Inhibition of Trypsin and Chymotrypsin from Diffent Animal Species: A comparative Study

Otras publicaciones, Werner Jaffe

Inhibition of Trypsin and Chymotrypsin from Diffent Animal Species: A comparative Study

Rascón, Ana;.Seid, Dinah S. y.Aizman. Aída

Comp. Biochem. Physiol. Vol. 82B No.2:375-378. Pergamon Press Ltd., Gran Bretaña, 1984

  1. The effect of 3 purified trypsin inhibitors and 4 legume seed extracts on the trypsins and chymotrypsins of the activated pancreata of 11 animal species, including man, was measured.
  2. The activation was performed by either homologous enterokinase or by bovine trypsin. Several trypsinogens were not activated by the latter.
  3. Rabbit trypsin was the most sensitive to all inhibitor preparations, while the human trypsin was the most resistant, except to the black bean extract.
  4. The response of the chymotrypsins was more variable .and those of capybara and rabbit showed extreme sensitivity.
  5. Considerable differences between the extracts of black and white garden beans, both Phaseolusvulgaris, with respect to their reactivity toward different animal enzymes were detected.
  6. No relation between relative pancreas weight and susceptibility toward soybean trypsin inhibitor could be observed.

INTRODUCTION

The inhibition of pancreatic proteolytic enzymes by plant extracts, especially those from legume seeds may have nutritional consequences (Liener and Kakade, 1980). Although the inhibitors are thermolabile, some residual activity remains in standard heat-treated plant foods (Churella el al., 1976). Research regarding the effect of trypsin inhibitors in foods has be en performed mostly on soybeans. From the point of view of human nutrition other legume seeds are even more important than soybeans, depending on the population groups involved. In animal feeding the addition of uncooked legumes to feed with their inhibitors intact, may reduce its nutritional value.

Contradictory results have been reported with respect to the relative inhibitory activity of soybean trypsin inhibitors toward trypsins of different origins, and considerable differences in the susceptibility of the pancreatic proteases of different animal species have been observed (Krogdahl and Holm, 1983). The use of the commercially available bovine trypsinas a reference eniyme has been advocated by Belitz el al (1982) and criticized by Krogdahl and Holm (1979) and Holm and Krogdahl (1982).

The relative sensitivity of the pancreatic proteases of animals toward different inhibitors may bear upon the overall physiological process of digestion. In the present work we have compared the activity of seven inhibitor preparations, four seed extracts and three commercial inhibitors on the enzymes of 12 animal species including bovine and human, as a contribution to the study of their possible undesirable nutritional effects.

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