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Mechanisms of Interaction Between Vanillin and Milk Proteins in Model Systems
Author(s) -
Chobpattana W.,
Jeon I.J.,
Smith J.S.,
Loughin T.M.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb09438.x
Subject(s) - vanillin , chemistry , bovine serum albumin , hydrogen bond , urea , sodium dodecyl sulfate , hydrophobic effect , model system , sodium , chromatography , food science , biochemistry , organic chemistry , molecule , computational chemistry
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.