[Levanase from Fusarium solani-68].
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.
D001426:Bacterial Proteins; D005630:Fructans / Q000302:isolation & purification / Q000378:metabolism; D005670:Fusarium / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013696:Temperature
D001426:Bacterial Proteins; D005630:Fructans; D006026:Glycoside Hydrolases; C021512:levanase
O levanaze Fusarium solani 68.