| Full text | |
| Author(s): |
Correa, Thamy L. R.
[1]
;
Franco Cairo, Joao Paulo L.
[2, 3]
;
Cota, Junio
[4]
;
Damasio, Andre
[2]
;
Oliveira, Leandro C.
[5]
;
Squina, Fabio M.
[3]
Total Authors: 6
|
| Affiliation: | [1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biorenewables Natl Lab LNBR, Campinas, SP - Brazil
[2] Univ Estadual Campinas, Inst Biol IB, Dept Biochem & Tissue Biol, UNICAMP, Campinas, SP - Brazil
[3] Univ Sorocaba UNISO, Programa Proc Tecnol & Ambientais, Cidade Univ, Rod Raposo Tavares, Km 92-5, BR-18023000 Sorocaba, SP - Brazil
[4] Univ Fed Minas Gerais UFMG, Inst Ciencias Agr ICA, Montes Claros, MG - Brazil
[5] Sao Paulo State Univ Unesp, Inst Biosci Humanities & Exact Sci, Dept Phys, Sao Jose Do Rio Preto, SP - Brazil
Total Affiliations: 5
|
| Document type: | Journal article |
| Source: | International Journal of Biological Macromolecules; v. 166, p. 1188-1196, JAN 1 2021. |
| Web of Science Citations: | 0 |
| Abstract | |
It is urgent the transition from a fossil fuel-based economy to a sustainable bioeconomy based on bioconversion technologies using renewable plant biomass feedstocks to produce high chemicals, bioplastics, and biofuels. beta-Glucosidases are key enzymes responsible for degrading the plant cell wall polymers, as they cleave glucanbased oligo- and polysaccharides to generate glucose. Monosaccharide-tolerant or -stimulated beta-glucosidases have been reported in the past decade. Here, we describe a novel mechanism of beta-glucosidase stimulation by glucose and xylose. The glycoside hydrolase 1 family beta-glucosidase from Thermotoga petrophila (TpBgl1) displays a typical glucose stimulation mechanism based on an increased V-max and decreased K-m in response to glucose. Through molecular docking and dynamics analyses, we mapped putative monosaccharide binding regions (BRs) on the surface of TpBgl1. Our results indicate that after interaction with glucose or xylose at BR1 site, an adjacent loop region assumes an extended conformation, which increases the entrance to the TpBgl1 active site, improving product formation. Biochemical assays with TpBgl1 BR1 mutants, TpBgl1(D49A/Y410A) and TpBgl1(D49K/Y410H) resulted in decreasing and abolishing monosaccharide stimulation, respectively. These mutations also impaired the BR1 looping extension responsible for monosaccharide stimulation. This study provides a molecular basis for the rational design of beta-glucosidases for biotechnological applications. (C) 2020 Elsevier B.V. All rights reserved. (AU) | |
| FAPESP's process: | 15/50590-4 - Lignin valorization in cellulosic ethanol plants: biocatalytic conversion via ferulic acid to high value chemicals |
| Grantee: | Fábio Márcio Squina |
| Support Opportunities: | Program for Research on Bioenergy (BIOEN) - Thematic Grants |
| FAPESP's process: | 16/09950-0 - Functional, structural characterizations and biotechnological application of lytic polysaccharide monooxygenases from the lower termite Coptotermes gestroi |
| Grantee: | João Paulo Lourenço Franco Cairo |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 12/20549-4 - Secretion of heterologous glycoproteins in Aspergillus: effect of glycosylation pattern in functional parameters of glycosyl hydrolases |
| Grantee: | André Ricardo de Lima Damasio |
| Support Opportunities: | Program for Research on Bioenergy (BIOEN) - Young Investigators Grants |
| FAPESP's process: | 10/18198-3 - Systems biology of sugarcane bagasse microbial decomposition interactions |
| Grantee: | Fábio Márcio Squina |
| Support Opportunities: | Research Grants - Visiting Researcher Grant - International |