Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/339573
Type: Artigo
Title: Cross-linking with polyethylenimine confers better functional characteristics to an immobilized β-glucosidase from Exiguobacterium antarcticum B7
Author: Rodrigues de Melo, Ricardo
Carlos Alnoch, Robson
de Sousa, Amanda Silva
Sato, Helia Harumi
Ruller, Roberto
Mateo, Cesar
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
Subject: Glutaraldeido
Country: Suiça
Editor: MDPI
Rights: Aberto
Identifier DOI: 10.3390/catal9030223
Address: https://www.mdpi.com/2073-4344/9/3/223
Date Issue: 2019
Appears in Collections:FEA - Artigos e Outros Documentos

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