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Characterization of milk coagulating properties from the extract of Withania coagulans
- NAZ, SHEHLA, MASUD, TARIQ, NAWAZ, MALIK ADIL
- International journal of dairy technology 2009 v.62 no.3 pp. 315-320
- Withania coagulans, acetone, ammonium sulfate, aspartic proteinases, calcium chloride, cheesemaking, chromatography, enzyme activity, milk, milk clotting, molecular weight, pH, rennet, sodium chloride, temperature
- Plant aspartic proteinases (APs) from Withania coagulans were extracted by using NaCl (0.85%) and were characterized by pH, temperature stability, rennet strength and CaCl₂ 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 CaCl₂ 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.