Unravelling biochemical and structural features of Bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies

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Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorBrazilian Center for Research in Energy and Materials-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorBriganti, Lorenzo-
Autor(es): dc.creatorManzine, Livia R.-
Autor(es): dc.creatorde Mello Capetti, Caio Cesar-
Autor(es): dc.creatorde Araújo, Evandro Ares-
Autor(es): dc.creatorde Oliveira Arnoldi Pellegrini, Vanessa-
Autor(es): dc.creatorGuimaraes, Francisco Eduardo Gontijo-
Autor(es): dc.creatorde Oliveira Neto, Mario-
Autor(es): dc.creatorPolikarpov, Igor-
Data de aceite: dc.date.accessioned2025-08-21T21:05:37Z-
Data de disponibilização: dc.date.available2025-08-21T21:05:37Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-08-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2024.133182-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/298027-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/298027-
Descrição: dc.descriptionGlycoside hydrolase family 5 (GH5) encompasses enzymes with several different activities, including endo-1,4-β-mannosidases. These enzymes are involved in mannan degradation, and have a number of biotechnological applications, such as mannooligosaccharide prebiotics production, stain removal and dyes decolorization, to name a few. Despite the importance of GH5 enzymes, only a few members of subfamily 7 were structurally characterized. In the present work, biochemical and structural characterization of Bacillus licheniformis GH5 mannanase, BlMan5_7 were performed and the enzyme cleavage pattern was analyzed, showing that BlMan5_7 requires at least 5 occupied subsites to perform efficient hydrolysis. Additionally, crystallographic structure at 1.3 Å resolution was determined and mannoheptaose (M7) was docked into the active site to investigate the interactions between substrate and enzyme through molecular dynamic (MD) simulations, revealing the existence of a − 4 subsite, which might explain the generation of mannotetraose (M4) as an enzyme product. Biotechnological application of the enzyme in stain removal was investigated, demonstrating that BlMan5_7 addition to washing solution greatly improves mannan-based stain elimination.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionInstituto de Física de São Carlos Universidade de São Paulo, Avenida Trabalhador São Carlense 400 - Centro, SP-
Descrição: dc.descriptionBrazilian Synchrotron Light Laboratory (LNLS) Brazilian Center for Research in Energy and Materials, São Paulo-
Descrição: dc.descriptionDepartamento de Física e Biofísica Instituto de Biociências de Botucatu Universidade Estadual Paulista, Distrito de Rubião Jr. s/n, SP-
Descrição: dc.descriptionDepartamento de Física e Biofísica Instituto de Biociências de Botucatu Universidade Estadual Paulista, Distrito de Rubião Jr. s/n, SP-
Descrição: dc.descriptionFAPESP: 2021/08780-1-
Descrição: dc.descriptionCNPq: 306852/2021-7-
Idioma: dc.languageen-
Relação: dc.relationInternational Journal of Biological Macromolecules-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectBacillus licheniformis-
Palavras-chave: dc.subjectCrystallographic structure-
Palavras-chave: dc.subjectGH5_7 mannanase-
Título: dc.titleUnravelling biochemical and structural features of Bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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