Abstract
Cell culture of fig (Ficuscarica) was evaluated as a source of thermostable cysteine proteases. Extracts of 28 day old callus contained a benzoyl-arginine-p-nitroanilide (BAPNA) hydrolase activity of 2200 U/g dry wt (49.5 U/mg protein) at 25°C. Thermal stability and thermal denaturation (at 70°C) properties showed some similarities to those of commercial ficin (Sigma). High performance gel filtration revealed the presence of a peak with BAPNA hydrolase and caseinolytic activity which matched commercial ficin. Covalent chromatography using Thiopropyl Sepharose 6B (Pharmacia) demonstrated that approx 50% of the total BAPNA hydrolase activity could be attributed to thiol-proteins.
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