Plant aspartic proteinases (APs) from Withania coagulans were extracted by using NaCl (0.85%) and were characterized by pH, temperature stability, rennet strength and CaCl 2 supplementation. Additionally, the milk-clotting enzyme was partially purified by fractional precipitation with ammonium sulphate and acetone followed by column chromatography of the most active fraction, giving specific activity of 12 307.6 U/mg. The maximum enzyme activity was observed at 4.25 pH and 37°C, which suggested its use in making cheese requiring moderate temperatures (Mozerella, Cheddar). The enzymatic activity increases as the concentration of CaCl 2 increases and decreases with the increase of temperature. SDS analysis showed the presence of a single unique band having a molecular weight of 66 KDa.
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