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

Detalhes bibliográficos
Autor(a) principal: Colombo, Lívia Tavares
Data de Publicação: 2016
Outros Autores: 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
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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spelling 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
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