Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
DOI: | 10.1371/journal.pone.0247822 |
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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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 Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes Leonel, Tatiane Fernanda [UNESP] 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 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 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] 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] 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 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_ |
1822218375480213504 |
dc.identifier.doi.none.fl_str_mv |
10.1371/journal.pone.0247822 |