加熱殺菌方法の異なる市販牛乳タンパク質のペプシンによる消化性

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タイトル別名
  • Peptic Digestibility of Proteins in Different Heat-treated Commercial Cow's Milks.
  • カネツ サッキン ホウホウ ノ コトナル シハン ギュウニュウ タンパクシツ

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Three types of commercially available heat-treated milk (low temperature long time-treated milk (LTLT milk), high temperature short time-treated milk (HTST milk) and ultra-high temperature-treated milk (UHT milk)) were evaluated for their peptic digestibility using 16% SDS-polyacrylamide gel electrophoresis and Western blot analysis wish anti-bovine casein, anti-bovine β-lactoglobulin (β-LG) and antibovine α-lactalbumin (α-LA) antibodies. The digestion profile of casein was similar for all the types of milk, and the intact proteins of casein disappeared rapidly upon peptic digestion. α-LA in the LTLT and HTST milks was more resistant than casein to peptic digestion, and this resistance was also maintained in UHT milk, although to a lesser extent. Similarly, β-LG in the LTLT and HTST milks was resistant to peptic digestion, but this resistance was almost lost in UHT milk, so that β-LG in UHT milk was easily digested by pepsin, in a similar manner to casein. In rats, β-LG in UHT milk was digested more rapidly in the stomach than that in HTST milk. These results indicate that α-LA and β-LG differ in their peptic digestibility among different heat-treated milks, and that loss of resistance to peptic digestion of β-LG in UHT milk may have important consequences for reducing its allergenic properties.

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