J. Agric. Food Chem. 1997, 45, 3826−3831
3826
Glycation of Proteinous Inhibitors: Loss in Trypsin Inhibitory Activity by the Blocking of Arginine and Lysine Residues at Their Reactive Sites Yasuko Kato*,† and Tsukasa Matsuda‡ Kawasaki University of Medical Welfare, 288 Matsushima, Kurashiki, Okayama 701-01, Japan, and Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University, Nagoya 464-01, Japan
Lysine-type trypsin inhibitors [Japanese quail ovomucoid (QOM) and Bowman-Birk inhibitor (BBI)], and arginine-type trypsin inhibitors [chicken ovomucoid (COM) and Kunitz soybean trypsin inhibitor (KSTI)] were modified with glucose by amino-carbonyl reaction at 50 °C and 65% relative humidity for 15 days. Free amino groups of inhibitors were blocked rapidly and decreased to
