Improved enzymatic performance of graphene-immobilized β-glucosidase A in the presence of glucose-6-phosphate.
Anderson Albino GomesElisa Pazinatto TelliLuiz Claudio MilettiEverton SkoronskiMarcos Gomes GhislandiGustavo Felippe da SilvaMaria de Lourdes B MagalhãesPublished in: Biotechnology and applied biochemistry (2017)
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.
Keyphrases
- anaerobic digestion
- ionic liquid
- magnetic nanoparticles
- room temperature
- molecular docking
- blood glucose
- carbon nanotubes
- walled carbon nanotubes
- hydrogen peroxide
- wastewater treatment
- risk assessment
- electronic health record
- type diabetes
- nitric oxide
- adipose tissue
- big data
- blood pressure
- inflammatory response
- weight loss
- climate change
- deep learning
- metabolic syndrome
- glycemic control