Hostname: page-component-5d59c44645-mrcq8 Total loading time: 0 Render date: 2024-02-23T18:57:15.428Z Has data issue: false hasContentIssue false

Novel dietary strategy for overcoming the antinutritional effects of soyabean whey of high agglutinin content

Published online by Cambridge University Press:  09 March 2007

A. Pusztai
Affiliation:
Rowett Research Institute, Bucksbum, Aberdeen AB21 9SB
G. Grant
Affiliation:
Rowett Research Institute, Bucksbum, Aberdeen AB21 9SB
S. Bardocz
Affiliation:
Rowett Research Institute, Bucksbum, Aberdeen AB21 9SB
E. Gelencser
Affiliation:
Central Food Research Institute, 1022-Budapest, Hungary
GY. Hajos
Affiliation:
Central Food Research Institute, 1022-Budapest, Hungary
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.

A diet-switching experiment, which aimed to improve the utilization of soyabean whey was carried out for 61 d with young rats. Feeding was arranged in such a way that after a few days on the soyabean diet, the rats were switched to a high-quality lactalbumin diet for a short period, after whicb the cycle was repeated several times. The weights of the rats at the end of the soyabean phases were significantly less than those of animals pair-fed on a high-quality diet throughout. However, the test group regained the weight loss after switching to the lactalbumin diet. After three cycles there were no significant differences between the weights of the test rats fed on a poor soyabean diet for over a third of the experiment and those fed on the lactalbumin diet throughout. Feed conversion was always significantly higher with test rats in the lactalbumin period than with continually pair-fed controls. Similarly, faecal N losses were significantly higher for test rats in the soyabean phase, but these differences disappeared after switching to the lactalbumin diet. At the end of the experiment there were no significant differences in body protein or lipids between the groups although the pancreas was significantly heavier while the liver was lighter in soyabean-fed rats. The high destruction of trypsin inhibitors in the gut suggests that they probably had little effect on protein digestion in the gut. In contrast, as selective depletion of the agglutinin from soyabean whey removed the nutritional benefit in the lactalbumin part of the cycle, the improved feed conversion in this period must have been the result mainly of the survival and functionality of soyabean agglutinin and the benefits due to the hyperplastic growth and faster renewal of the gut surface it induced. As processing is unnecessary, this novel method is cheap and can be easily adapted for the use of soyabean whey, regarded as a waste product.

Type
General Nutrition
Copyright
Copyright © The Nutrition Society 1997

References

REFERENCES

Banwell, J. G., Howard, R., Cooper, D & Costerton, J. W. (1988). Bacterial overgrowth by indigenous microflora in the phytohemagglutinin fed rat. Canadian Journal of Microbiology 34, 10091013.Google Scholar
Bardocz, S., Grant, G., Ewen, S. W. B., Duguid, T. J., Brown, D. S., Englyst, K & Pusztai, A. (1995). Reversible effect of phytohaemagglutinin on the growth and metabolism of rat gastrointestinal tract. Gut 37, 353360.Google Scholar
Bardocz, S., Grant, G., Pusztai, A., Franklin, M. F & Carvalho, A.de, F. F. U. (1996). The effect of phytohaemagglutinin at different dietary concentrations on the growth, body composition and plasma insulin of the rat. British Journal of Nutrition 76, 613626.Google Scholar
Calderon de la Barca, A. M., Vazquez-Moreno, L & Robles-Burgueno, M. R. (1991). Active soybean lectin in foods: isolation and quantitation. Food Chemistry 39, 321327.Google Scholar
Gallaher, D & Schneeman, B. O. (1986). Nutritional and metabolic response to plant inhibitors of digestive enzymes. In Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, pp. 167184 [Friedman, M., editor]. New York: Plenum Press.Google Scholar
Grant, G., Dorward, P. M & Pusztai, A. (1993). Pancreatic enlargement is evident in rats fed diets containing raw soybeans (Glycine max) or cowpeas (Vigna unguiculata) for 800 days but not in those fed diets based on kidney beans (Phaseohs vulgaris) or lupinseed (Lupinus angustifolius). Journal of Nutrition 123, 22072215.Google Scholar
Grant, G., McKenzie, N. H., Watt, W. B., Stewart, I. C., Dorward, P. M & Pusztai, A. (1986). Nutritional evaluation of soya beans (Glycine max): nitrogen balance and fractionation studies. Journal of the Science of Food and Agriculture 37, 10011010.Google Scholar
Gupta, Y. P. (1987). Nutritive value of soybean. International Journal of Tropical Agriculture 5, 247279.Google Scholar
Hajos, Gy., Gelencser, E., Pusztai, A., Grant, G., Sakhri, M & Bardocz, S. (1995). Biological effects and survival of trypsin inhibitors and the agglutinin from soybean in the small intestine of the rat. Jounral of Agricultural and Food Chemistry 43, 165170.Google Scholar
Harboe, N & Inglid, A. (1973). Immunization, isolation of immunoglobulins, estimation of antibody titre. Scandinavian Journal of Immunology 2 (Suppl. 1), 161164.Google Scholar
Liener, I. E. (1994). Implications of antinutritional components in soybean foods. Critical Reviews in Food Science and Nutrition 34, 3167.Google Scholar
Pusztai, A & Bardocz, S. (1995). Physiological roles of lectins in plants and the effects of their inclusion in the diet on the gut and metabolism of mammals. In Phytochemicals and Health. Proceedings of the 10th Annual Penn State Symposium in Plant Physiology, pp. 179191 [Gustine, D.L. and Flores, H. E., editors]. Rockville, MD: American Society of Plant Physiologists.Google Scholar
Pusztai, A., Clarke, E. M. W & King, T. P. (1979). The nutritional toxicity of Phuseolus vulgaris lectins. Proceedings of the Nutrition Society 38, 115120.Google Scholar
Pusztai, A., Ewen, S. W. B., Grant, G., Peumans, W. J., van Damme, E. J. M., Rubio, L & Bardocz, S. (1990). The relationship between survival and binding of plant lectins during small intestinal passage and their effectiveness as growth factors. Digestion 46 (Suppl. 2), 308316.Google Scholar
Pusztai, A., Grant, G., Brown, D. J., Stewart, J. C & Bardocz, S. (1992). Nutritional evaluation of the trypsin (EC 3.4.21.4) inhibitor from cowpea (Vigna unguiculata Walp.). British Journal of Nutrition 68, 783791.Google Scholar
Pusztai, A., Grant, G., Duguid, T., Brown, D.S., Peumans, W. J., Van Damme, E. J. M & Bardocz, S. (1993). Kidney bean lectin-induced Escherichia coli overgrowth in the small intestine is blocked by GNA, a mannose-specific lectin. Journal of Applied Bacteriology 75, 360368.Google Scholar
Pusztai, A., Watt, W. B & Stewart, J. C. (1991). A comprehensive scheme for the isolation of trypsin inhibitors and the agglutinin from soybean seeds. Journal of Agricultural and Food Chemistry 39, 862866.Google Scholar
Rackis, J. J., Wolf, W. J & Baker, E. C. (1986). Protease inhibitors in plant foods; content and inactivation. In Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, pp. 299331 [Friedman, M., editor]. New York: Plenum Press.Google Scholar