| β-glucosidase has derived from plants﹑animals and microbes, as abiocatalyst which hydrolysis glycosidic bonds, has been widely used infood, industrial, pharmaceutical and other industries, and its research hasa certain theoretical and practical value.Basing on the strategy of the acticity isolation, this study getWGEA1strain that had the advantages of the biochemical properties andproduced the enzyme β-glucosidase fast, it was screened and identifiedas Exiguobacterium sp preliminarily;Preliminary optimized fermentationconditions to get the optimum fermentation conditions, from the originalactivity3.62U/ml to25.34U/ml; further estimated its enzymaticproperties, found that WGEA1enzyme production optimum temperatureand pH were55℃and8, below50℃, the activity was relatively stableunder the conditions of pH5~8; Metal ions of the Ba2+and Cu2+, Mn2+had the more stronger relative activity that were more than150%,but Al3+and K+that had the most strongest inhibition, the residual activity werelower than50%; Organic solvents acetone as a reinforcing agent toenhance the activity, but methanol, ethanol and ethyl acetate inhibited theenzyme activity; In addition, in the environment of pH5, the enzyme as acatalyst, TLC analyzed catalytic synthesis of products preliminarily.The research that Exiguobacterium sp. WGEA1producedβ-glucosidase and analyzed the catalytic results of the fermentation brothqualitatively, it laid thebasis for in-depth study of the enzyme catalyticefficiency from Exiguobacterium sp.WGEA1in the non-aqueousphase,laid the foundation to continue to study the biochenmical propertiesof the target strains,and thus it will have a good application prospect. |