Effects of phytic acid on the digestion of casein and soybean protein with trypsin, pancreatin or pepsin.

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  • INAGAWA Junichi
    Department of Agricultural Chemistry, Faculty of Agriculture, Tamagawa University
  • KIYOSAWA Isao
    Department of Agricultural Chemistry, Faculty of Agriculture, Tamagawa University
  • NAGASAWA Taro
    Department of Agricultural Chemistry, Faculty of Agriculture, Tamagawa University

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Other Title
  • トリプシン，パンクレアチンおよびペプシンによるカゼインおよび大豆タンパク質の消化性に及ぼすフィチン酸の影響
  • トリプシン パンクレアチン オヨビ ペプシン ニ ヨル カゼイン オヨビ ダイ

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The effects of phytic acid on the digestion of casein and soybean protein with trypsin, pancreatin or pepsin were examined by determining the concentrations of amino groups released from the reaction mixture using the TNBS method. Phytic acid did not affect the proteolysis of either casein or soybean protein by trypsin or pancreatin. The disc gel electrophoretic patterns of these proteins treated with trypsin also confirmed that the presence of phytic acid did not affect the proteolysis. The addition of Ca2+ ion up to a concentration of 50mM slightly lowered trypsin activity in the presence or absence of phytic acid. Peptic digestivities of the proteins decreased with phytic acid concentration. The addition of Ca2+ ion up to a concentration of 50mM showed no effect on peptic activity in the presence or absence of phytic acid. Disc gel electrophoretic patterns indicated that the peptic digestivities of αs-and β-caseins and 7S globulin decreased with phytic acid concentration, and that the digestivity of 11S globulin was not influenced to such an extent as that of 7S globulin. The inhibition by phytic acid was considered to occur as a result of an interaction of phytic acid with the proteins, rather than with pepsm.

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