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

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Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorLaboratory of Biochemistry and Plant Microorganisms-
Autor(es): dc.creatorLeonel, Tatiane Fernanda [UNESP]-
Autor(es): dc.creatorPepe, Elisângela Soares Gomes [UNESP]-
Autor(es): dc.creatorCastellane, Tereza Cristina Luque [UNESP]-
Autor(es): dc.creatorDa Silva Vantini, Juliana [UNESP]-
Autor(es): dc.creatorFunnicelli, Michelli Inácio Gonçalves [UNESP]-
Autor(es): dc.creatorDe MacEdo Lemos, Eliana Gertrudes [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T00:46:04Z-
Data de disponibilização: dc.date.available2022-02-22T00:46:04Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-03-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1371/journal.pone.0247822-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/206068-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/206068-
Descrição: dc.descriptionAfter 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.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionSchool of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)-
Descrição: dc.descriptionDepartment of Technology Laboratory of Biochemistry and Plant Microorganisms-
Descrição: dc.descriptionGraduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)-
Descrição: dc.descriptionSchool of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)-
Descrição: dc.descriptionGraduate Program in Agricultural and Livestock Microbiology School of Agricultural and Veterinarian Sciences São Paulo State University (UNESP)-
Idioma: dc.languageen-
Relação: dc.relationPLoS ONE-
???dc.source???: dc.sourceScopus-
Título: dc.titleBagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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