Abstract：The interaction of mangiferin with trypsin under physiological condition was studied using fluorescence,three-dimensional fluorescence and circular dichroism spectroscopy.The results showed that the probable quenching mechanism of fluorescence of trypsin by mangiferin was a static quenching by forming the ground-state MA-trypsin complex.The thermodynamic parameters,enthalpy change(ΔH) and entropy change(ΔS) were calculated to be 70.45 kJ·mol-1 and 321.90 J·mol-1·K-1 via the van’t Hoff equation,which suggested that the hydrophobic interactions plays major role in the binding of mangiferin to trypsin.The binding locality was an area 3.99 nm away from tryptophan residue in trypsin based on the Frster theory of non-radioactive energy transfer.Analysis of three-dimensional fluorescence and CD spectra showed that the binding of mangiferin to trypsin could induce partial changes in the secondary structure of the protein. 更多
2012, Vol. 34 
