Abstract
ABSTRACTFig tree latex (ficin) was stepwise purified by ion exchange chromatography on carboxymethyl (CM)‐cellulose and gel filtration chromatography on Sephadex G‐100, and then utilized in the production of teleme. Following ion exchange chromatography, the milk clotting to proteolytic activity ratio (MCA/PA) increased from 1.97 to 3.1 and following gel filtration, to 7.4. The purified fraction gave better chemical and sensory properties than teleme made by fig tree latex. The protein content of teleme made by fig tree latex and the purified fraction were 3.90 and 6.50%, respectively. Syneresis in teleme decreased from 95% to 85% upon purification of the proteolytic enzymes. Exclusion of proteolytic activity appears to be essential to improve the quality of teleme.
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