Dina Naseer Ali; Ahmed Ahmed; Alaa Hussein J. Alqaisi
Abstract
This study focuses on synthesizing three pyrazole derivatives, namely B, C, and D. Fourier transform infrared spectroscopy (FTIR) and proton nuclear magnetic resonance spectroscopy ...
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This study focuses on synthesizing three pyrazole derivatives, namely B, C, and D. Fourier transform infrared spectroscopy (FTIR) and proton nuclear magnetic resonance spectroscopy (1H-NMR) were used to study the synthesized derivatives. Pyrazole derivative B was produced from the chalcone derivative (A) reaction with (4-nitrophenyl) hydrazine. The pyrazole derivatives C and D were produced from the reaction of chalcone derivative (A) with hydrazide derivatives (N-(2-oxopropyl)benzamide and 3-acetyl-1-cyclopropyl-6-fluoro-7-(piperazine-1-yl)quinolin-4(1H)-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 7 U/mL and a specific activity of 8.75 U/mg protein. These results were achieved using an ammonium sulfate saturation ratio of 65%. The graph shows a peak in enzyme activity at 3.75 U/mL in the elution area. This peak, fraction 55, has 11.3 U/mg protein activity. The stability of α-amylase was constant over a pH range of 5.0 to 9.0. In the pH range of 6 to 7, enzyme stability is highest at pH 7. At pH 5 and 9, strength decreased. The enzyme was less active at pH 5 and 6 but more active at pH 7 and 9. However, enzyme activity peaked at pH 8.0. The α-amylase enzyme maintained 100% activity at 27-37 °C, demonstrating stability. However, enzyme activity decreased to 50% at 47 °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 50%.