Purification and Characterization of a Major Trypsin Inhibitor, FMTI-II, from Foxtail Millet Grain
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概要
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A major trypsin inhibitor was purified from the extract of the whole grain of foxtail millet, Setaria italica, to an electrophoretically homogeneous protein by conventional methods. This inhibitor (FMTI-II) has a molecular weight of 7500 and contains high levels of basic amino acids, acidic amino acids, prolinc, and half-cystine. FMTI-II inhibited bovine and hog trypsins in a 1:1 (M/M) stoichiometry: the Ki values were 3.0 × 10-11 M and 2.2 × 10-10 M, respectively. Bovine α-chymotrypsin, subtilisin BPN, hog pepsin, and papain were not inhibited. The inhibitor was stable in a wide range of pH and was heatresistant at acidic pH. The chemical modification suggested that FMTI-II had a Lys-X bond as a trypsin reactive-site. FMTI-II resembles rice bran and wheat germ trypsin inhibitors, showing that it is a Bowman-Birk type inhibitor.
- 社団法人 日本農芸化学会の論文
著者
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Tashiro Misao
Department Of Food Science And Nutrition Faculty Of Living Science Kyoto Prefectural University
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Katayama Yoshiho
Department Of Food And Nutrition Faculty Of The Science Of Living Osaka Clty University
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MAKI Zensuke
Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University
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KIHIRA Yuko
Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University
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KATAYAMA Yoshiho
Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University
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