Molecular Insights into Cadaverine–Alkaline Phosphatase Interactions: Combined Spectroscopic and Computational Approaches

The relevance of enzyme stabilization is increasing with the growing number of enzyme applications. The lack of proper stability of enzymes in processing conditions is one of the significant problems associated with using enzymes in industrial biotechnology. Natural organic molecules, such as osmolytes, offer several advantages, including increased solubility in hydrophobic substrates. In this study, we examined the effect of cadaverine as an osmolyte on the stability and kinetics of bovine alkaline phosphatase (BALP). The results revealed that cadaverine binds to the enzyme and alters its absorption spectra. Additionally, cadaverine lowers the fluorescence spectrum of the enzyme through a static quenching mechanism. According to fluorescence and docking measurements, cadaverine interacts with BALP through hydrogen bonds and van der Waals interactions. The circular dichroism spectroscopy study showed that the presence of cadaverine alters the structure of BALP. Cadaverine also enhances BALP activity by increasing Km and Vmax. Molecular simulation results further supported cadaverine binding to BALP and its impact on the structure. Overall, these findings suggest that cadaverine has the potential to stabilize BALP.