Hostname: page-component-78c5997874-94fs2 Total loading time: 0 Render date: 2024-11-05T04:07:04.982Z Has data issue: false hasContentIssue false
  • English
  • Français

Effects of dietary proteinase inhibitors from field bean (Vicia faba L.) and field-bean meal on pancreatic function in the rat

Published online by Cambridge University Press:  08 December 2008

Bene W. Abbey ,
G. Norton  and
R. J. Neale
Bene W. Abbey
Affiliation:
Department of Applied Biochemistry and Nutrition, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough LEI2 5RD
G. Norton
Affiliation:
Department of Applied Biochemistry and Nutrition, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough LEI2 5RD
R. J. Neale
Affiliation:
Department of Applied Biochemistry and Nutrition, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough LEI2 5RD
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.

1. Male weanling rats were fed casein diets containing 1.25, 2.5, 5.0 and 10 g/kg active or autoclaved proteinase inhibitors (PI) from field bean (Vicia faba L.), and raw- and autoclaved-field-bean meal (FBM) diets. After 7, 14 and 21 d on the diets pancreas weights were measured and pancreas and intestinal trypsin (EC 3.4.4.4) and chymotrypsin (EC 3.4.4.5) assayed.

2. Pancreas weights increased on the raw FBM and active-PI-supplemented diets. Maximum pancreatic hypertrophy measured as the percentage increase above controls was observed after 14 d in rats fed on raw FBM. The same percentage increase in pancreas size compared with appropriate controls was obtained with rats fed casein diets supplemented with 5 g active PI/kg.

3. Pancreas trypsin and chymotrypsin levels decreased with increasing dietary PI level. Similarly, lower pancreas trypsin and chymotrypsin levels were observed in rats given raw FBM.

4. Intestinal trypsin and chymotrypsin increased with increasing dietary PI inclusion level. Although the magnitude of this response decreased with the period of feeding the differences in enzyme levels were still significant even after 21 d.

5. It was concluded that the PI alone in raw-FBM diets could not entirely be responsible for the enlargement of the pancreas and the excess secretion of pancreatic enzymes since in synthetic diets PI levels of five times those in FBM were required to produce responses of similar magnitude.

Type
Papers of direct relevance to Clinical and Human Nutrition
Information
British Journal of Nutrition , Volume 41 , Issue 1 , January 1979 , pp. 39 - 45
Copyright
Copyright © The Nutrition Society 1979

References

Abbey, B. W., Neale, R. J. & Norton, G. (1979). Br. J. Nutr. 41, 31.CrossRefGoogle Scholar
Chernick, S. S., Lepkovsky, S. & Chaikoff, I. L. (1948). Am. J. Physiol. 155, 33.CrossRefGoogle Scholar
Garlick, J. D. & Nesheim, M. C. (1966). J. Nutr. 88, 100.CrossRefGoogle Scholar
Gertler, A. & Nitsan, Z. (1970). J. Nutr. 24, 893.CrossRefGoogle Scholar
Green, G.M. & Lyman, R. L. (1972). Proc. Soc. exp. Biol. Med. 140, 6.CrossRefGoogle Scholar
Haines, P. C. & Lyman, R. L. (1961). J. Nutr. 74, 445.CrossRefGoogle Scholar
Hawk, P. B., Oser, B. L. & Summerson, W. H. (1954). Practical Physiological Chemistry, 13th ed.London: Churchill.Google Scholar
Hewitt, D., Coates, M. E., Kakade, M. L. & Liener, I. E. (1973). Br. J. Nutr. 29, 423.CrossRefGoogle Scholar
Howard, F. & Yudkin, J. (1963). Br. J. Nutr. 17, 281.CrossRefGoogle Scholar
Kakade, M.L., Hoffa, D. E. & Liener, I. E. (1973). J. Nutr. 103, 1772.CrossRefGoogle Scholar
Kakade, M.L., Swenson, D. H. & Liener, I. E. (1970). Analyt. Biochem. 33, 255.CrossRefGoogle Scholar
Khayambashi, H. & Lyman, R. L. (1966). J. Nutr. 89, 455.CrossRefGoogle Scholar
Kunitz, M. (1947). J. gen. Physiol. 30, 291.CrossRefGoogle Scholar
Lepkovsky, S., Bingham, E. & Pencharz, R. (1959). Poulf. Sci. 38, 1289.CrossRefGoogle Scholar
Lyman, R. L. & Lepkovsky, S. (1957). J. Nutr. 62, 269.CrossRefGoogle Scholar
Neiss, E., Ivy, C. A. & Nesheim, M. (1972). Proc. Soc. exp. Biol. Med. 140, 291.CrossRefGoogle Scholar
Rackis, J. J. (1965). Fedn Proc. Fedn Am. Socs exp. Biol. 24, 1488.Google Scholar
Rothman, S. & Wells, H. (1967). Am. J. Physiol. 213, 215.CrossRefGoogle Scholar
Saxena, H.C., Jensen, L. S. & McGinnis, J. (1963). Proc. Soc. exp. Biol. Med. 112, 101.CrossRefGoogle Scholar
Seidl, D., Jaffe, M. & Jaffe, W. G. (1969). J. agric. Fd Chem. 17, 1318.CrossRefGoogle Scholar