In the present study, solid state fermentation was carried out using orange peel waste to produce β-glucosidase from Trichoderma viride. A locally isolated fungal strain T. viride was cultured in the solid state medi...In the present study, solid state fermentation was carried out using orange peel waste to produce β-glucosidase from Trichoderma viride. A locally isolated fungal strain T. viride was cultured in the solid state medium of orange peel (50% w/w moisture) under optimized fermentation conditions and maximum activity of 515 ± 12.4 U/mL was recorded after 4th day of incubation at pH 5.5 and 30℃. Indigenously produced β-glucosidase was subjected to the ammonium sulfate precipitation and Sephadex-G-100 gel filtration chromatography. In comparison to the crude extract β-glucosidase was 5.1-fold purified with specific activity of 758 U/mg. The enzyme was shown to have a relative molecular weight of 62 kDa as evidenced by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified β-glucosidase displayed 6 and 60℃ as an optimum pH and temperature respectively.展开更多
文摘In the present study, solid state fermentation was carried out using orange peel waste to produce β-glucosidase from Trichoderma viride. A locally isolated fungal strain T. viride was cultured in the solid state medium of orange peel (50% w/w moisture) under optimized fermentation conditions and maximum activity of 515 ± 12.4 U/mL was recorded after 4th day of incubation at pH 5.5 and 30℃. Indigenously produced β-glucosidase was subjected to the ammonium sulfate precipitation and Sephadex-G-100 gel filtration chromatography. In comparison to the crude extract β-glucosidase was 5.1-fold purified with specific activity of 758 U/mg. The enzyme was shown to have a relative molecular weight of 62 kDa as evidenced by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified β-glucosidase displayed 6 and 60℃ as an optimum pH and temperature respectively.
