Purification and Some Properties of β-1, 3-Glucanase of Suspension-cultured Tobacco Cells

Abstract

A laminaran-hydrolyzing enzyme was purified from the homogenate of suspension-cultured tobacco cells by the treatment with ion-exchangers and gel filtration. The purified enzyme was homogenious in disc-electrophoresis and was a basic protein. The optimal pH of the enzyme was 5.0. The enzyme was stable at temperature below 40°C. The inhibitory effect of Hg²⁺ Cu²⁺ and Ag⁺ was observed. Investigation of the hydrolysis product revealed that the enzyme attacked laminaran endo-wise to form laminari-tetraose, -triose, -biose and glucose.