Qualitas Plantarum

, Volume 23, Issue 1–3, pp 157–169 | Cite as

Trypsin inhibitors of broad bean (Vicia faba L.)

  • Arjumand Sultan Warsy
  • M. Stein
Article

Abstract

We have isolated and purified two trypsin inhibitors from broad bean(Vicia faba L.). On the evidence of acrylamide gel electrophoresis these two inhibitors, labelled BBTI-1 and BBTI-2, are pure and distinct. Trypsin inactivation and stability studies indicate that BBTI-2 has the greater specific activity and is the more heat stable than BBTI-1. The amino acid pattern confirms the distinctness of the two inhibitors. From qualitative evidence it is inferred that two inhibitors are not simple proteins, but possibly glycoproteins which could explain the stability characteristics observed.

Keywords

Acrylamide Trypsin Inhibitor Stability Characteristic Broad Bean Qualitative Evidence 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Zusammenfassung

Wir haben aus Dicken Bohnen(Vicia faba) zwei Trypsin-Inhibitoren isoliert und gereinigt. Nach den Befunden der Acrylamidgel-Elektrophorese sind diese beiden Inhibitoren, mit den Bezeichnungen BBTI-1 und BBTI-2, rein und von einander verschieden. Trypsin-Inaktivierungs- und Stabilisierungs-Versuche ergaben, daß BBTI-2 eine größere spezifische Aktivität besitzt und hitzestabiler ist als BBTI-1. Die Aminosäurenzusammensetzung bestätigt die Verschiedenheit der beiden Inhibitoren. Aus den qualitativen Befunden kann gefolgert werden, daß zwei Inhibitoren nicht einfache Proteine sind, aber möglicherweise Glycoproteine, die den beobachteten stabilen Charakter erklären würden.

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References

  1. Birk, Y. (1961). Purification and some properties of highly active inhibitor of trypsin and α-chymotrypsin from soybeans.Biochim. Biophys. Acta 54:378–381.PubMedGoogle Scholar
  2. Birk, Y. (1968). Chemistry and nutrition significance of proteinase inhibitors from plant sources. In: ‘Chemistry, Pharmacology and Clinical Applications of Proteinase Inhibitors’. (A. N. Black & E. F. Mammen, eds).Ann. N.Y. Acad. Sci. 146:388–399.PubMedGoogle Scholar
  3. Borchers, R. & Ackerson, C. W. (1950). The nutritive value of legume seeds. X. Effect of autoclaving and trypsin inhibitor test for 17 species.J. Nutr. 41:339–345.PubMedGoogle Scholar
  4. Chu, H. M. & Chi, C. W. (1965). The isolation and crystallization of two trypsin inhibitors of low molecular weight from mung bean (Phaseolus aureus Roxb.).Scientia sin. 14:1441–1453.Google Scholar
  5. Garlich, J. D. & Nesheim, M. C. (1966). Relationship of fractions of soybeans and a crystalline trypsin inhibitor to the effects of feeding unheated soybean meal to chicks.J. Nutr. 88:100–110.PubMedGoogle Scholar
  6. Hummel, B. C. W. (1959). A modified spectrophotometric determination of chymotrypsin, trypsin and thrombin.Can. J. Biochem. Physiol. 37:1393–1399.PubMedGoogle Scholar
  7. Jones, G., Moore, S. & Stein, W. H. (1963). Properties of chromatographically purified trypsin inhibitors from lima beans.Biochemistry 2:66–71.Google Scholar
  8. Krahn, J. & Stevens, F. C. (1970). Lima bean trypsin inhibitor. Limited proteolysis by tripsin and chymotrypsin.Biochemistry 9:2646–2652.PubMedGoogle Scholar
  9. Kress, L. F., Martin, S. R. & Laskowski, Sr., M. (1971). Isolation of isoinhibitors from porcine.Biochim Biophys. Acta 24:836–844.Google Scholar
  10. Kunitz, M. (1947). Crystalline soybean trypsin inhibitor. II. General properties.J. Gen. Physiol. 30:291–310.Google Scholar
  11. Learmonth, E. C. & Wood, J. C. (1960). A Trypsin inhibitor in wheat flour.Chem. Ind. (London): 1569–1570.Google Scholar
  12. Liener, I. E., Deuel, H. J. Jr. & Fevold, H. L. (1949). The effect of supplemental methionine on the nutritive value of diets containing concentrates of soybean trypsin inhibitor.J. Nutr. 39:325–339.PubMedGoogle Scholar
  13. Liener, I. E. (ed). (1969) Toxic Constituents of Plant Foodstuffs. Academic Press, New York and London.Google Scholar
  14. Lillevick, H. A. (1970). The Determination of total organic nitrogen. In: ‘Methods of food analysis’. pp. 601–615.Google Scholar
  15. Lowry, O. H., Rosenbrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent.J. Biol. Chem. 193:265–275.PubMedGoogle Scholar
  16. Nesheim, M. C. & Garlich, J. D. (1966). Digestibility of unheated soybean meal for laying hens.J. Nutr. 88:187–192.PubMedGoogle Scholar
  17. Population Bulletin, (1971). 27 : No. 2.Google Scholar
  18. Pusztai, A. (1966). The isolation of two proteins, glycoprotein I and trypsin inhibitor from the seeds of kidney bean(Phaseolus vulgaris).Biochem. J. 101:379–384.PubMedGoogle Scholar
  19. Rackis, J. J. (1965). Physiological properties of soybean trypsin inhibitors and their relationship to pancreatic hypertrophy and growth inhibition of rats.Federation Proc. 24:1488–1493.Google Scholar
  20. Rackis, J. J. (1972). Biologically active components. In: ‘Soybeans: Chemistry and Technology’. pp. 158–202. (A. K. Smith & S. J. Circle eds). Avi Publishing Company Inc., Westpoint, Connecticut.Google Scholar
  21. Rhodes, M. B., Bennet, N. & Feeney, R. E. (1960). The trypsin and chymotrypsin inhibitors from avian egg whites.J. Biol. Chem. 235:1686–1693.Google Scholar
  22. Ryan, C. A. & Balls, A. K. (1962). An inhibitor of chymotrypsin fromSolanum tuberosum and its behaviour towards trypsin.Proc. Natl. Acad. Sci. U.S. 48:1839–1844.Google Scholar
  23. Ryan, C. A. & Shumway, L. K. (1970). Studies on the structure and function of chymotrypsin inhibitor I in the Solanaceae family. In: ‘Proceedings of the International Research Conference on Proteinase Inhibitors’. pp. 175–188. (H. Fritz & H. Tschesche eds). Walter de Gruyter, Berlin.Google Scholar
  24. Smith, A. K. & Circle, S. J. (1972). Protein products as food ingredients. In: ‘Soybeans: Chemistry and Technology’. pp. 339–388. (A. K. Smith & S. J. Circle eds). Avi Publishing Company Inc., Westpoint, Connecticut.Google Scholar
  25. Sohonie, K. & Ambe, K. S. (1955). Crystalline inhibitors from the Indian field bean and the double bean.Nature, London: 175:508–509.PubMedGoogle Scholar
  26. Sohonie, K., Apte, U. & Ambe, K. S. (1958). Trypsin inhibitors in Indian foodstuffs. V. Effect of raw double beans(Faba vulgaris) and double bean trypsin inhibitor on the growth of rats.J. Sci. Indust. Res. 17C:42–46.Google Scholar
  27. Weder, J. & Hory, H. D. (1972). Trypsin-und Chymotrypsin-Inhibiteron in Leguminosen. I. Nachweis und Isoliering verschiedener Inhibitoren vonPisum sativum.Lebensm.-Wiss. u. Technol. 5:54–63.Google Scholar
  28. Wilson, B. J., McNab, J. M. & Bentley, H. (1972). Trypsin inhibitor activity in the field bean (Vicia faba L.)J. Sci. Fd Agric. 23:679–684.Google Scholar

Copyright information

© Dr. W. Junk b.v. Publishers 1973

Authors and Affiliations

  • Arjumand Sultan Warsy
    • 1
  • M. Stein
    • 1
  1. 1.Food Science Laboratories Dept. of Applied Biochemistry and NutritionUniversity of Nottingham Sutton BoningtonLoughboroughEngland

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