Abstract:

The aim was to provide the basis for the isolation and purification of β-1,3-glucanase and chitinase, and the use of mycoparasite. β-1,3-glucanase and chitinase were isolated from two mycoparasites (TR1 and TR2) of Cronartium ribicola. The enzymatic activities of β-1,3-glucanase and chitinase were detected. The results showed that optimum temperature of β-1,3-glucanase from TR1 and TR2 was 35℃. The optimum pH of β-1,3-glucanase from TR1 was 4.0 and Km was 43.82 μg/mL. Ca2+ was activator of the enzyme and Cu2+, Fe3+, Al3+, Zn2+ were inhibitors. The optimum pH of β-1,3-glucanase from TR2 was 5.0 and Km was 71.28 μg/mL. Ca2+ and Mn2+ were activators of the enzyme and Cu2+, Fe3+, Al3+ were inhibitors. Activators of chitinase from TR1 and TR2 were Mn2+ and Ca2+ and inhibitor was Cu2+. The optimum temperature of chitinase from TR1 was 40℃ and the optimum pH was 6.0, Km of the enzyme was 92.49 μg/mL. The optimum temperature of chitinase from TR2 was from 30℃ to 50℃. The optimum pH was 5.0 and Km was 71.11 μg/mL. β-1,3-glucanase and chitinase produced by TR1 and TR2 possess high stability, so that it was feasible to use crude enzyme directly in field control of blister rust.