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Improved enzymatic performance of graphene‐immobilized β‐glucosidase A in the presence of glucose‐6‐phosphate
Author(s) -
Albino Gomes Anderson,
Pazinatto Telli Elisa,
Miletti Luiz Claudio,
Skoronski Everton,
Gomes Ghislandi Marcos,
Felippe da Silva Gustavo,
Borba Magalhães Maria de Lourdes
Publication year - 2017
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1569
Subject(s) - hydrolysis , chemistry , cellulose , immobilized enzyme , enzymatic hydrolysis , phosphate , catalysis , graphene , biomass (ecology) , enzyme , chromatography , chemical engineering , organic chemistry , materials science , nanotechnology , oceanography , engineering , geology
Optimization of cellulose enzymatic hydrolysis is crucial for cost‐effective bioethanol production from lignocellulosic biomass. Enzyme immobilization in solid support allows enzyme recycling for reuse, lowering hydrolysis costs. Graphene is a nanomaterial isolated in 2004, which possesses exceptional properties for biomolecule immobilization. This study evaluates the potential for β‐glucosidase recycling by immobilization on graphene nanosheets. Data reported here demonstrated that graphene‐immobilized β‐glucosidase can be recycled for at least eight cycles. Immobilization did not change the optimal temperature of catalysis and improved enzymatic stability upon storage. The role of glucose‐6‐phosphate on immobilized enzyme was also investigated, demonstrating that glucose‐6‐phosphate acts as a mixed‐type activator and improves storage stability of immobilized enzyme. Complete cellulose hydrolysis using graphene‐immobilized β‐glucosidase in the presence of glucose‐6‐phosphate resulted in greatly improved hydrolysis rates, demonstrating the potential of this strategy for biomass hydrolysis.