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

Catalysts

RobsonCarlos Alnoch¹  Ricardo Rodrigues de Melo¹  Cesar Mateo¹  Hélia Harumi Sato²  Roberto Ruller³  AmandaSilva de Sousa⁴ 

[1] Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica (CSIC), Marie Curie 2. Cantoblanco, Campus UAM, 28049 Madri, Spain;Departamento de Ciência de Alimentos, Faculdade de Engenharia de Alimentos, Universidade Estadual de Campinas (UNICAMP), CEP 13083-862 Campinas, São Paulo, Brazil;Instituto de Biociências, Universidade Federal de Mato Grosso do Sul (UFMS), CEP 79070-900 Campo Grande, Brazil;Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), CEP 13083-970 Campinas, São Paulo, Brazil;

关键词: β-glucosidase immobilization;    tetrameric enzyme;    glutaraldehyde;    polyethylenimine;    pH-stability;    cellobiose hydrolysis;   

DOI  :  10.3390/catal9030223

来源: DOAJ

【 摘 要 】

β-glucosidases are ubiquitous, well-characterized and biologically important enzymes with considerable uses in industrial sectors. Here, a tetrameric β-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 °C to 50 °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 β-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 β-glucosidase for future use in the bioethanol production.

【 授权许可】

Unknown