Extraction, Partial Purification and Utilization of Milk Coagulating Enzyme from Kiwifruit (Actinidia Deliciosa) in Fresh Cheesemaking

The study aimed to determine the potential of kiwifruit milk clotting enzyme in cheesemaking. crude enzyme, extracted with sodium phosphate buffer (pH 7.0), was partially purified by 30-80% ammonium sulfate precipitation. 50% saturation exhibited maximum activity (MCA), along 1.56 purification fold, and 78.84% recovery. From SDS-PAGE analysis, protease showed two bands a molecular mass 24 kDa 23 respectively. optimum conditions (temperature pH milk) for minimum time coagulation (TOC) MCA were determined response surface methodology (RSM). numerical optimization study, cheesemaking 6.5 temperature 55oC, having 0.94 desirability. cheese prepared had significantly (p<0.05) higher moisture, ash, calcium content, yield than rennet cheese, while lower fat content acidity observed coagulated cheese. However, non-significant (p>0.05) difference protein obtained between both cheeses. This highlighted that has ability be used as an efficient fresh