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The effects of milk proteins on vanillin intensity reduction were studied in a phosphate buffer (pH 6.5) using urea and sodium dodecyl sulfate (SDS) as bond disrupting agents. The reduction of vanillin occurred immediately as the protein was introduced to the system. Bovine serum albumin (BSA) interacted more with vanillin than sodium caseinate (CAS) did. Heat treatment had no effect on vanillin reduction of the CAS system; however, free vanillin content was higher in the heated than nonheated BSA system. Hydrogen bonding appeared to be a major force for the interaction of vanillin and CAS. However, hydrophobic interaction seemed to be more important than hydrogen bonding in the vanillin and BSA system.