PERTANIKA JOURNAL OF TROPICAL AGRICULTURAL SCIENCE

ß-l,3-glucanase enzyme from culture filtrate of Trichoderma harzianum BIO 10671 was successively purified by precipitation with 80% acetone followed by anion-exchange chromatography on Neobar AQ and chromatofocusing on a Mono P HR 5/20 column. Two ß-l,3-glucanases of 32kDa and 66kDa were purified to homogeneity as judged by SDS-PAGE. The pH optimum for the enzymes activity was pH 4-5 and maximum activity was obtained at 45°C. Enzyme activity was slightly inhibited by 20-45% in its activity by 20mM of Zn2+, Ca2+, Co2+, Mg2+Cu2+ Mn2+ and Fe2+. The highest ß-l,3-glucanase hydrolysis activity was obtained on laminarin due to the similarity on ß-glucosidic bonds and followed on pustulan, glucan and cellulose, respectively.