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Hypoglycaemic and anorexigenic activities of an α-amylase inhibitor from white kidney beans (Phaseolus vulgaris) in Wistar rats

Published online by Cambridge University Press:  09 March 2007

M. A. Tormo ,
I. Gil-Exojo ,
A. Romero de Tejada  and
J. E. Campillo
M. A. Tormo*
Affiliation:
Department of Physiology, Faculty of Medicine, University of Extremadura, Apartado de Correos 108, 06071, Badajoz, Spain
I. Gil-Exojo
Affiliation:
Department of Physiology, Faculty of Medicine, University of Extremadura, Apartado de Correos 108, 06071, Badajoz, Spain
A. Romero de Tejada
Affiliation:
Department of Physiology, Faculty of Medicine, University of Extremadura, Apartado de Correos 108, 06071, Badajoz, Spain
J. E. Campillo
Affiliation:
Department of Physiology, Faculty of Medicine, University of Extremadura, Apartado de Correos 108, 06071, Badajoz, Spain
*
*Corresponding author: Dr M. A. Tormo, fax +34 924 289437, email, matormo@unex.es
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Abstract

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An inhibitor of α-amylase was isolated and purified from an extract of white kidney beans (Phaseolus vulgaris). The acute oral administration of the inhibitor (50 mg/kg body weight) to adult Wistar rats together with a starch load (2 g/kg body weight suspended in NaCl (9 g/l)) reduced the increase in glycaemia over the basal value (NaCl, 222 (SEM 49); inhibitor, 145 (SEM 16) mmol/l×180 min; P<0.05) without modifying the insulin response. On administering the inhibitor orally (50 mg/kg body weight dissolved in NaCl (9 g/l)) for 21 d to rats fed on a standard diet, a decline was observed in the glycaemia values on day 0 (NaCl, 5.53 (SEM 0.12); inhibitor, 5.25 (SEM 0.16) mmol/l) relative to those obtained on days 10 (NaCl, 5.00 (SEM 0.14); inhibitor, 4.60 (SEM 0.08) mmol/l; P<0.05) and 21 (NaCl, 5.22 (SEM 0.22); inhibitor, 4.50 (SEM 0.12) mmol/l; P<0.01) of treatment, without modifying the plasma concentration of insulin. There was found to be a significant anorexigenic action of the inhibitor; there was reduced food intake (NaCl, 23.07 (SEM 0.31); inhibitor, 19.50 (SEM 0.49) g/d; P<0.01), a reduced weight gain (NaCl, 52 (SEM 3); inhibitor, −1.33 (SEM 8.9) g/21 d; P<0.01), as well as changes in the activity of some intestinal enzymes such as maltase (NaCl, 87 (SEM 7); inhibitor, 127 (SEM 11) U/g proteins; P<0.05). The present study has shown, for the first time, that the prolonged administration of an α-amylase inhibitor reduces blood glucose levels and body-weight gain in Wistar rats.

Keywords

α-Amylase inhibitorGlycaemiaWeightFood intakeDisaccharidases
Type
Research Article
Information
British Journal of Nutrition , Volume 92 , Issue 5 , November 2004 , pp. 785 - 790
Copyright
Copyright © The Nutrition Society 2004

References

Boivin, M, Zinsmeister, AR, Go, VL & DiMagno, EP (1987) Effect of a purified amylase inhibitor on carbohydrate metabolism after a mixed meal in healthy humans. Mayo Clin Proc 62, 249–255.CrossRefGoogle ScholarPubMed
Bo-Linn, GW, Santa, Ana Ca, Morawski, SG & Fordtran, JS (1982) Starch blockers - their effect on calorie absorption from a high-starch meal. N Engl J Med 307, 1413–1416.CrossRefGoogle ScholarPubMed
Bowman, DE (1945) Amylase inhibitor of navy bean. Science 102, 358–359.CrossRefGoogle Scholar
Dahlqvist, A (1964) Method for assay of intestinal disaccharidases. Anal Biochem 7, 18–25.CrossRefGoogle ScholarPubMed
Jaffe, WG & Lette, CL (1968) Heat-labile growth-inhibiting factors in beans (Phaseolus vulgaris). J Nutr 94, 203–210.CrossRefGoogle ScholarPubMed
Jain, NK, Boivin, M, Zinsmeister, AR, Brown, ML, Malagelada, JR & DiMagno, EP (1989) Effect of ileal perfusion of carbohydrates and amylase inhibitor on gastrointestinal hormones and emptying. Gastroenterology 96, 377–387.CrossRefGoogle ScholarPubMed
Jain, NK, Boivin, M, Zinsmeister, AR & DiMagno, EP (1991) The ileum and carbohydrate-mediated feedback regulation of postprandial pancreaticobiliary secretion in normal humans. Pancreas 6, 495–505.CrossRefGoogle ScholarPubMed
Kataoka, K & DiMagno, EP (1999) Effect of prolonged intraluminal alpha-amylase inhibition on eating, weight, and the small intestine of rats. Nutrition 15, 123–129.CrossRefGoogle ScholarPubMed
Kotaru, M, Iwami, K, Yeh, HY & Ibuki, F (1989) In vivo action of alpha-amylase inhibitor from cranberry bean (Phaseolus vulgaris) in rat small intestine. J Nutr Sci Vitaminol (Tokyo) 35, 579–588.CrossRefGoogle ScholarPubMed
Layer, P, Carlson, GL & DiMagno, EP (1985) Partially purified white bean amylase inhibitor reduces starch digestion in vitro and inactivates intraduodenal amylase in humans. Gastroenterology 88, 1895–1902.CrossRefGoogle ScholarPubMed
Layer, P, Rizza, RA, Zinsmeister, AR, Carlson, GL & DiMagno, EP (1986 a) Effect of a purified amylase inhibitor on carbohydrate tolerance in normal subjects and patients with diabetes mellitus. Mayo Clin Proc 61, 442–447.CrossRefGoogle ScholarPubMed
Layer, P, Zinsmeister, AR & DiMagno, EP (1986 b) Effects of decreasing intraluminal amylase activity on starch digestion and postprandial gastrointestinal function in humans. Gastroenterology 91, 41–48.CrossRefGoogle ScholarPubMed
Le Berre-Anton, V, Bompard-Gilles, C, Payan, F & Rouge, P (1997) Characterization and functional properties of the alpha-amylase inhibitor (alpha-AI) from kidney bean (Phaseolus vulgaris) seeds. Biochim Biophys Acta 1343, 31–40.CrossRefGoogle ScholarPubMed
Liener, IE, Donatucci, DA & Tarcza, JC (1984) Starch blockers: a potential source of trypsin inhibitors and lectins. Am J Clin Nutr 39, 196–200.Google ScholarPubMed
Maranesi, M, Carenini, G & Gentili, P (1984) Nutritional studies on anti alpha-amylase: I) Influence on the growth rate, blood picture and biochemistry and histological parameters in rats. Acta Vitaminol Enzymol 6, 259–269.Google ScholarPubMed
Marshall, JJ & Lauda, CM (1975) Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris. J Biol Chem 250, 8030–8037.CrossRefGoogle ScholarPubMed
Moreno, J, Altabella, T & Chrispeels, MJ (1990) Characterization of alpha-amylase inhibitor, a lectin like protein in the seeds of Phaseolus vulgaris. Plant Physiol 92, 703–709.CrossRefGoogle ScholarPubMed
Mulimani, VH & Rudrappa, G (1994) Effect of heat treatment and germination on alpha amylase inhibitor activity in chick peas (Cicer arietinum L.). Plant Foods Hum Nutr 46, 133–137.CrossRefGoogle ScholarPubMed
Puls, W & Kneup, U (1973) Influence of an amylase inhibitor (BAY d 7791) on blood glucose, serum insulin and NEFA in starch loading tests in rats, dog and man. Diabetologia 9, 97–101.CrossRefGoogle Scholar
Pusztai, A (1966) The isolation of two proteins, glycoprotein I and a trypsin inhibitor, from the seeds of kidney bean (Phaseolus vulgaris). Biochem J 101, 379–384.CrossRefGoogle Scholar
Pusztai, A, Grant, G, Duguid, T, Brown, DS, Peumans, WJ, Van Damme, EJ & Bardocz, S (1995) Inhibition of starch digestion by alpha-amylase inhibitor reduces the efficiency of utilization of dietary proteins and lipids and retards the growth of rats. J Nutr 125, 1554–1562.Google ScholarPubMed
Pusztai, A, Grant, G, Stewart, JC & Watt, WB (1988) Isolation of soybean trypsin inhibitors by affinity chromatography on anhydrotrypsin-Sepharose 4B. Anal Biochem 172, 108–112.CrossRefGoogle ScholarPubMed
Royal, Decree (1988) Real Decreto 223/1988 de 14 de marzo, sobre protección de los animales utilizados para experimentación y otros fines científicos (Royal Decree 223/1988, 14 March, Principles for care and use of experimental animals). BOE 67, 8509–8512.Google Scholar
Rosenberg, IH (1982) Starch blockers - still no calorie-free lunch. N Engl J Med 307, 1444–1445.CrossRefGoogle ScholarPubMed
Wallenfels, K, Foldi, P, Nierman, H, Bender, H & Linder, D (1978) The enzymic synthesis, by transglucosylation of a homologous series of glycosidically substituted malto-oligo-saccharides, and their use as amylase substrates. Carbohydr Res 61, 359–368.CrossRefGoogle Scholar
Watford, M, Lund, P & Krebs, HA (1979) Isolation and metabolic characteristics of rat and chicken enterocytes. Biochem J 178, 589–596.CrossRefGoogle ScholarPubMed
Whitaker, JR, Filho, FF & Lajolo, FM (1988) Parameters involved in binding of porcine pancreatic alpha-amylase with black bean inhibitor: role of sulfhydryl groups, chloride, calcium, solvent composition and temperature. Biochimie 70, 1153–1161.CrossRefGoogle ScholarPubMed