| Full text | |
| Author(s): |
Colussi, Francieli
[1]
;
da Silva, Viviam M.
[1]
;
Miller, Ian
[1]
;
Cota, Junio
[2]
;
de Oliveira, Leandro C.
[3]
;
de Oliveira Neto, Mario
[4]
;
Squina, Fabio M.
[2]
;
Garcia, Wanius
[1]
Total Authors: 8
|
| Affiliation: | [1] Univ Fed Abc, CCNH, Santo Andre, SP - Brazil
[2] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Ciencia & Tecnol Bioetanol, Campinas, SP - Brazil
[3] UNESP Univ Estadual Paulista, Inst Biociencias Letras & Ciencias Exatas, Dept Fis, Sao Jose Do Rio Preto, SP - Brazil
[4] UNESP Univ Estadual Paulista, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP - Brazil
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | Amino Acids; v. 47, n. 5, p. 937-948, MAY 2015. |
| Web of Science Citations: | 8 |
| Abstract | |
The beta-glucosidases are enzymes essential for several industrial applications, especially in the field of plant structural polysaccharides conversion into bioenergy and bioproducts. In a recent study, we have provided a biochemical characterization of two hyperthermostable beta-glucosidases from Thermotoga petrophila belonging to the families GH1 (TpBGL1) and GH3 (TpBGL3). Here, as part of a continuing investigation, the oligomeric state, the net charge, and the structural stability, at acidic pH, of the TpBGL1 and TpBGL3 were characterized and compared. Enzymatic activity is directly related to the balance between protonation and conformational changes. Interestingly, our results indicated that there were no significant changes in the secondary, tertiary and quaternary structures of the beta-glucosidases at temperatures below 80 A degrees C. Furthermore, the results indicated that both the enzymes are stable homodimers in solution. Therefore, the observed changes in the enzymatic activities are due to variations in pH that modify protonation of the enzymes residues and the net charge, directly affecting the interactions with ligands. Finally, the results showed that the two beta-glucosidases displayed different pH dependence of thermostability at temperatures above 80 A degrees C. TpBGL1 showed higher stability at pH 6 than at pH 4, while TpBGL3 showed similar stability at both pH values. This study provides a useful comparison of the structural stability, at acidic pH, of two different hyperthermostable beta-glucosidases and how it correlates with the activity of the enzymes. The information described here can be useful for biotechnological applications in the biofuel and food industries. (AU) | |
| FAPESP's process: | 12/21054-9 - Biophysical studies and of the synergistic action of thermophilics enzymes involved in the hydrolysis of mannans |
| Grantee: | Wanius José Garcia da Silva |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 08/58037-9 - Library generation for biomass-conversion enzymes from soil metagenome |
| Grantee: | Fábio Márcio Squina |
| Support Opportunities: | Program for Research on Bioenergy (BIOEN) - Young Investigators Grants |
| FAPESP's process: | 12/03503-0 - Studies of stability, flexibility and enzymatic activity of the beta-mannanase from hyperthermophilic bacterium Thermotoga petrophila |
| Grantee: | Viviam Moura da Silva |
| Support Opportunities: | Scholarships in Brazil - Master |
| FAPESP's process: | 11/13242-7 - Studies of enzymatic mechanisms for the improvement of bio-fuel production |
| Grantee: | Leandro Cristante de Oliveira |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |