[Identification of catalytically active groups in inulinase from Bacillus polymyxa 722]. / Identifikatsiia kataliticheski aktivnykh grupp inulinazy Bacillus polymyxa 772.

Inulinase from Bacillus polymyxa 722 hydrolyzing a polyfructosan inulin was studied. The dependence of inulinase activity on pH, measurements of pK value, calculation of 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 cleavage of beta-2,1-fructoside bonds in the inulin molecule with inulinase is considered.

[Biosynthesis of inulinases by Bacillus bacteria]. / Biosintez inulinaz bakteriiami roda Bacillus.

Biosynthesis of extracellular inulinase by bacteria Bacillus polymyxa 29, B. polymyxa 722, and B. subtilis 68 was studied. The optimal parameters for the producer growth were as follows: pH 7.0, 33-35 degrees C, the growth duration within 72 h. The presence of mineral reduced or of organic nitrogen was necessary for the enzyme biosynthesis. The inulinase biosynthesis was sharply activated in the presence of carbohydrates. B. polymyxa 722 and B. polymyxa 29 displayed the maximal activity on a starch-containing culture medium, the maximal activity of B. subtilis 68 was found in the presence of sucrose. Inulin did not induce the inulinase biosynthesis by the strains studied. The time course of bacteria growth and of the enzyme biosynthesis was studied.