Study on the interaction between surfactin and alkaline protease in aqueous solution

The interaction between surfactin and alkaline protease in aqueous solution has been studied. Ultraviolet visible absorption spectra (UV-vis) show that surfactin causes the extension of peptide chain of the alkaline protease resulting in the weakening of hydrophobic interaction between the hydrophobic groups. Fluorescence spectra indicate that the interaction of surfactin with the tryptophan and tyrosine residues led to a change of conformation of the alkaline protease. Fourier transform infrared spectroscopy (FTIR) proves complex weak interactions between surfactin and alkaline protease, especially hydrogen bonds. Enzyme activity measurements demonstrate that low concentration of surfactin can increase the enzyme activity of alkaline protease, while high concentrations inhibit it. The particle size and Zeta potential measurements confirm that the system particle size and Zeta potential are dependent on the concentration of surfactin, in addition, there is the electrostatic interaction between surfactin and alkaline protease. Surface tension measurements indicate that the binds of surfactin and alkaline protease molecules are spontaneous. Based on experimental results, the composite model of surfactin and alkaline protease in aqueous solution is proposed.