Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes

Detalhes bibliográficos
Autor(a) principal: Leonel, Tatiane Fernanda [UNESP]
Data de Publicação: 2021
Outros Autores: Pepe, Elisângela Soares Gomes [UNESP], Castellane, Tereza Cristina Luque [UNESP], Da Silva Vantini, Juliana [UNESP], Funnicelli, Michelli Inácio Gonçalves [UNESP], De MacEdo Lemos, Eliana Gertrudes [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1371/journal.pone.0247822
http://hdl.handle.net/11449/206068
Resumo: After being isolated from a sugarcane pile, the bacterium Chitinophaga sp. CB10 demonstrated to be a rich source of carbohydrases, with 350 predicted CAZyme domains. CB10 was able to grow on carbohydrates of different structural complexities: glucose, carboxymethylcellulose, corn starch, galactomannan, Aloe vera gum and sugarcane bagasse. The sugarcane bagasse is a rich source of complex polymers, and the diversity of metabolites released by its enzymatic hydrolysis has an important role for green chemistry, including minority pathways such as the degradation of mannan conjugates. In this sense, CB10 demonstrated considerable levels of gene expression for mannanases, and was stable for a period of 96-144 hours in the presence of sugarcane bagasse as sole carbon source. The bacterium showed respectively 4.8x and 5.6x expression levels for two genes predicted for GH2 β-mannosidase: one located within a gene cluster identified as polysaccharide utilization loci(PUL), and another a classic β-mannosidase. These enzymes shared less than 45% of identity with enzymes characterized from the genus Chitinophaga belonging to the phylum Bacteroidetes. The degree of novelty - as demonstrated by the low identity with previously characterized enzymes; the remarkable capability to grow in different substrates; mannanase activity, evidenced by the release of residual oligosaccharides in the cultivation with galactomannan (HPLC-RID, 12.3 mMol); associated to the ability of mannanases expression in a low concentration of inductor conditions (sugarcane bagasse, 0.2%) indicate the high potential for the application of CB10 as a source of enzymes in the production of oligosaccharides from biomass. This capacity might prove to be very valuable for the biorefinery process of pre-biotic precursors and other functional oligosaccharides focused on the food and pharmaceutical industries.
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spelling Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetesAfter being isolated from a sugarcane pile, the bacterium Chitinophaga sp. CB10 demonstrated to be a rich source of carbohydrases, with 350 predicted CAZyme domains. CB10 was able to grow on carbohydrates of different structural complexities: glucose, carboxymethylcellulose, corn starch, galactomannan, Aloe vera gum and sugarcane bagasse. The sugarcane bagasse is a rich source of complex polymers, and the diversity of metabolites released by its enzymatic hydrolysis has an important role for green chemistry, including minority pathways such as the degradation of mannan conjugates. In this sense, CB10 demonstrated considerable levels of gene expression for mannanases, and was stable for a period of 96-144 hours in the presence of sugarcane bagasse as sole carbon source. The bacterium showed respectively 4.8x and 5.6x expression levels for two genes predicted for GH2 β-mannosidase: one located within a gene cluster identified as polysaccharide utilization loci(PUL), and another a classic β-mannosidase. These enzymes shared less than 45% of identity with enzymes characterized from the genus Chitinophaga belonging to the phylum Bacteroidetes. The degree of novelty - as demonstrated by the low identity with previously characterized enzymes; the remarkable capability to grow in different substrates; mannanase activity, evidenced by the release of residual oligosaccharides in the cultivation with galactomannan (HPLC-RID, 12.3 mMol); associated to the ability of mannanases expression in a low concentration of inductor conditions (sugarcane bagasse, 0.2%) indicate the high potential for the application of CB10 as a source of enzymes in the production of oligosaccharides from biomass. This capacity might prove to be very valuable for the biorefinery process of pre-biotic precursors and other functional oligosaccharides focused on the food and pharmaceutical industries.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)Department of Technology Laboratory of Biochemistry and Plant MicroorganismsGraduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)Graduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)Universidade Estadual Paulista (Unesp)Laboratory of Biochemistry and Plant MicroorganismsLeonel, Tatiane Fernanda [UNESP]Pepe, Elisângela Soares Gomes [UNESP]Castellane, Tereza Cristina Luque [UNESP]Da Silva Vantini, Juliana [UNESP]Funnicelli, Michelli Inácio Gonçalves [UNESP]De MacEdo Lemos, Eliana Gertrudes [UNESP]2021-06-25T10:26:03Z2021-06-25T10:26:03Z2021-03-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1371/journal.pone.0247822PLoS ONE, v. 16, n. 3 March, 2021.1932-6203http://hdl.handle.net/11449/20606810.1371/journal.pone.02478222-s2.0-85102766080Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPLoS ONEinfo:eu-repo/semantics/openAccess2021-10-22T20:49:01Zoai:repositorio.unesp.br:11449/206068Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:52:28.414290Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
title Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
spellingShingle Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
Leonel, Tatiane Fernanda [UNESP]
title_short Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
title_full Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
title_fullStr Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
title_full_unstemmed Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
title_sort Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
author Leonel, Tatiane Fernanda [UNESP]
author_facet Leonel, Tatiane Fernanda [UNESP]
Pepe, Elisângela Soares Gomes [UNESP]
Castellane, Tereza Cristina Luque [UNESP]
Da Silva Vantini, Juliana [UNESP]
Funnicelli, Michelli Inácio Gonçalves [UNESP]
De MacEdo Lemos, Eliana Gertrudes [UNESP]
author_role author
author2 Pepe, Elisângela Soares Gomes [UNESP]
Castellane, Tereza Cristina Luque [UNESP]
Da Silva Vantini, Juliana [UNESP]
Funnicelli, Michelli Inácio Gonçalves [UNESP]
De MacEdo Lemos, Eliana Gertrudes [UNESP]
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Laboratory of Biochemistry and Plant Microorganisms
dc.contributor.author.fl_str_mv Leonel, Tatiane Fernanda [UNESP]
Pepe, Elisângela Soares Gomes [UNESP]
Castellane, Tereza Cristina Luque [UNESP]
Da Silva Vantini, Juliana [UNESP]
Funnicelli, Michelli Inácio Gonçalves [UNESP]
De MacEdo Lemos, Eliana Gertrudes [UNESP]
description After being isolated from a sugarcane pile, the bacterium Chitinophaga sp. CB10 demonstrated to be a rich source of carbohydrases, with 350 predicted CAZyme domains. CB10 was able to grow on carbohydrates of different structural complexities: glucose, carboxymethylcellulose, corn starch, galactomannan, Aloe vera gum and sugarcane bagasse. The sugarcane bagasse is a rich source of complex polymers, and the diversity of metabolites released by its enzymatic hydrolysis has an important role for green chemistry, including minority pathways such as the degradation of mannan conjugates. In this sense, CB10 demonstrated considerable levels of gene expression for mannanases, and was stable for a period of 96-144 hours in the presence of sugarcane bagasse as sole carbon source. The bacterium showed respectively 4.8x and 5.6x expression levels for two genes predicted for GH2 β-mannosidase: one located within a gene cluster identified as polysaccharide utilization loci(PUL), and another a classic β-mannosidase. These enzymes shared less than 45% of identity with enzymes characterized from the genus Chitinophaga belonging to the phylum Bacteroidetes. The degree of novelty - as demonstrated by the low identity with previously characterized enzymes; the remarkable capability to grow in different substrates; mannanase activity, evidenced by the release of residual oligosaccharides in the cultivation with galactomannan (HPLC-RID, 12.3 mMol); associated to the ability of mannanases expression in a low concentration of inductor conditions (sugarcane bagasse, 0.2%) indicate the high potential for the application of CB10 as a source of enzymes in the production of oligosaccharides from biomass. This capacity might prove to be very valuable for the biorefinery process of pre-biotic precursors and other functional oligosaccharides focused on the food and pharmaceutical industries.
publishDate 2021
dc.date.none.fl_str_mv 2021-06-25T10:26:03Z
2021-06-25T10:26:03Z
2021-03-01
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/10.1371/journal.pone.0247822
PLoS ONE, v. 16, n. 3 March, 2021.
1932-6203
http://hdl.handle.net/11449/206068
10.1371/journal.pone.0247822
2-s2.0-85102766080
url http://dx.doi.org/10.1371/journal.pone.0247822
http://hdl.handle.net/11449/206068
identifier_str_mv PLoS ONE, v. 16, n. 3 March, 2021.
1932-6203
10.1371/journal.pone.0247822
2-s2.0-85102766080
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv PLoS ONE
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
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instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
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