Journal of Agricultural and Food Chemistry · 2013 · 24 citations · 51 references
Life SciencesBiochemistryBiotechnologyBiocatalysisBiochemical EngineeringEnzymologyBiocatalyst StabilityBiofuel ProductionEnzyme CharacterizationEnzyme ImmobilizationEnzyme KineticsEnzyme StabilityAgricultural ResiduesBeta-glucosidase ActivityBiocatalyst ImmobilizationHydrolysisImmobilized BiocatalystsKinetic Data AnalysisOperational Stabilityβ-Glucosidase Activity
β-Glucosidases represent an important group of enzymes due to their pivotal role in various biotechnological processes. One of the most prominent is biomass degradation for the production of fuel ethanol from cellulosic agricultural residues and wastes, where the use of immobilized biocatalysts may prove advantageous. Within such scope, the present work aimed to evaluate the feasibility of entrapping β-glucosidase in either sol-gel or in Lentikats supports for application in cellobiose hydrolysis, and to perform the characterization of the resulting bioconversion systems. The activity and stability of the immobilized biocatalyst over given ranges of temperature and pH values were assessed, as well as kinetic data, and compared to the free form, and the operational stability was evaluated. Immobilization increased the thermal stability of the enzyme, with a 10 °C shift to an optimal temperature in the case of sol-gel support. Mass transfer hindrances as a result of immobilization were not significant, for sol-gel support. Lentikats-entrapped glucosidase was used in 19 consecutive batch runs for cellobiose hydrolysis, without noticeable decrease in product yield. Moreover, encouraging results were obtained for continuous operation. In the overall, the feasibility of using immobilized biocatalysts for cellobiose hydrolysis was established.
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