Multispectroscopic studies on the interaction of maltol, a food additive, with bovine serum albumin

► Interaction of maltol and bovine serum albumin (BSA) is investigated by multispectroscopic techniques. ► Maltol can quench the fluorescence of BSA through a static quenching procedure. ► The binding of maltol to BSA is driven mainly by hydrophobic interactions. ► Subdomain IIA (Sudlow site I) of BSA is found to be the main binding site for maltol. ► The secondary structure of BSA has been changed in the presence of maltol.