Hostname: page-component-78c5997874-lj6df Total loading time: 0 Render date: 2024-11-14T06:35:18.219Z Has data issue: false hasContentIssue false
  • English
  • Français

Nutritional evaluation of the trypsin (EC 3.4.21.4) inhibitor from cowpea (Vigna unguiculata Walp.)

Published online by Cambridge University Press:  09 March 2007

A. Pusztal ,
G. Grant ,
D. J. Brown ,
J. C. Stewart ,
S. Bardocz ,
S. W. B. Ewen ,
A. M. R. Gatehouse  and
V. Hilder
A. Pusztal
Affiliation:
The Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
G. Grant
Affiliation:
The Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
D. J. Brown
Affiliation:
The Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
J. C. Stewart
Affiliation:
The Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
S. Bardocz
Affiliation:
The Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
S. W. B. Ewen
Affiliation:
Department of Pathology, University of Aberdeen Medical School, Aberdeen
A. M. R. Gatehouse
Affiliation:
Department of Biological Sciences, University of Durham, South Rd, Durham DH1 3LE
V. Hilder
Affiliation:
Department of Biological Sciences, University of Durham, South Rd, Durham DH1 3LE
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.

The effect of feeding rats purified cowpea (Vigna unguiculata Walp.) trypsin (EC 3.4.21.4) inhibitor in a semi-synthetic high-quality diet based on lactalbumin (10 g inhibitor/kg) for 10 d was a moderate reduction in the weight gain of rats in comparison with controls, despite an identical food intake in the two groups. The reduction in the growth rate was about 20% on a live weight basis. However, the corresponding value calculated from the weight of dry carcasses was less, only about 7%, probably because the water content of the body of the two groups of rats was different. Although most of the cowpea trypsin inhibitor (CpTI) was rapidly broken down in the digestive tract, its inclusion in the diet led to a slight, though significant, increase in the nitrogen content of faeces but not of urine. Accordingly, the net protein utilization of rats fed on inhibitor-containing diets was also slightly depressed while their energy expenditure was elevated. In agreement with results obtained for the protease inhibitors of soya bean, the slight anti-nutritional effects of CpTI were probably due mainly to the stimulation of the growth and metabolism of the pancreas. Thus, the nutritional penalty for increased insect-resistance after the transfer of the cowpea trypsin inhibitor gene into food plants is slight in the short-term.

Keywords

Trypsin inhibitorCowpeaAnti-nutritional effectsRat
Type
Nutritional Effects of Natural Toxicants
Information
British Journal of Nutrition , Volume 68 , Issue 3 , November 1992 , pp. 783 - 791
Copyright
Copyright © The Nutrition Society 1992

References

Abbey, B. W., Neale, R. J. & Norton, G. (1979 a). Nutritional effects of field bean (Vicia faba L.) proteinase inhibitors fed to rats. British Journal of Nutrition 41, 31–38.CrossRefGoogle ScholarPubMed
Abbey, B. W., Norton, G. & Neale, R. J. (1979 b). Effects of dietary trypsin inhibitors from field bean (Vicia faba L.) and field bean meal on pancreatic function in the rat. British Journal of Nutrition 41, 39–45.CrossRefGoogle ScholarPubMed
Bardocz, S., Grant, G., Brown, D. S., Ewen, S. W. B. & Pusztai, A. (1989). Involvement of polyamines in Phaseolus vulgaris lectin-induced growth of rat pancreas in vivo. Medical Science Research 17, 309–311.Google Scholar
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle ScholarPubMed
Coates, M. E., O'Donoghue, P. N., Payne, P. R. & Ward, R. J. (1969). Laboratory Animal Handbooks. 2. Laboratory Standards for Laboratory Rats and Mice, p. 15. London: Laboratory Animals Ltd.Google Scholar
Davidson, J., Mathieson, J. & Boyne, A. W. (1970). The use of automation in determining nitrogen by the Kjeldahl method, with final calculations by computer. Analyst 95, 181–193.CrossRefGoogle ScholarPubMed
Friedman, M. (1986). Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, [Friedman, M., editor]. New York and London: Plenum Press.CrossRefGoogle Scholar
Gallaher, D. & Schneeman, B. O. (1984). Nutritional and metabolic response to plant inhibitors of digestive enzymes. In Nutritional and Metabolic Aspects of Food Safety. Advances in Experimental Medicine and Biology, pp. 299–320 [Friedman, M., editor]. New York and London: Plenum Press.Google Scholar
Gatehouse, A. M. R. & Boulter, D. (1983). Assessment of the antimetabolic effects of trypsin inhibitors of cowpea (Vigna unguiculata) and other legumes on the development of the bruchid beetle Callosobruchus maculatus. Journal of Science of Food and Agriculture 34, 345–350.CrossRefGoogle Scholar
Gatehouse, A. M. R., Gatehouse, J. A. & Boulter, D. (1980). Isolation and characterisation of trypsin inhibitors from cowpea (Vigna unguiculata). Phytochemistry 19, 751–756.CrossRefGoogle Scholar
Gatehouse, A. M. R., Gatehouse, J. A., Dobie, P., Kilminster, A. & Boulter, D. (1979). Biochemical basis of insect resistance in Vigna unguiculata. Journal of Science of Food and Agriculture 30, 948–958.CrossRefGoogle Scholar
Grant, G., More, L. J., McKenzie, N. H., Stewart, J. C. & Pusztai, A. (1983). A survey of the nutritional and haemagglutination properties of legume seeds generally available in the UK. British Journal of Nutrition 50, 207–214.CrossRefGoogle ScholarPubMed
Hilder, V. A., Barker, R. F., Samour, R. A., Gatehouse, A. M. R., Gatehouse, J. A. & Boulter, D. (1989). Protein and cDNA sequences of Bowman-Birk protease inhibitors from cowpea (Vigna unguiculata Walp.). Plant Molecular Biology 13, 701–710.CrossRefGoogle ScholarPubMed
Hilder, V. A., Gatehouse, A. M. R., Sheerman, S. E., Barker, R. F. & Boulter, D. (1987). A novel mechanism of insect resistance engineered into tobacco. Nature 330, 156–159.CrossRefGoogle Scholar
Jahn, R., Schliebler, W. & Greengard, P. A. (1984). A quantitative dot immunobinding assay for proteins using nitrocellulose membrane filters. Proceedings of the National Academy of Sciences U.S.A. 81, 1684–1687.CrossRefGoogle ScholarPubMed
Johnson, L. R. & Chandler, A. M. (1973). RNA and DNA of gastric and duodenal mucosa in antrectomized and gastrin-treated rats. American Journalof Physiology 224, 937–940.CrossRefGoogle ScholarPubMed
Kochar, N., Walker, A. F. & Pike, D. J. (1988). Effect of variety on protein content, amino acid composition and trypsin inhibitor activity of cowpeas. Food Chemistry 29, 65–78.CrossRefGoogle Scholar
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227, 680–685.CrossRefGoogle ScholarPubMed
Liener, I. E. & Kakade, M. L. (1980). Protease inhibitors. In Toxic Constituents of Plant Foodstuffs, 2nd ed., pp. 7–71 [Liener, I. E., editor]. New York: Academic Press.Google Scholar
Lovtrup, S. (1962). Chemical determination of DNA in animal tissues. Acta Biochimica Polonica 9, 411–424.Google Scholar
Madar, Z., Gertler, A. & Birk, Y. (1979). The fate of the Bowman-Birk trypsin inhibitor from soybeans in the digestive track of chicks. Comparative Biochemistry and Physiology 62A, 1057–1061.CrossRefGoogle Scholar
Palmer, D. W. & Peters, T. Jr. (1969). Automated determination of free amino groups in serum and plasma using 2,4,6-trinitrobenzene sulfonate. Clinical Chemistry 15, 891–901.CrossRefGoogle Scholar
Pusztai, A. (1967). Trypsin inhibitors of plant origin, their chemistry and potential role in animal nutrition. Nutrition Abstracts and Reviews 37, 1–9.Google ScholarPubMed
Richardson, M. (1981). Plant protein inhibitors of enzymes; their role in animal nutrition and plant defence. Journal of Biological Education 15, 178–182.CrossRefGoogle Scholar
Rubio, L. A., Grant, G.Bardocz, S., Dewey, P. & Pusztai, A. (1991). Nutritional response of growing rats to faba beans (Vicia faba L., minor) and faba bean fractions. British Journal of Nutrition 66, 533–542.CrossRefGoogle ScholarPubMed
Schachterle, G. R. & Pollack, R. L. (1973). A simplified method for the quantitative assay of small amounts of protein in biological material. Analytical Biochemistry 51, 654–655.CrossRefGoogle Scholar
Seiler, N. & Knödgen, B. (1980). HPLC procedure for the simultaneous determination of the natural polyamines and their monoacetyl derivatives.Journal of Chromatography 221, 227–235.CrossRefGoogle ScholarPubMed
Sneider, W. C. (1957). Determination of nucleic acids in tissue by pentose analysis. Methods in Enzymology 3, 680–684.CrossRefGoogle Scholar
Technicon Instruments Corporation (1963 a). Creatinine; Technicon AutoAnalyzer Method File, N-11a.Google Scholar
Technicon Instruments Corporation (1963 b). Urea nitrogen; Technicon AutoAnalyzer Method File, N-11c.Google Scholar
Unicam Instruments Ltd. (1960). Ammonia; Methodology Sheet No. 51.Google Scholar
Zivin, J. A. & Snarr, J. F. (1973). An automated colorimetric method for the measurement of 3-hydroxybutyrate. Analytical Biochemistry 52, 456–461.CrossRefGoogle ScholarPubMed