzymes belonging to 17 glycosyl hydrolase (GH) families. One third of the putative proteins belong to the GH3 family, which includes β-glucosidase enzymes known to be important in the cellulose-deconstruction process but present with low activity in commercial enzyme preparations. Phylogenetic analysis of the amino acid sequences of seven selected proteins, including three β-glucosidases, showed low relatedness with protein sequences deposited in databases. These findings highlight microbial consortia obtained from a mixture of decomposing biomass residues, such as sugar cane bagasse and cow manure, as a rich resource of novel enzymes potentially useful in biotechnology for saccharification of lignocellulosic substrate. |
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Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manureCellulases genesCellulose degradationFosmid library sequencingMetagenomic libraryEnvironments where lignocellulosic biomass is naturally decomposed are sources for discovery of new hydrolytic enzymes that can reduce the high cost of enzymatic cocktails for second-generation ethanol production. Metagenomic analysis was applied to discover genes coding carbohydrate-depleting enzymes from a microbial laboratory subculture using a mix of sugarcane bagasse and cow manure in the thermophilic composting phase. From a fosmid library, 182 clones had the ability to hydrolyse carbohydrate. Sequencing of 30 fosmids resulted in 12 contigs encoding 34 putative carbohydrate-active enzymes belonging to 17 glycosyl hydrolase (GH) families. One third of the putative proteins belong to the GH3 family, which includes β-glucosidase enzymes known to be important in the cellulose-deconstruction process but present with low activity in commercial enzyme preparations. Phylogenetic analysis of the amino acid sequences of seven selected proteins, including three β-glucosidases, showed low relatedness with protein sequences deposited in databases. These findings highlight microbial consortia obtained from a mixture of decomposing biomass residues, such as sugar cane bagasse and cow manure, as a rich resource of novel enzymes potentially useful in biotechnology for saccharification of lignocellulosic substrate.Antonie van Leeuwenhoek2018-04-19T10:42:02Z2018-04-19T10:42:02Z2016-06-27info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdf15729699https://doi.org/10.1007/s10482-016-0723-4http://www.locus.ufv.br/handle/123456789/18806engv. 109, Issue 9, p. 1217–1233, September 2016Springer International Publishing Switzerlandinfo:eu-repo/semantics/openAccessColombo, Lívia TavaresOliveira, Marcelo Nagem Valério deCarneiro, Deisy GuimarãesSouza, Robson Assis deAlvim, Mariana Caroline TocantinsSantos, Josenilda Carlos dosSilva, Cynthia Canêdo daVidigal, Pedro Marcus PereiraSilveira, Wendel Batista daPassos, Flávia Maria Lopesreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFV2024-07-12T07:16:46Zoai:locus.ufv.br:123456789/18806Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452024-07-12T07:16:46LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.none.fl_str_mv |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure |
title |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure |
spellingShingle |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure Colombo, Lívia Tavares Cellulases genes Cellulose degradation Fosmid library sequencing Metagenomic library |
title_short |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure |
title_full |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure |
title_fullStr |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure |
title_full_unstemmed |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure |
title_sort |
Applying functional metagenomics to search for novel lignocellulosic enzymes in a microbial consortium derived from a thermophilic composting phase of sugarcane bagasse and cow manure |
author |
Colombo, Lívia Tavares |
author_facet |
Colombo, Lívia Tavares Oliveira, Marcelo Nagem Valério de Carneiro, Deisy Guimarães Souza, Robson Assis de Alvim, Mariana Caroline Tocantins Santos, Josenilda Carlos dos Silva, Cynthia Canêdo da Vidigal, Pedro Marcus Pereira Silveira, Wendel Batista da Passos, Flávia Maria Lopes |
author_role |
author |
author2 |
Oliveira, Marcelo Nagem Valério de Carneiro, Deisy Guimarães Souza, Robson Assis de Alvim, Mariana Caroline Tocantins Santos, Josenilda Carlos dos Silva, Cynthia Canêdo da Vidigal, Pedro Marcus Pereira Silveira, Wendel Batista da Passos, Flávia Maria Lopes |
author2_role |
author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Colombo, Lívia Tavares Oliveira, Marcelo Nagem Valério de Carneiro, Deisy Guimarães Souza, Robson Assis de Alvim, Mariana Caroline Tocantins Santos, Josenilda Carlos dos Silva, Cynthia Canêdo da Vidigal, Pedro Marcus Pereira Silveira, Wendel Batista da Passos, Flávia Maria Lopes |
dc.subject.por.fl_str_mv |
Cellulases genes Cellulose degradation Fosmid library sequencing Metagenomic library |
topic |
Cellulases genes Cellulose degradation Fosmid library sequencing Metagenomic library |
description |
Environments where lignocellulosic biomass is naturally decomposed are sources for discovery of new hydrolytic enzymes that can reduce the high cost of enzymatic cocktails for second-generation ethanol production. Metagenomic analysis was applied to discover genes coding carbohydrate-depleting enzymes from a microbial laboratory subculture using a mix of sugarcane bagasse and cow manure in the thermophilic composting phase. From a fosmid library, 182 clones had the ability to hydrolyse carbohydrate. Sequencing of 30 fosmids resulted in 12 contigs encoding 34 putative carbohydrate-active enzymes belonging to 17 glycosyl hydrolase (GH) families. One third of the putative proteins belong to the GH3 family, which includes β-glucosidase enzymes known to be important in the cellulose-deconstruction process but present with low activity in commercial enzyme preparations. Phylogenetic analysis of the amino acid sequences of seven selected proteins, including three β-glucosidases, showed low relatedness with protein sequences deposited in databases. These findings highlight microbial consortia obtained from a mixture of decomposing biomass residues, such as sugar cane bagasse and cow manure, as a rich resource of novel enzymes potentially useful in biotechnology for saccharification of lignocellulosic substrate. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-06-27 2018-04-19T10:42:02Z 2018-04-19T10:42:02Z |
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 |
15729699 https://doi.org/10.1007/s10482-016-0723-4 http://www.locus.ufv.br/handle/123456789/18806 |
identifier_str_mv |
15729699 |
url |
https://doi.org/10.1007/s10482-016-0723-4 http://www.locus.ufv.br/handle/123456789/18806 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
v. 109, Issue 9, p. 1217–1233, September 2016 |
dc.rights.driver.fl_str_mv |
Springer International Publishing Switzerland info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Springer International Publishing Switzerland |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
pdf application/pdf |
dc.publisher.none.fl_str_mv |
Antonie van Leeuwenhoek |
publisher.none.fl_str_mv |
Antonie van Leeuwenhoek |
dc.source.none.fl_str_mv |
reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
instname_str |
Universidade Federal de Viçosa (UFV) |
instacron_str |
UFV |
institution |
UFV |
reponame_str |
LOCUS Repositório Institucional da UFV |
collection |
LOCUS Repositório Institucional da UFV |
repository.name.fl_str_mv |
LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV) |
repository.mail.fl_str_mv |
fabiojreis@ufv.br |
_version_ |
1817559915301961728 |