
Extracellular levanase was isolated from the culture of Fusarium solani-68 by ammonium sulfate precipitation at 0.8 saturation and purified in part by Sephadex G-150 gel chromatography. Levanase showed maximum activity at pH = 6.0 and t = 45 degrees C. The levanase reaction (hydrolysis of high molecular levane with a molecular weight of 1--5 min) reached a maximum rate at a polysaccharide concentration of 6.7 mg/ml, Michaelis constant being 1.5 X 10(-6) M. Levanase remained stable at pH 5.4--7.5 and temperature 40--45 degrees C.
Kinetics, Bacterial Proteins, Fusarium, Glycoside Hydrolases, Temperature, Hydrogen-Ion Concentration, Fructans
Kinetics, Bacterial Proteins, Fusarium, Glycoside Hydrolases, Temperature, Hydrogen-Ion Concentration, Fructans
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