Gadallah,, M. (2004). PRODUCTION, PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR ALKALINE PROTEASE FROM ISOLATED TRICHODERMA VIRIDE.. Journal of Soil Sciences and Agricultural Engineering, 29(10), 6015-6023. doi: 10.21608/jssae.2004.243878
M. A. Gadallah,. "PRODUCTION, PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR ALKALINE PROTEASE FROM ISOLATED TRICHODERMA VIRIDE.". Journal of Soil Sciences and Agricultural Engineering, 29, 10, 2004, 6015-6023. doi: 10.21608/jssae.2004.243878
Gadallah,, M. (2004). 'PRODUCTION, PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR ALKALINE PROTEASE FROM ISOLATED TRICHODERMA VIRIDE.', Journal of Soil Sciences and Agricultural Engineering, 29(10), pp. 6015-6023. doi: 10.21608/jssae.2004.243878
Gadallah,, M. PRODUCTION, PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR ALKALINE PROTEASE FROM ISOLATED TRICHODERMA VIRIDE.. Journal of Soil Sciences and Agricultural Engineering, 2004; 29(10): 6015-6023. doi: 10.21608/jssae.2004.243878
PRODUCTION, PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR ALKALINE PROTEASE FROM ISOLATED TRICHODERMA VIRIDE.
Microbal Biotechnology, Dept. National Research center Dokki, Cairo, Egypt
Abstract
The production and purification of alkaline protease from local strain of the Egyptian soil fungus trichoderrna viridi was investigated. The enzyme which hydrolyze casein was produced at high level when fungus was grown for 6 days on a medium supplemented with 1.5% wlv starch as a carbon source, soybean flower (0.14% N2) as a nitrogen source and initial pH 6.5 at 28·C. A 30.06 fold purified enzyme was obtained by acetone precipitation flowed by gel filtration using sephadix G-100. Protease was found to be highly active at pH 8.5 and 55·C, and stable up to 60 min at pH 7 and 50·C. Mutations Zn2+, Mn2+ and Cu2+ activated the enzyme, whereas C02+, Fe2+ and k+ inhibited the enzyme activity. The activity of enzyme was found to be stable in liquid detergent (locally producer).
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