Identification of Catalytically Active Groups in Inulinase from Bacillus polymyxa 722

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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.

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