Abstract
To simulate the effects of nutritionally adequate and inadequate vegetariandiets, rats were fed, for 28 days, an isonitrogenous, isocaloric, amino acidunbalanced cereal diet (CD) deficient in lysine and tryptophan or abalanced cereal-legume diet (CLD). The impact of these diets on enzymesresponsible for digestion of proteins and carbohydrates were measured.Neither experimental diet significantly affected the animal's final weight orfeed consumption in comparison with controls fed a standard mixed dietfrom plant and animal sources. However, during the first three weeks, theweight gain of rats fed the CD was significantly lower (p<0.01;p<0.05) than that of the controls. CD fed rats also had a higher feedefficiency ratio (p<0.05), demonstrating increased feed consumptionper unit of body weight. They also had decreased pancreaticα-amylase activity (p<0.05), serum phytolytic and zoolyticα-amylase activity (p<0.05) and serum protein level(p<0.05) than the controls. Activity of pancreatic trypsin and intestinalenzymes (sucrase, maltase, aminopeptidase N) were the same as in thecontrols. In rats fed CLD, growth, food consumption, and enzyme activitiesdid not change, however serum protein and glucose levels were higher(p<0.025; p<0.005) than in the controls. It is hypothesized thatdecrease in α-amylase activity was mostly related to the tryptophandeficiency in the CD because this enzyme contains the highest amount oftryptophan units among all tested enzymes.
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References
Pavlov IP (1897) Lectures on the Functioning of the Main Digestive Glands. The complete works. vol. 2, book 2, Moscow-Leningrad: Publishers USSR Acad. Sci., 1951. (in Russian).
Snook JT (1973) Protein digestion. Nutritional and metabolic considerations.World Rew Nutr Diet 18: 121–176.
Corring T (1980) The adaptation of digestive enzymes to the diet: its physiological significance. Repr Nutr Devel 20: 1217–1235.
Puigserver A, Wicker C, Gaucher C (1986) Adaptation of pancreatic and intestinal hydrolases to dietary changes. In Desnuelle P, Sjöström H, Noren O (eds), Molecular and Cellular Basis of Digestion, Amsterdam, New York, London: Elsevier Science Publishers B.V., pp 113–124.
Brannon PM (1990) Adaptation of exocrine pancreas to diet. An Rev Nutr 10: 85–105.
Dagorn JC, Lahaie RG (1981) Dietary regulation of pancreatic protein synthesis. I. Rapid and specific modulation of enzyme synthesis by changes in dietary composition. Biochim Biophys Acta 654: 111–118.
Sanderson IRS (1997) Diet and gene expression in the intestine. Balliere's Clin Gastroenterol 11: 441–463.
Ugolev AM (1961) Digestion and its Adaptational Evolution. Moscow: Publishers Vischaja Schkola, (in Russian).
Magee DF, Anderson EG (1955) Changes in pancreatic enzymes brought about by alteration in the nature of the dietary protein. Amer J Physiol 181: 79–82.
Pond WW, Snyder W, Snook JT, Walker EF, McNeil DA, Stillings BR (1971) Relative utilization of casein, fish protein concentrate and isolated soybean protein for growth and pancreatic enzyme regeneration of the protein-calorie malnourished baby pig. J Nutr 101: 1193–1200.
Committee on Nutrition American Academy of Pediatrics (1998). Nutritional aspects of vegetarian diets. In RE Kleinman (ed), Pediatric Nutrition Handbook. 4th ed. Elk Grove Village, IL: American Academy of Pediatrics, pp 573–586.
Gong EJ, Heald FP (1988) Diet, nutrition and adolescence. In Shils ME, Young VR (eds), Modern Nutrition in Health and Disease, Philadelphia: Lea & Febiger, pp 969–981.
Young VR, Pellett PL (1994) Plant proteins in relation to human protein and amino acid nutrition. Am J Clin Nutr 59 (suppl): 1203S–1212S.
Havala S, Dwyer J (1993) Position of the American Dietetic Association: vegetarian diets. J Amer Diet Assoc 93: 1317–1319.
Slavin J (1993) Nutritional benefits of soy protein and soy fibers. J Amer Diet Assoc 91: 816–819.
Pierre KJJ, Tung KK, Nadj H (1976) A new enzymatic kinetic method for determination of amylase. Clin Chem 22: 1219.
Rick W (1974) Trypsin. Measurment with N?-p-toluensulfonyl-L-arginine methyl ester as substrate. In Bergmayer HU (ed), Methods of Enzymatic Hydrolysis, New York, London: Academic Press 2: 1021–024.
Dahlqvist A (1968) Assay of intestinal disaccharidases. Anal Biochem 22: 99–107.
Fujita M, Parsons DS, Wojnarowska F (1972) Oligopeptidases of brush-border membranes of rat small intestinal mucosal cells. J Physiol 227: 377–394.
Bradford MM (1976) A refined and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254.
Rick W, Stegbauer HP (1974) ?-Amylase. Measurement of reducing groups. In Bergmeyer NH (ed), Methods of enzymatic analysis. New York, London: Academic Press 2: 885–890.
Van Dyke RW (1989) Mechanism of digestion and absorption of food. In Slesenger MH, Fordtran JS (eds) Gastrointestinal Disease, Pathophysiology, diagnosis, management. Saunders Company, pp 1062-1088.
Levitt MD, Ellis C, Engel RR (1977) Isoelectric focusing studies of human serum and tissue isoamylases. J Lab Clin Med 90: 141–152.
Lebenthal E, Lerner A (1995) Salivary secretion. In Yamada T (ed), Textbook of Gastroenterology v.1. Philadelphia: Pippincott Company, pp 279–295.
Kazmarek MJ, Rosenmund H (1977) The action of human pancreatic and salivary isoamylases on starch and glycogen. Clin Chim Acta 79: 69–73.
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Kushak, R.I., Drapeau, C. & Winter, H.S. Pancreatic and intestinal enzyme activities in rats in response to balanced and unbalanced plant diets. Plant Foods Hum Nutr 57, 245–255 (2002). https://doi.org/10.1023/A:1021877305750
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DOI: https://doi.org/10.1023/A:1021877305750