Journal of the American Oil Chemists' Society

, Volume 74, Issue 9, pp 1161–1164 | Cite as

Protease inhibitors and in vitro digestibility of karanja (Pongamia glabra) oil seed residue. A comparative study of various treatments



Trypsin and chymotrypsin inhibitor activities (TIA and CIA) were assayed before and after processing of Karanja oil seed residue. Upon treatment, the loss of TIA and CIA varied with the type of processing or extraction: the reduction after solvent extraction ranged between 34 and 15%, respectively. These activities were completely removed in 2.4% HCl; 83.35 and 54.86% were removed on autoclaving; 33.86 and 15.30% on fermentation; and removal was 4.36–83.69% and 3.66–77.59% after exposure to different doses of gamma radiation (1, 5, 10, and 50 KGy). An in vitro digestibility study was carried out to confirm the inactivation of the inhibitors and showed improvements from 45 to 81%, with the maximum observed in 2.4% HCl solvent-refluxed residue. A linear relationship was observed between the reduction in protease inhibitor activities and the improvement in digestibility.

Key Words

Antinutrients autoclaving detoxification fermentation in-vitro digestibility irradiation Karanja oilseed residue nutritive value protease inhibitors solvent treatment 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Nadkarni, A.K., Pongamia glabra, in Indian Materia Medica, edited by K.M. Nadkarni, Bombay Popular Prakashan, India. 1975, vol. 1, pp. 1001–1004.Google Scholar
  2. 2.
    Vimal, D.P., and K.T. Naphade, Utilization of Nonedible Oil Seeds—Recent Trends, J. Sci. Ind. Res. 39:197–211 (1980).Google Scholar
  3. 3.
    Singh, U.V., Studies on Better Utilization of Nonedible Oil Seed Cakes, Karanja (Pongamia glabra) Seed Cake, Ph.D. Thesis, Indian Agriculture Research Institute, New Delhi, India, 1966.Google Scholar
  4. 4.
    Liener, I.E., Protease Inhibitors, in Toxic Constituent of Plant Foodstuffs. Academic Press, New York, 1969, pp. 8–68.Google Scholar
  5. 5.
    Liener, I.E., Effect of Antinutrients and Toxic Factors on Quality and Utilization of Legume Proteins, J. Food Sci. 41:1076–1079 (1976).CrossRefGoogle Scholar
  6. 6.
    Michail, D.E., and A.R. John, The Effect of Solvent Extraction upon the Utilization of Rapeseed Meal Protein by Rats, J. Sci. Food Agric. 34:917–920 (1983).CrossRefGoogle Scholar
  7. 7.
    Phillippy, B.Q., M.R. Johnston, S.H. Tao, and M.R.S. Fax, Inositol Phosphates in Processed Foods, J. Food Sci. 53:496–499 (1988).CrossRefGoogle Scholar
  8. 8.
    Piergiovanni, A.R., and C. Della Gatter, Amylase Inhibitors in Cowpea (Vigna ungriculata): Effect of Soaking and Cooking Methods, Food Chem. 51:79–81 (1994).CrossRefGoogle Scholar
  9. 9.
    Natanam, R., R. Kadirvel, and R. Ravi, The Toxic Effects of Karanja (Pongamia glabra Vent) Oil and Cake on Growth and Feed Efficiency in Broiler Chicks, Animal Feed Sci. Technol. 27:95–100 (1989).CrossRefGoogle Scholar
  10. 10.
    Rackis, J.J., W.J. Wolf, and C.E. Baker, Protease Inhibitors in Plant Foods. Content and Inactivation, Adv. Exp. Med. 199:299–347 (1986).Google Scholar
  11. 11.
    Siy, R.D., and F.D.F. Talbot, Preparation of Low Phytate Rapeseed Protein Ultrafiltration: 1. The Aqueous Extraction of Phytate from Deoiled Rapeseed Meal, J. Am. Oil Chem. Soc. 59:191–194 (1982).Google Scholar
  12. 12.
    Alpana, R., and B.M. Chauhan, Effect of Phytic Acid on Protein Digestibility (in vitro) and HC1 Extractibility of Minerals in Pearl Millet Sprouts, Cereal Chem. 70:504–506 (1993).Google Scholar
  13. 13.
    Gupta, M., and K. Neelum, Effect of rabedi Fermentation on Phytic Acid and In Vitro Digestibility of Barley, Nahrung 37:141–146 (1993).PubMedCrossRefGoogle Scholar
  14. 14.
    Singh, U., B. Singh, and O.D. Smith, Effect of Various Processing Methods on Phytic Acid and Protein Digestibility of Groundnut, J. Food Sci. Technol. 28:345–347 (1991).Google Scholar
  15. 15.
    Rhee, K.C., Detoxification and Deallergenation of Oil Seed Meals, Proc. World Conf., Oil Seed Tech. Util. 346:50–55 (1992).Google Scholar
  16. 16.
    Mulimani, V.H., and S. Paranjyothi, Effect of Heat Treatment on Trypsin/Chymotrypsin Activity of Red Gram (Cajanus cagan L.), Plant Foods Hum. Nutr. (Dordrecht, Neth.) 46:103–107 (1994).CrossRefGoogle Scholar
  17. 17.
    Hafez, Y.S., A.I. Mohamed, G. Singh, and F.M. Hewedy, Effect of Gamma Radiation on Protein and Fatty Acids of Soybean, J. Food Sci. 50:1271–1274 (1985).CrossRefGoogle Scholar
  18. 18.
    Joseph, A., and M. Dikshit, Effect of Irradiation on the Protease Inhibitor Activity and Digestibility (in vitro) of Safflower Oil Cake, J. Am. Oil Chem. Soc. 70:935–937 (1993).CrossRefGoogle Scholar
  19. 19.
    Mandal, B., Protease Inhibitors and In Vitro Protein Digestibility of Defatted Seed Cakes of Akashmoni and Karanja, Ibid.:1124–1126 (1985).CrossRefGoogle Scholar
  20. 20.
    Egan, H., R.S. Kirk, and R. Sawyers, General Chemical Methods, in Pearson’s Chemical Analysis of Food, 8th edn., Churchill Livingstone, Edinburgh, London, 1981, pp. 7–34.Google Scholar
  21. 21.
    Kakade, M.L., N. Simons, and I.E. Liener, An Evaluation of Natural vs. Synthetic Substrates for Measuring the Antitryptic Activity of Soybean Samples, Cereal Chem. 44:518–524 (1969).Google Scholar
  22. 22.
    Kadade, M.L., D.H. Swenson, and I.E. Liener, Note on the Determination of Chymotrypsin and Chymotrypsin Inhibitor Activity Using Casein, Anal. Biochem. 33:255–258 (1970).CrossRefGoogle Scholar
  23. 23.
    Fretzdorff, B., and J.M. Brummer, Reduction of Phytic Acid During Bread Making of Whole Meal Breads, Cereal Chem. 69:266–270 (1992).Google Scholar
  24. 24.
    Lowry, O.H., N.J. Rosebrough, A.L. Farr, and R.J. Randall, Protein. 9. Measurement with the Folin Phenol Reagent, J. Biol. Chem. 193:265–275 (1951).PubMedGoogle Scholar
  25. 25.
    Boonvisut, S., and J.R. Whitaker, Effect of Heat, Amylase, and Disulfide Bond Cleavage on the In-vitro Digestibility of Soybean Proteins, J. Agric. Food Chem. 24:1130–1135 (1976).PubMedCrossRefGoogle Scholar
  26. 26.
    Raghuramulu, N., K.N. Madhavan, and S. Kalyanasundaram, Statistical Methods, in A Manual of Laboratory Techniques, Silver prints Hyderabad-39, India, 1983, pp. 282–308.Google Scholar
  27. 27.
    Kapoor, A.C., and Y.P. Gupta, Trypsin Inhibitor Activity in Soybean Seeds, Ind. J. Nutr. Dietet. 15:429–431 (1978).Google Scholar
  28. 28.
    Nehad, M.A., Effect of Presoaking on Faba Beans. Enzyme Inhibitors and Polyphenol on Cooking, J. Agric. Food Chem. 28:1479–1482 (1991).Google Scholar
  29. 29.
    Sandberg, A.S., The Effect of Food Processing on Phytate Hydrolysis and Availability of Iron and Zinc, in Nutritional and Toxicological Consequences of Food Processing, Plenum Press, New York, 1991, pp. 499–508.Google Scholar
  30. 30.
    Singh, M., and A.D. Krikorian, Inhibition of Trypsin Activity In-Vitro by Phytate, J. Agric. Food Chem. 30:799–800 (1982).CrossRefGoogle Scholar
  31. 31.
    Higuchi, M., I. Truchiya, and I. Kazuo, Growth Inhibition and Small Intestinal Lesions in Rats After Feeding with Isolated Winged Bean Lectins, Agric. Biol. Chem. 48:695–698 (1984).Google Scholar
  32. 32.
    Sripad, G., and N. Rao, Effect of Methods to Remove Polyphenols from Safflower Meal on the Physiochemical Properties of the Proteins, J. Agric. Food Chem. 35:962–966 (1987).CrossRefGoogle Scholar
  33. 33.
    Jay, J.M., Food Preservation Using Irradiation, in Modern Microbiology, CBS Publishers and Distributers, Delhi, India, 1987, pp. 297–316.Google Scholar

Copyright information

© AOCS Press 1997

Authors and Affiliations

  1. 1.Biochemistry Division, Department of ChemistryUniversity of PunePuneIndia

Personalised recommendations