The interaction between yeast β-glucan and myosin and its effects on flavor adsorption capacity of myosin were investigated in the present study. The effects of yeast β-glucan with different additive amounts on the structures of myosin and flavor binding capacity were determined by Zeta potential analysis， UV spectra， fluorescence spectroscopy， Raman spectroscopy and gas chromatography-mass spectrometry technology. The results showed that， with the increase of yeast β-glucan， the solubility， absolute value of zeta potential， surface hydrophobicity and active sulfhydryl content of myosin increased firstly and then decreased. The intrinsic fluorescence intensity of myosin decreased gradually， while the intensity of the UV absorption increased gradually. When the additive level of yeast β-glucan was 0-2%， the α-helix content decreased significantly (P < 0.05)， while the content of β-sheet increased significantly (P < 0.05). When the additive level was more than 2%， the content of α-helix increased gradually and the β-sheet decreased. The incorporation of yeast β-glucan promoted the unfolding of myosin structure， enhancing the binding ability of protein and selected flavor compounds. When the additive amount of yeast β-glucan exceeded 2%， the flavor binding ability of protein was not significantly increased.