title: Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence of fibronection type III-like domain.
abstract: Non-productive adsorption of cellulases onto lignins is an important mechanism that negatively affects the enzymatic hydrolysis of lignocellulose biomass. Here, we examined the non-productive adsorption of two bacterial β-glucosidases (GH1 and GH3) on lignins. The results showed that β-glucosidases can adsorb to lignins through different mechanisms. GH1 β-glucosidase adsorption onto lignins was found to be strongly pH-dependent, suggesting that the adsorption is electrostatically modulated. For GH3 β-glucosidase, the results suggested that the fibronectin type III-like domain interacts with lignins through electrostatic and hydrophobic interactions that can partially, or completely, overcome repulsive electrostatic forces between the catalytic domain and lignins. Finally, the increase of temperature did not result in the increase of β-glucosidases adsorption, probably because there is no significant increase in hydrophobic regions in the β-glucosidases structures. The data provided here can be useful for biotechnological applications, especially in the field of plant structural polysaccharides conversion into bioenergy and bioproducts.
authors.affiliation: Centro de Ciências Naturais e Humanas (CCNH), Universidade Federal do ABC (UFABC), Santo André, SP, Brazil.
authors.forename: Viviam M
authors.initials: VM
authors.lastname: da Silva
authors.affiliation: Centro de Ciências Naturais e Humanas (CCNH), Universidade Federal do ABC (UFABC), Santo André, SP, Brazil.
authors.forename: Anderson S
authors.initials: AS
authors.lastname: de Souza
authors.affiliation: Departamento de Física e Biofísica, Instituto de Biociências, UNESP-Univ Estadual Paulista, Botucatu, SP, Brazil.
authors.forename: Djanira R
authors.initials: DR
authors.lastname: Negrão
authors.affiliation: Instituto de Física de São Carlos (IFSC), Universidade de São Paulo (USP), São Carlos, SP, Brazil.
authors.forename: Igor
authors.initials: I
authors.lastname: Polikarpov
authors.affiliation: Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Campinas, SP, Brazil.
authors.forename: Fabio M
authors.initials: FM
authors.lastname: Squina
authors.affiliation: Departamento de Física e Biofísica, Instituto de Biociências, UNESP-Univ Estadual Paulista, Botucatu, SP, Brazil.
authors.forename: Mario
authors.initials: M
authors.lastname: de Oliveira Neto
authors.affiliation: Instituto de Física de São Carlos (IFSC), Universidade de São Paulo (USP), São Carlos, SP, Brazil.
authors.forename: João R C
authors.initials: JR
authors.lastname: Muniz
authors.affiliation: Centro de Ciências Naturais e Humanas (CCNH), Universidade Federal do ABC (UFABC), Santo André, SP, Brazil. Electronic address: wanius.garcia@ufabc.edu.br.
authors.forename: Wanius
authors.initials: W
authors.lastname: Garcia
mesh_terms: D000327:Adsorption; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D056804:Biofuels; D018533:Biomass; D001709:Biotechnology; D044602:Cellulases / Q000737:chemistry* / Q000378:metabolism*; D000071238:Fibronectin Type III Domain; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D008031:Lignin / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D055672:Static Electricity; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D056804:Biofuels; D011994:Recombinant Proteins; C036909:lignocellulose; D008031:Lignin; D044602:Cellulases
keywords: Fibronectin type III-like domain; Hyperthermostable; Lignin; Thermotoga petrophila; β-Glucosidases