Purification and Properties of F-I_a, a β-1, 3 Glucanase Which is Highly Lytic toward the Cell Walls of Pilicularia oryzae P₂

Abstract

F-I_a which showed the highest lytic activity toward Piricularia oryzae P₂ cell walls among the six multiple β-1, 3 glucanases produced by Bacillus circulans WL 12 was purified and some of its properties were studied. The preparation was homogeneous by disc polyacrylamide gel electrophoresis at pH 9.4 and 4.0. The molecular weight was estimated to be around 48, 000. F-I_a hydrolyzed laminarin by a random mechanism. The enzyme liberated glucose, oligosaccharides and a high molecular weight heteroglycan from Piricularia oryzae P₂ cell walls. Heteroglycan showed a singles edimentation peak in ultracentrifugation and contained mannose, glucose and galactose.