Immobilization Of β-Glucosidase By Self-catalysis And Compared To Crosslinking With Glutaraldehyde

Different types of enzymes have been effectively immobilized on the surface of the nanoparticles.The immobilization of the enzyme on nanomaterials shows the potential applications in the biotechnological industry.In this work from several other enzymes,we selected theβ-glucosidase,which is very significant in industrial area.The efficiency and reusability ofβ-glucosidase was found higher after immobilization on nanoparticles.The anion exchange process was choosed for the purification and theβ-glucosidase,which was extracted from fruiting bodies of Agrocybe aegirit.The Si O₂ nanoparticles（nano-Si O₂）crosslink with glutaraldehyde（GA）was selected for immobilization ofβ-glucosidase.Initially,by the adsorption process theβ-glucosidase was immobilized and finally crosslink with genipin（GP）which was prepared by the hydrolysis of geniposide byβ-glucosidase.Then the properties of both immobilized GA-crosslinkedβ-glucosidase and GP-crosslinkedβ-glucosidase were compared and the immobilization yields were measured as 83.34%and 96.29%.The p H 6 was found optimal for PGA-crosslinkedβ-glucosidase and freeβ-glucosidase and he most favorable p H for GP-crosslinkedβ-glucosidase was measured about 4.5-7.5.The optimal temperature for GA-crosslinkedβ-glucosidase and GP-crosslinkedβ-glucosidase was found as 50°C,70°C.The best temperature for the freeβ-glucosidase was 55°C.Additionally,the scanning electron microscope（SEM）was used for the characterization of the GA-crosslinkedβ-glucosidase and GP-crosslinkedβ-glucosidase.The high performance liquid chromatography（HPLC）was used for the analysis of the geniposide consumption in the reaction system of GA-crosslinkedβ-glucosidase.