Effect of soya bean antinutritional proteins on rats and sheep

Authors

  • Károly Baintner Dept. of Physiology, Fac. of Animal Science, Pannon Agricultural University, H-7401 Kaposvár, Guba S. u. 40. Hungary , Pannon Agrarwisenschaftliche Universität, Fakultät für Tierproduktion, H-7401 Kaposvár, Guba S. u. 40. Ungarn
  • D. A. H. Farningham The Rowett Research Institute, AB2 9SB Aberdeen/Bucksburn, Scotland, UK , Rowett Forschungsinstitut, AB2 9SB Aberdeen/Bucksburn, Schotland, Gro britannien
  • P. Kiss Dept. of Agricultural Chemistry, Gödöllő Agricultural University, Gödöllő, Hungary , Lehrstuhl für Agrochemie, Gödöllő Agrarwisenschaftliche Universität, Gödöllő, Ungarn
  • L. Bruce The Rowett Research Institute, AB2 9SB Aberdeen/Bucksburn, Scotland, UK , Rowett Forschungsinstitut, AB2 9SB Aberdeen/Bucksburn, Schotland, Gro britannien
  • Arpad Pusztai The Rowett Research Institute, AB2 9SB Aberdeen/Bucksburn, Scotland, UK , Rowett Forschungsinstitut, AB2 9SB Aberdeen/Bucksburn, Schotland, Gro britannien

Keywords:

lectin, inhibitor, soya bean, rat, sheep

Abstract

In the first experiment we showed that isolated soya bean lectin (SBA) and trypsin inhibitor (STI) are unable to suppress food consumption in rats, if administered orally at a level of 100 mg/kg b.w. Other factors connected with raw soya bean may be responsible for suppression. In another experiment defatted raw soya bean flour was administered intraruminally at a level of 10 g/kg b.w. to a sheep fitted with ruminál, duodenal and ileal cannulas. Soya bean lectin (SBA) and trypsin inhibitors appeared in the duodenum within 1 hour; both reached the terminal ileum and had disappeared by the time 24 hours had elapsed. The passage of the lectin along the gut progressively lagged behind that of the inhibitors, which indicates that this lectin binds to the intestinal surface in this species. The inhibitors were neutralised by marked pancreatic hypersecretion resulting in a supraphysiological trypsin level in the intestine. This experiment shows that soya bean antinutritional proteins pass along the digestive tract at different rates, and if administered intraruminally they are not degraded effectively in the forestomachs. It is assumed that this differential passage may also occur in monogastric animals.

Author Biography

  • Károly Baintner, Dept. of Physiology, Fac. of Animal Science, Pannon Agricultural University, H-7401 Kaposvár, Guba S. u. 40. Hungary, Pannon Agrarwisenschaftliche Universität, Fakultät für Tierproduktion, H-7401 Kaposvár, Guba S. u. 40. Ungarn

    corresponding author
    baintner@atk.kaposvar.pate.hu

References

Brand, S. J., Morgan, R. G. H. (1981). The release of rat intestinal cholecystokinin after oral trypsin inhibitor measured by bioassay. J. Physiol. Lond., 319. 325–343. https://doi.org/10.1113/jphysiol.1981.sp013911

Calam, J., Bojarski, J. C., Springer, C. J. (1987). Raw soya-bean flour increases cholecystokinin release in man. Br. J. Nutr., 58. 175–179. https://doi.org/10.1079/BJN19870084

Green, G. M., Lyman, L. (1972). Feedback regulation of pancreatic enzyme secretion as a mechanism for trypsin inhibitor-induced hypersecretion in rats. Proc. Soc. Exp. Biol. Med., 140. 6–12. https://doi.org/10.3181/00379727-140-36384

Jordinson, M., Playford, R. J., Calam, J. (1997). Effects of a panel of dietary lectins on cholecystokinin release in rats. Am. J. Physiol., 273. G946–G950. https://doi.org/10.1152/ajpgi.1997.273.4.G946

Pusztai, A. (1991). Plant Lectins. Cambridge University Press. https://doi.org/10.1017/CBO9780511895371

Pusztai, A., Ewen, S. W., Grant, G., Peumans, W. J., van Damme, E. J., Rubio, L., Bardocz, S. (1990). Relationship between survival and binding of plant lectins during small intestinal passage and their effectiveness as growth factors. Digestion, 46. Suppl. 2. 308–316. https://doi.org/10.1159/000200402

Pusztai, A., Grant, G., Bardocz, S., Baintner, K., Gelencsér, E., Ewen, S. W. B. (1997). Both free and complexed trypsin inhibitors stimulate pancreatic secretion and change duodenal enzyme levels. Am. J. Physiol., 272. G340–G350. https://doi.org/10.1152/ajpgi.1997.272.2.G340

Pusztai, A., Watt, W. B., Stewart, J. C. (1991). A comprehensive scheme for the isolation of trypsin inhibitors and the agglutinin from soybean seeds. J. Agric. Food Chem., 39. 862–866. https://doi.org/10.1021/jf00005a009

Schwert, G. W., Takenaka, Y. (1955). A spectrophotometric determination of trypsin and chymotrypsin. Biochim. Biophys. Acta, 16. 570–575. https://doi.org/10.1016/0006-3002(55)90280-8

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Published

1999-07-15

Issue

Section

Section 6 – Animal Nutrition and Other Topics

How to Cite

Baintner, K., Farningham, D. A. H., Kiss, P., Bruce, L., & Pusztai, A. (1999). Effect of soya bean antinutritional proteins on rats and sheep. Acta Agraria Kaposváriensis, 3(2), 379-385. https://journal.uni-mate.hu/index.php/aak/article/view/1584

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