In this paper, several spectroscopic techniques were used to investigate the interaction of engeletin (ELN) with bovine serum albumin (BSA). The analysis of UV-Vis absorption and fluorescence spectra revealed that ELN and BSA formed a static complex ELN-BSA, and ELN quenched the fluorescence of BSA effectively. According to the thermodynamic parameters ΔS(0) = 47.27 J·mol(-1)·K(-1) and ΔΗ(0) = -10.34 kJ·mol(-1), the hydrophobic and hydrogen bond interactions were suggested to be the major interaction forces between ELN and BSA. Raman spectroscopy indicated that the binding of ELN slightly changed the conformations and microenviroment of BSA and decreased the α-helix content of BSA.