Interaction and Antioxidant Activities of Phlorizin and Bovine Hemoglobin in Three Different Solvents

The interaction of bovine hemoglobin(BHb)and phlorizin(PHL)and its effects on antioxidant activities of PHL were investigated using ultraviolet spectra,fluorescence spectra,synchronous fluorescence spectra,infrared spectra methods and DPPH and ABTS free radical scavenging assays in deionized water(dH₂O),10%dimethyl sulfoxide(DMSO)and 10% ethanol(EtOH),respectively. The results showed that PHL had a great ability to quench BHb's fluorescence with the increase of PHL concentration,quenching mechanism was an on-radiative energy transfer in static modes,interaction force was driven mainly by Vander Waals forces and hydrogen bond,and PHL was much closer to Trp residue in three different solvents. The slight red shifts for amide band Ⅰ and amide band Ⅱ were observed in dH₂O. The scavenging effects of PHL-BHb on DPPH and ABTS free radical all increased compared with PHL except for 10% EtOH-DPPH. This study showed that the interaction of BHb and PHL and its activities could be influenced by solvents polarity in different degrees.