Study of alkaline phosphatase interaction with putrescine using multi-spectroscopic and docking methods.

The vast application of enzymes in various industries has encouraged scientists to optimize enzymes activity and stability. Solvent engineering is a well-known method used for stabilizing enzymes. Putrescine is a polyamine that can serve as as an enzyme stabilizer. In this study, the structure and activity of bovine alkaline phosphatase (BALP) were studied in the presence of putrescine. The results confirmed that putrescine could bind to BALP and change the UV-vis spectra of the enzyme. Moreover, putrescine quenched the BALP fluorescence spectra by static quenching mechanism. Putrescine interacted with BALP spontaneously by different forces such as van der Waals and hydrogen bonding. Circular dichroism spectra studies also revealed that the BALP structure was changed in the presence of putrescine. Furthermore, the kinetic parameters showed that BALP was activated by putrescine. Moreover, docking studies confirmed that hydrogen bonds, van der Waals forces and hydrophobic interactions played the major role in the BALP-put complex formation. In general, these results showed that putrescine could modify the BALP activity and structure.

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