Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized beta-glucosidase from Exiguobacterium antarcticum B7

Autor(es)

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]

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: CATALYSTS; v. 9, n. 3 MAR 2019.
• Citações Web of Science: 0

Resumo

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)

• Processo FAPESP: 17/14253-9 - Avaliação do potencial biotecnológico do sistema celulolítico de Xanthomonas axonopodis pv. citri: uma abordagem estrutural, funcional e aplicada
• Beneficiário: Ricardo Rodrigues de Melo
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado