Hostname: page-component-586b7cd67f-t8hqh Total loading time: 0 Render date: 2024-11-23T08:43:36.409Z Has data issue: false hasContentIssue false

Activities of enzymes of the pancreas, and the lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-containing diets

Published online by Cambridge University Press:  09 March 2007

A. E. Ahmed
Affiliation:
Department of Agricultural Biochemistry and Nutrition, University of Newcastle upon Tyne, Newcastle upon Tyne NEI 7RU
R. Smithard
Affiliation:
Department of Agricultural Biochemistry and Nutrition, University of Newcastle upon Tyne, Newcastle upon Tyne NEI 7RU
M. Ellis
Affiliation:
Department of Agricultural Biochemistry and Nutrition, University of Newcastle upon Tyne, Newcastle upon Tyne NEI 7RU
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Diets containing vegetable tannins, predominantly hydrolysable gallotannins, at levels of 13.5, 25 and 50 g/kg were fed to growing broiler cockerels to examine their effect on enzymes in the pancreas, the intestinal lumen and the intestinal mucosa. Pancreas weight per unit live weight showed a significant (P < 0.05) increase with increasing level of dietary tannin while that of the liver remained unaffected. Trypsin (EC 3.4.21.4) and α-amylase (EC 3.2.1.1) activities in the pancreas of birds fed at the highest level of tannins were more than double those from birds fed on a tannin-free control diet. In the intestinal lumen inhibition of trypsin activity increased with increasing level of dietary tannin; α-amylase activity was inhibited at intermediate tannin levels but was restored at the highest level. Dipeptidase (EC 3.4.13.11) and sucrose α-glucosidase (disaccharidase) (EC 3.2.1.48) in the intestinal mucosa were both inhibited by tannins. Growth of the birds and digestibility of nitrogen were adversely affected by the tannin-containing diets.

Type
Diet and its Effects on Gastrointestinal Function
Copyright
Copyright © The Nutrition Society 1991

References

REFERENCES

Abbey, B. W., Norton, G. & Neale, R. J. (1979). Effect of dietary proteinase inhibitors from field bean (Vicia faba L.) and field bean meal on pancreatic function in rats. British Journal of Nutrition 41, 3945.CrossRefGoogle Scholar
Asquith, T. N. & Butler, L. G. (1985). Use of dye-labelled protein as spectrophotometric assay for protein precipitants such as tannins. Journal of Chemical Ecology 11, 15351544.CrossRefGoogle Scholar
Barrowman, J. A. & Mayston, P. D. (1974). The trophic influence of cholecystokinin on the rat pancreas. Journal of Physiology 238, 73P.Google ScholarPubMed
Brand, S. J. & Morgan, R. G. H. (1981). The release of rat intestinal cholecystokinin after oral trypsin inhibitor measured by bioassay. Journal of Physiology 319, 325343.CrossRefGoogle ScholarPubMed
Dahlqvist, A. (1968). Assay of intestinal disaccharidase. Analytical Biochemistry 22, 99107.CrossRefGoogle Scholar
Dembinski, A. B. & Johnson, L. R. (1980). Stimulation of pancreatic growth by secretin, caerulein and pentagastrin. Endocrinology 106, 323327.CrossRefGoogle ScholarPubMed
Fenton, T. W. & Fenton, M. (1979). An improved method for chromic oxide determination in feed and faeces. Canadian Journal of Animal Science 59, 631634.CrossRefGoogle Scholar
Gertler, A. & Nitsan, Z. (1970). The effect of trypsin inhibitors on pancreatopeptidase E, trypsin, chymotrypsin and amylase in the pancreas and intestinal tract of chicks receiving raw and heated soya bean diets. British Journal of Nutrition 24, 893904.CrossRefGoogle ScholarPubMed
Grant, G., Wat, W. B., Stewart, J. C. S. & Pusztai, A. (1987). Effect of dietary soya bean (Glycine max) lectin and trypsin inhibitors upon the pancreas of the rat. Medical Science Research 15, 11971198.Google Scholar
Griffiths, D. W. & Moseley, G. (1980). Effect of diet containing field beans of high and low polyphenolic content on the activity of digestive enzymes in the intestine of rats. Journal of the Science of Food and Agriculture 31, 255259.CrossRefGoogle Scholar
Hagerman, A. E. & Butler, L. G. (1980). Determination of protein in tannin–protein precipitate. Journal of Agricultural Chemistry 28, 952957.CrossRefGoogle Scholar
Hagerman, A. E. & Klucher, K. M. (1986). Tannin protein interaction. In Flavanoids in Biology and Medicine. Biochemical, Pharmacological and Structure–Activity Relationships, pp. 6776 [Harbourne, J. and Middeton, E., editors]. New York: Alan R. Liss.Google Scholar
Hamerstrand, G. E., Black, L. T. & Glover, J. D. (1981). Trypsin inhibitor in soy products: modification of the standard analytical procedure. Cereal Chemistry 58, 4245.Google Scholar
Horigome, T., Kumar, R. & Okamoto, K. (1988). Effect of condensed tannins prepared from leaves of fodder plants on digestive enzymes in vitro and in the intestine of rats. British Journal of Nutrition 60, 275285.CrossRefGoogle ScholarPubMed
Johnson, L. R. & Guthrie, O. D. (1974). Effect of CCK and 16,16-dimethyl PGE on RNA and DNA of gastric and duodenal mucosa. Gastroenterology 70, 5965.CrossRefGoogle Scholar
Kotb, A. R. & Luckly, T. D. (1972). Markers in nutrition. Nutrition Abstracts and Reviews 42, 813845.Google ScholarPubMed
Lasheras, B., Cenarruzabeitia, M. N., Fontan, J., Lluch, M. & Larralde, J. (1980). Effect of raw legume diets on disaccharidase activity in the small intestine of chicks. Revistas Española de Fisiología 36, 331336.Google ScholarPubMed
Launiala, K. (1968). Effect of unabsorbed sucrose and mannitol on the intestinal flow and mean transit time. Scandinavian Journal of Gastroenterology 3, 665671.Google ScholarPubMed
Levison, D. A., Morgan, R. G. H., Brimacombe, J. S., Hopwood, D., Coghill, G. & Wormsley, K. G. (1979). Carcinogenic effects of di-(2-hydroxypropyl)-nitrosamine (DHPN) in male Wistar rats: promotion of pancreatic cancer by a raw soya flour diet. Scandinavian Journal of Gastroenterology 14, 217224.CrossRefGoogle ScholarPubMed
Liddle, R. A., Godfine, I. D., Rosen, M. S., Taplitz, R. A. & Williams, J. A. (1985). CCK bioactivity in human plasma. Journal of Clinical Investigation 75, 11441152.CrossRefGoogle ScholarPubMed
Lumen, B. O. & Salamat, L. A. (1980). Trypsin inhibitor activity in winged beans and possible role of tannins. Journal of Agricultural and Food Chemistry 28, 353365.CrossRefGoogle Scholar
Mainz, D. L., Black, O. & Webster, P. D. (1973). Hormonal control of pancreatic growth. Journal of Clinical Investigation 52, 23002304.CrossRefGoogle ScholarPubMed
Makker, H. P. S., Singh, B. & Dawra, R. K. (1987). Tannin–nutrients interaction – a review. International Journal of Animal Science 2, 127140.Google Scholar
Martin, J. S., Martin, M. M. & Bernays, E. A. (1987). Failure of tannic acid to inhibit digestion or reduce digestibility of plant protein in gut fluids of insect herbivores. Journal of Chemical Ecology 13, 605621.CrossRefGoogle ScholarPubMed
Martin, M. M., Rocholum, D. C. & Martin, J. S. (1985). Effect of surfactants, pH and certain cations on the precipitation of protein by tannins. Journal of Chemical Ecology 11, 485494.CrossRefGoogle ScholarPubMed
Miller, D. & Grane, R. K. (1961). The digestive function of the epithelium of small intestine. I – an intracellular locus of disaccharide and sugar phosphate ester hydrolysis. Biochimica et Biophysica Acta 52, 281293.CrossRefGoogle ScholarPubMed
Mitjavilla, S., Lacombe, C., Carrera, G. & Derache, R. (1977). Effect of tannic acid and oxidised tannic acid on the functional state of rat intestinal epithelium. Journal of Nutrition 107, 21132121.CrossRefGoogle Scholar
Mohammed, T. A. & Ahmed, A. E. (1987). Feeding and metabolic studies on the nutritive value of grain sorghums with reference to their tannin content. Sudan Journal of Veterinary Science and Animal Husbandry 26, 91101.Google Scholar
Mole, S. & Waterman, P. G. (1985). Stimulatory effect of tannins–cholic acid on tryptic hydrolysis of protein. Journal of Chemical Ecology 11, 13231332.CrossRefGoogle Scholar
Mole, S. & Waterman, P. G. (1987). Tannic acid and proteolytic enzymes: enzyme inhibition or substrate deprivation. Phytochemistry 26, 99102.CrossRefGoogle Scholar
Nicholson, J. A. & Kim, Y. S. (1975). A one step L-amino acid oxidase assay for intestinal peptide hydrolysis activity. Analytical Biochemistry 63, 100117.CrossRefGoogle Scholar
Price, M. L., Scoyoc, S. V. & Butler, L. G. (1978). Critical evaluation of vanillin reaction as an assay for tannin in sorghum grain. Journal of Agricultural and Food Chemistry 26, 12141218.CrossRefGoogle Scholar
Rothman, S. S. & Wells, H. (1967). Enhancement of pancreatic growth by pancreozymin. American Journal of Physiology 213, 215218.CrossRefGoogle ScholarPubMed
Sarkar, S. K. & Howarth, R. E. (1976). Specificity of vanillin test for flavanols. Journal of Agricultural and Food Chemistry 24, 317320.CrossRefGoogle ScholarPubMed
Terpstra, K. & De Hart, N. (1974). The estimation of urinary nitrogen and faecal nitrogen in poultry excreta. Zeitschrift für Tierphysiologie, Tierernährung and Futtermittelkunde 32, 306320.CrossRefGoogle ScholarPubMed
Watanabe, T. & Yasuda, M. (1977). Electron microscopic study of the pancreas of the domestic fowl. Cell Tissue Research 180, 453465.CrossRefGoogle ScholarPubMed