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MILK PROTEIN/STAINLESS STEEL INTERACTION RELEVANT TO THE INITIAL STAGE OF FOULING IN THERMAL PROCESSING
Author(s) -
KIM J.C.,
LUND D.B.
Publication year - 1998
Publication title -
journal of food process engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 45
eISSN - 1745-4530
pISSN - 0145-8876
DOI - 10.1111/j.1745-4530.1998.tb00459.x
Subject(s) - adsorption , chemistry , casein , fouling , matrix (chemical analysis) , phosphate , langmuir adsorption model , chromatography , analytical chemistry (journal) , thermodynamics , organic chemistry , biochemistry , membrane , physics
Effect of temperature and surface preconditioning on β‐lactoglobulin (β‐lg) adsorption onto stainless steel have been studied using column adsorption chromatography. As temperature increased from 25 to 85C, amount of adsorbed β‐lg increased gradually and eventually reached a plateau value. Above 85C, slope of the adsorption boundary curve was significantly less than that at lower temperatures suggesting that the association constant for Langmuir adsorption isotherm increased. Conformation change caused by heat treatment also resulted in higher amount of adsorption at equilibrium (1.65 mgm −2 ) than native β‐lg (0.7 mgm −2 ) at 25C. Adsorption behavior of k‐casein was different from that of β‐lg as reflected in the shape of the adsorption curve as well as the amount of adsorption at equilibrium. A significant amount of k‐casein was adsorbed onto a β‐lg saturated surface, whereas no additional adsorption of β‐lg occurred onto a k‐casein saturated surface. These observations were in agreement with previous work. Favorable adsorption of β‐lg onto calcium phosphate‐deposited stainless steel suggests the formation of calcium phosphate/β‐lg matrix in multilayer deposit during the thermal processing of milk.