Isolation and purification of ficin from fig latex
1986
Kim, J.P. | Suh, J.S. | Kim, J.S. (Chungang Univ., Seoul (Korea R.). Dept. of Food Science and Technology)
Ficin, a proteolytic enzyme in fig latex, was extracted and purified with using ammonium sulfate and CM-cellulose column chromatography, respectively, and studied for its chemical properties. The disegel electrophoresis s howed one major and three minor bands for (NH4)2SO4 extract and only one band showed after CM-cellulose chromatography. The optimum conditions for ficin were 21.8% as acidic, 3.5% as basic and 74.7% as neutral amino acids. The amino acids analysis indicated that the ficin was composed of 174 amino acids residue having molecular weight of 19,500
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