Advanced search
Start date
Betweenand
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Author(s):
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]
Total Authors: 8
Affiliation:
[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
Total Affiliations: 4
Document type: Journal article
Source: Enzyme and Microbial Technology; v. 87-88, p. 1-8, JUN 2016.
Web of Science Citations: 3
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 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)

FAPESP's process: 14/02065-5 - Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dimensional structure of the Central Domain an its role in the thermostabilization of whole enzyme
Grantee:Viviam Moura da Silva
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 15/02897-3 - Structural and functional analysis of the fibronectin type III domain (FnIII) of one beta-glucosidase belonging to the family GH3: interaction with large polymeric substrates and thermostability
Grantee:Wanius José Garcia da Silva
Support type: Program for Research on Bioenergy (BIOEN) - Regular Program Grants