Non-productive adsorption of bacterial beta-glucosidases on lignins is electrostatically modulated and depends on the presence of fibronection type III-like domain

Autor(es)

da Silva, Viviam M. ^[1] ; de Souza, Anderson S. ^[1] ; Negrao, Djanira R. ^[2] ; Polikarpov, Igor ^[3] ; Squina, Fabio M. ^[4] ; de Oliveira Neto, Mario ^[2] ; Muniz, Joao R. C. ^[3] ; Garcia, Wanius ^[1]

Afiliação do(s) autor(es)

^[1] Univ Fed Abc, CCNH, Santo Andre, SP - Brazil

^[2] UNESP Univ Estadual Paulista, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP - Brazil

^[3] Univ Sao Paulo, IFSC, Sao Carlos, SP - Brazil

^[4] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, Campinas, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Enzyme and Microbial Technology; v. 87-88, p. 1-8, JUN 2016.
• Citações Web of Science: 3

Resumo

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 beta-glucosidases (GH1 and GH3) on lignins. The results showed that beta-glucosidases can adsorb to lignins through different mechanisms. GH1 beta-glucosidase adsorption onto lignins was found to be strongly pH-dependent, suggesting that the adsorption is electrostatically modulated. For GH3 beta-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 beta-glucosidases adsorption, probably because there is no significant increase in hydrophobic regions in the beta-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. (C) 2016 Elsevier Inc. All rights reserved. (AU)

• Processo FAPESP: 15/02897-3 - Análise estrutural e funcional do domínio fibronectina tipo III (FnIII) de uma beta-glicosidase da família GH3: interação com substratos poliméricos e termoestabilidade
• Beneficiário: Wanius José Garcia da Silva
• Modalidade de apoio: Auxílio à Pesquisa - Programa BIOEN - Regular
• Processo FAPESP: 14/02065-5 - Modular hipertermoestável endo-beta-1,4-mananase: determinação da estrutura tridimensional do domínio central e seu papel na termoestabilização global da enzima
• Beneficiário: Viviam Moura da Silva
• Modalidade de apoio: Bolsas no Brasil - Doutorado