Dina Ali - Plant Biotechnology Department, College of Biotechnology, Al- Nahrain University, Baghdad, Iraq
Ahmed Ahmed - Chemistry Department, College of Science, Al- Nahrain University, Baghdad, Iraq
Alaa J. Alqaisi - Chemistry Department, College of Science, Al- Nahrain University, Baghdad, Iraq

This study focuses on synthesizing three pyrazole derivatives, namely B, C, and D. Fourier transform infrared spectroscopy (FTIR) and proton nuclear magnetic resonance spectroscopy (۱H-NMR) were used to study the synthesized derivatives. Pyrazole derivative B was produced from the chalcone derivative (A) reaction with (۴-nitrophenyl) hydrazine. The pyrazole derivatives C and D were produced from the reaction of chalcone derivative (A) with hydrazide derivatives (N-(۲-oxopropyl)benzamide and ۳-acetyl-۱-cyclopropyl-۶-fluoro-۷-(piperazine-۱-yl)quinolin-۴(۱H)-one), respectively. The Purification of α-amylase was conducted on pancreatic cancer patients from Iraq, employing three distinct purifying techniques. The experiment yielded a high level of enzyme activity, specifically ۷ U/mL and a specific activity of ۸.۷۵ U/mg protein. These results were achieved using an ammonium sulfate saturation ratio of ۶۵%. The graph shows a peak in enzyme activity at ۳.۷۵ U/mL in the elution area. This peak, fraction ۵۵, has ۱۱.۳ U/mg protein activity. The stability of α-amylase was constant over a pH range of ۵.۰ to ۹.۰. In the pH range of ۶ to ۷, enzyme stability is highest at pH ۷. At pH ۵ and ۹, strength decreased. The enzyme was less active at pH ۵ and ۶ but more active at pH ۷ and ۹. However, enzyme activity peaked at pH ۸.۰. The α-amylase enzyme maintained ۱۰۰% activity at ۲۷-۳۷ °C, demonstrating stability. However, enzyme activity decreased to ۵۰% at ۴۷ °C when temperature increased. The inhibitory effect of bis-chalcone and pyrazole derivatives increased with concentration. The results show that compound B has the most significant inhibitory efficacy, at ۵۰%.

cancer, Pancreatic cancer, Pyrazole, α-amylase