A novel approach for the waste industry: Investigating the impact of synthetic acetovanilone derivatives on thermophilic recombinant xylanase and its enzymatic effects.

In this study, acetovanillone derivative compounds (1–7) were synthesized, and their structures were analyzed using nuclear magnetic resonance (¹H NMR—¹³C NMR)and Fourier-transform infrared (FTIR) methods. The xylanase gene within the scope of the study was cloned using recombinant DNA techniques. The purified recombinant protein was subjected to comprehensive characterization, including assessment of pH stability, temperature dependency, and substrate specificity. The optimal temperature and pH for the enzyme were determined to be 72 ºC and 6.0, respectively. Investigations were done into how the synthetic compounds affected the xylanase enzyme. Especially compound 2 increased the activity at concentrations of 0.1, 0.3, 0.5 and 0.7 mM by 176.9, 153.25, 146.22 and 115.41%, respectively, compared to the positive control. It has also been observed that the effect on activity decreases with increasing concentration. Compound 3, on the contrary, increased the activity at high concentrations (0.7 and 1 mM) by 147.30 and 153.93%, respectively. Considering the positive sample (100%), CaCI₂ shows 70.38% activity at 0.1 mM, 68.04% at 0.3 mM, 79.96% at 0.5 mM, 61.99% at 0.7 mM, and 85.59% at 1 mM.These results show that CaCI₂ causes a slight decrease in enzyme activity.ZnCI₂, the zinc compound, and CuCI₂, the copper compound, showed a similar decrease in activity. It was determined that these different reactions showed different relative activity of the metal ions at varying concentrations for the recombinant xylanase enzyme. [ABSTRACT FROM AUTHOR]