Purification and characterisation of ,B-l,3-giucanase from trichodenna harzianum BIO 10671

• Main Authors: Mustafa, Muskhazli, Ramli, Salfarina, Ithnin, Nalisha, Tohfah, Nor Farizan
• Format: Article
• Language: English
• Published: Universiti Putra Malaysia Press 2005
• Online Access: http://psasir.upm.edu.my/id/eprint/3653/1/Purification_and_Characterisation_of_%2CB-l%2C3-giucanase_from.pdf; http://psasir.upm.edu.my/id/eprint/3653/; http://www.pertanika.upm.edu.my/Pertanika%20PAPERS/JTAS%20Vol.%2028%20(1)%20Apr.%202005/JTAS%20Vol.28%20(1)%202005%20(23-31).pdf

B-1,3-glucanase enzyme from culture filtrate of Trichoderma harzianum BIO 10671 was successively purified by precipitation with 80%acetonefollowed by anion-exchange chromatography on Neobar AQ and chromatofocusing on a Mono P HR 5/20 column. Two {3-1,3-glucanases of 32kDa and 66kDa were purified to homogeneity as judged by SDS-PAGE. The pH aptimum far the enzymes activity was pH 4-5 and maximum activity was obtained at 4YG. Enzyme activity was slightly inhibited by 20-45% in its activity by 20mM of Zn2+, Ca2+, Co2+, Mi+, Cu2+, Mn2+and Fe2+. The highest f3-1,3-glucanase hydrolysis activity was obtained on laminarin due to the similarity on f3-glucosidic bonds and followed on pustulan, glucan and cellulose, respectively.