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Light susceptibility of crocin and high degree of unsaturation limit its application in food systems. This study aimed to investigate the impact of molecular binding of crocin to β-lactoglobulin (β-LG) on crocin stability as well as the conformational stability of β-LG. The overall binding affinity was estimated about 1.74 × 10³ M⁻¹ through following UV spectral changes of β-LG at different concentrations of crocin. A 1:1 binding stoichiometry for the complex of crocin and β-LG was recognized using Job's method. The results of molecular docking and molecular dynamic simulation indicated that in addition to a single hydrogen bond with an oxygen linker attached to polyene chain, hydrophobic interactions play the major role in binding of crocin's polyene chain to β-LG surface. Three-dimensional emission and CD spectra showed conformational alterations in both tertiary and secondary structure of β-LG varying with crocin …