At 1600µg/ml, the greatest percentage of denaturation of egg albumin was inhibited by synthesized acetophenone (89.16±0.38%). At the greatest concentration, the synthesized acetophenone showed a significant effect of obstructing protein denaturation in a dose-dependent manner. It was investigated whether the synthesized acetophenone could keep BSA from becoming denaturated. Synthesized acetophenone demonstrated the greatest percentage denaturation of BSA to be 76.59±0.56% at 1600µg/ml. The RBC membrane was stabilized by the synthesized acetophenone in a dose-dependent manner, with the maximum stability occurring at 1600 µg/ml. At 1600 µg/ml, the greatest percentage inhibition of RBC membrane lysis (91.15±0.31%) was observed, in contrast to DS (90.01±0.02%) and piroxicam (80.34±0.29%). The highest and lowest levels of trypsinase activity hindrance were seen at 1600µg/ml and 50µg/ml, respectively, for the synthesized acetophenone. The greatest percentage of trypsinase activity suppression was found to be 83.94±0.24.