Production and some properties of two chitosanases fromBacillus alvei

Abstract

Bacillus alvei, a potent chitosanase producer, secreted an extracellular chitosan‐degrading enzyme in the absence of chitosan. Extracellular secretion of chitosanase reached levels corresponding to 2.3 U/ml after less than two days. The enzyme was purified by precipitation with ammonium sulfate followed by CM‐cellulose chromatography. Two chitosanases, chitosanase A and B were purified from the culture fluid. Chitosanase A exhibited substrate specificity for chitosan, while chitosanase B possessed comparable specific activities toward glycol chitin and colloidal chitin. The apparent Km and Vmax, determined at 37 °C and pH 5.6, were 0.8 mg/ml and 2.5 μmol/min, respectively. The enzyme showed an endo‐splitting type of cleavage reaction and the end products of chitosan hydrolysis were oligomeric products.

Chitosan Modification and Pharmaceutical/Biomedical Applications

“…The specific enzyme for chitosan hydrolysis has been found in a wide range of organisms, including bacteria [8,9], fungi [10,11] and plants [12]. Most of these chitosanases are characterized as endo-type and they split β-1,4 glycosidic linkages in chitosan in a random way to form chitosan oligomers.…”