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J. Biochem, 2004, Vol. 135, No. 3 421-427
© 2004 The Japanese Biochemical Society

BIOCHEMISTRY

Inhibitory Effect of 0.19 {alpha}-Amylase Inhibitor from Wheat Kernel on the Activity of Porcine Pancreas {alpha}-Amylase and Its Thermal Stability

Hiroshi Oneda, Seungjae Lee and Kuniyo Inouye*

Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502

The inhibitory effect of 0.19 {alpha}-amylase inhibitor (0.19 AI) from wheat kernel on the porcine pancreas {alpha}-amylase (PPA)–catalyzed hydrolysis of p-nitrophenyl-{alpha}-D-maltoside (pNP-G2) was examined. 0.19 AI is a homodimer of 26.6 kDa with 13.3-kDa subunits under the conditions used. The elution behaviors in gel filtration HPLC of PPA and 0.19 AI indicated that a PPA molecule bound with a 0.19 AI molecule (homodimer) at a molar ratio of 1:1. 0.19 AI inhibited PPA activity in a competitive manner with an inhibitor constant, Ki, of 57.3 nM at pH 6.9, 30°C, and the binding between them was found to be endothermic and entropy-driven. The activation energy for the thermal inactivation of 0.19 AI was determined to be 87.0 kJ/mol, and the temperature, T50, giving 50% inactivation in a 30-min incubation at pH 6.9 was 88.1°C. The high inhibitory activity of 0.19 AI against PPA and its high thermal stability suggest its potential for use in the prevention and therapy of obesity and diabetes.

* To whom correspondence should be addressed. Tel: +81-75-753-6266, Fax: +81-75-753-6265, E-mail: inouye{at}kais.kyoto-u.ac.jp


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