2012food preservation scienceOpen access

Effect of Heat-denaturation of Milk Protein on the Baking Quality of Milk

Chihiro KIKUCHI, Daiki Oka, Hiroshi Ueno, Makoto Shiota, Tomohiro Noguchi, Katsumi Takano

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Abstract

The baking quality of heated (80℃, 30min) skim milk was higher than that of non-heated skim milk. The results of 2-dimensional gel electrophoresis (Blue native-PAGE/sodium dodecyl sulfate-PAGE) showed polymer formation between casein micelle, α-lactalbumin (α-La) and β-lactoglobulin (β-Lg). The α-La molecule was observed to interact with β-Lg, which was bound to κ-casein on the surface of the casein micelle with intermolecular disulfide bonds. The heated mixture of casein, α-La, and β-Lg reduced the decline in the baking quality of milk. However, α-La and β-Lg were the factors originally responsible for the decline in the baking quality. Thus, we observed that a heated polymer of casein, α-La, and β-Lg is an important factor determining the baking quality of milk.

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The baking quality of heated (80℃, 30min) skim milk was higher than that of non-heated skim milk. The results of 2-dimensional gel electrophoresis (Blue native-PAGE/sodium dodecyl sulfate-PAGE) showed polymer formation between casein micelle, α-lactalbumin (α-La) and β-lactoglobulin (β-Lg). The α-La molecule was observed to interact with β-Lg, which was bound to κ-casein on the surface of the casein micelle with intermolecular disulfide bonds. The heated mixture of casein, α-La, and β-Lg reduced the decline in the baking quality of milk. However, α-La and β-Lg were the factors originally responsible for the decline in the baking quality. Thus, we observed that a heated polymer of casein, α-La, and β-Lg is an important factor determining the baking quality of milk.

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Available abstract

The baking quality of heated (80℃, 30min) skim milk was higher than that of non-heated skim milk. The results of 2-dimensional gel electrophoresis (Blue native-PAGE/sodium dodecyl sulfate-PAGE) showed polymer formation between casein micelle, α-lactalbumin (α-La) and β-lactoglobulin (β-Lg). The α-La molecule was observed to interact with β-Lg, which was bound to κ-casein on the surface of the casein micelle with intermolecular disulfide bonds. The heated mixture of casein, α-La, and β-Lg reduced the decline in the baking quality of milk. However, α-La and β-Lg were the factors originally responsible for the decline in the baking quality. Thus, we observed that a heated polymer of casein, α-La, and β-Lg is an important factor determining the baking quality of milk.

Key concepts: Casein, Skimmed milk, Food science, Chemistry, Micelle, Denaturation (fissile materials), Disulfide bond, Sodium dodecyl sulfate

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