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Effect of Hydrogen Peroxide and Heat on Some Characteristics of B-Lactoglobulin¹

Department of Food Science and Human Nutrition, Michigan State University, East Lansing 48823

ABSTRACT

Model systems of ß-lactoglobulin AB in simulated milk dialysate plus 5% lactose were treated with hydrogen peroxide (.01 to .lo%, w/v). Peroxide was dissipated with catalase before or after a heat treatment of 85 C for 12 min. No discernible changes in the composition and physical properties of the protein were encountered for samples subjected to hydrogen peroxide alone. However, when peroxide was present during the heat treatment, all the protein sulfhydryls were destroyed and partially (at .01% H₂O₂) or totally (at .l0% H₂O₂) , converted to cysteie acid. Methionine residues were reduced from 7 to 45% in the heated H₂O₂-containing samples. Neither methionine sulfoxide nor methionine sulfone was detected in the amino acid chromatograms.

Turbidity measurements and acrylamide gel electropherograms indicated that presence of peroxide during heat treatment inhibited aggregation of ß-lactoglobulin. Nonprotein nitrogen determinations on heated samples indicated that there was no significant breakdown in the peptide chain.

¹ Published with the approval of the Michigan Agricultural Experiment Station as Journal Article 5819.

² Present address: National Starch and Chemical Corp. Plainfield, New Jersey.