Identification of Catalytically Active Groups in Inulinase from Bacillus polymyxa 722


    loading  Checking for direct PDF access through Ovid

Abstract

Inulinase from Bacillus polymyxa 722, hydrolyzing a polyfructosan inulin, was studied. The dependence of inulinase activity on pH, measurements of pK value, calculation of the ionization heat, photoinactivation with methylene blue, and inhibition with p-chloromercuribenzoate suggest that the active center of this enzyme contains imidazole and sulfhydryl groups. A possible mechanism underlying the cleavage of β-2,1-fructoside bonds in the inulin molecule by inulinase is considered.

    loading  Loading Related Articles