| Full text | |
| Author(s): |
Rodrigues de Melo, Ricardo
[1, 2]
;
Carlos Alnoch, Robson
[2, 3]
;
de Sousa, Amanda Silva
[1]
;
Sato, Helia Harumi
[4]
;
Ruller, Roberto
[5]
;
Mateo, Cesar
[2]
Total Authors: 6
|
| Affiliation: | [1] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, BR-13083970 Campinas, SP - Brazil
[2] CSIC, Inst Catalisis & Petroleoquim, Dept Biocatalisis, Marie Curie 2 Cantoblanco, Campus UAM, Madri 28049 - Spain
[3] Univ Fed Parana, Dept Bioquim & Biol Mol, Cx P 19081 Ctr Politecn, BR-81531980 Curitiba, Parana - Brazil
[4] Univ Estadual Campinas, UNICAMP, Fac Engn Alimentos, Dept Ciencia Alimentos, BR-13083862 Campinas, SP - Brazil
[5] Univ Fed Mato Grosso do Sul UFMS, Inst Biociencias, BR-79070900 Campo Grande - Brazil
Total Affiliations: 5
|
| Document type: | Journal article |
| Source: | CATALYSTS; v. 9, n. 3 MAR 2019. |
| Web of Science Citations: | 0 |
| Abstract | |
beta-glucosidases are ubiquitous, well-characterized and biologically important enzymes with considerable uses in industrial sectors. Here, a tetrameric -glucosidase from Exiguobacterium antarcticum B7 (EaBglA) was immobilized on different activated agarose supports followed by post-immobilization with poly-functional macromolecules. The best result was obtained by the immobilization of EaBglA on metal glutaraldehyde-activated agarose support following cross-linking with polyethylenimine. Interestingly, the immobilized EaBglA was 46-fold more stable than its free form and showed optimum pH in the acidic region, with high catalytic activity in the pH range from 3 to 9, while the free EaBglA showed catalytic activity in a narrow pH range (>80% at pH 6.0-8.0) and optimum pH at 7.0. EaBglA had the optimum temperature changed from 30 degrees C to 50 degrees C with the immobilization step. The immobilized EaBglA showed an expressive adaptation to pH and it was tolerant to ethanol and glucose, indicating suitable properties involving the saccharification process. Even after 9 cycles of reuse, the immobilized -glucosidase retained about 100% of its initial activity, demonstrating great operational stability. Hence, the current study describes an efficient strategy to increase the functional characteristics of a tetrameric -glucosidase for future use in the bioethanol production. (AU) | |
| FAPESP's process: | 17/14253-9 - Evaluation of the biotechnological potential of the cellulolytic system of Xanthomonas axonopodis pv. citri: a structural, functional and applied approach |
| Grantee: | Ricardo Rodrigues de Melo |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |