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The effect of dietary raw and autoclaved soya-bean protein fractions on growth, pancreatic enlargement and pancreatic enzymes in rats

Published online by Cambridge University Press:  24 July 2007

Michael Naim ,
Arieh Gertler  and
Yehudith Birk
Michael Naim
Affiliation:
Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Arieh Gertler
Affiliation:
Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Yehudith Birk
Affiliation:
Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
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Abstract

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1. Raw soya-bean meal (RS) was fractionated into soya-bean lyophilized extract (SLE), soya-bean lyophilized residue (SLR), acid-precipitated proteins (APP) and whey proteins.

2. Trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1) inhibitors (TI) were soluble at pH 8 and remained soluble after the extract was acidified to pH 4·4. Except for whey, heating abolished, almost totally, their inhibiting activity.

3. Feeding SLE diet (high TI content) and APP diet (low TI content) resulted in growth depression below the RS level. Feeding the SLR diet resulted in an optimal growth. Feeding diets containing heated fractions improved the growth rate though not to the level observed with heated RS (HS) diet.

4. RS, SLE, APP and whey diets produced similar pancreatic enlargement which could be totally (RS, whey) or partially (SLE, APP) abolished by heating.

5. Feeding the RS diet reduced pancreatic amylase content. The factor responsible for this effect cofractionated with SLE and whey proteins.

6. Two groups of factors in the various diets were probably responsible for the elevation in pancreatic proteases. The first group were the heat-labile factors present in RS, SLE and whey whereas the second group resisted the heat treatment and were found in APP and SLR.

7. The results suggest that for optimal growth rate of rats, heat treatment should be given to the unfractionated soya-bean proteins rather than to the isolated fractions. The results further indicated that TI are not the only factors that can lead to pancreatic enlargement and changes in pancreatic enzymes composition.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 47 , Issue 2 , March 1982 , pp. 281 - 288
Copyright
Copyright © The Nutrition Society 1982

References

Barnes, R. H. & Kwong, E. (1965). J. Nutr. 86, 245.CrossRefGoogle Scholar
Bernfeld, P. (1955). Meth. Enzym. 1, 149.CrossRefGoogle Scholar
Bielorai, R. & Bondi, A. (1963). J. Sci. Fd Agric. 14, 124.CrossRefGoogle Scholar
Booth, A. N., Robbins, D. J., Ribelin, W. E. & De Eds, F. (1960). Proc. Soc. exp. Biol. Med. 104, 681.CrossRefGoogle Scholar
Borchers, R. (1958). J. Nutr. 66, 235.CrossRefGoogle Scholar
Box, G. E. P., Hunter, W. G. & Hunter, J. S. (1978). Statistics for Experimenters. An Introduction to Design, Data Analysis and Model Building. New York: John Wiley.Google Scholar
Gertler, A., Birk, Y. & Bondi, A. (1967). J. Nutr. 91, 358.CrossRefGoogle Scholar
Gertler, A. & Nitsan, Z. (1970). Br. J. Nutr. 24, 893.CrossRefGoogle Scholar
Gorril, A. D. L. & Thomas, J. W. (1967). Analyt. Biochem. 19, 211.CrossRefGoogle Scholar
Green, G. M. & Lyman, R. L. (1972). Proc. Soc. exp. Biol. Med. 140, 6.CrossRefGoogle Scholar
Hegarty, P. V. J., Kim, S. H. & Ahn, P. C. (1977). Growth 41, 221.Google ScholarPubMed
Horwitz, W. (1960). Official Methods of Analyses of the Association of Official Agricultural Chemists. Washington, DC: Association of Official Agricultural Chemists.Google Scholar
Johnson, L. R. (1974). In Gastrointestinal Physiology, p. 17 [Jacobson, E. D. and Shanbour, L. L., editors]. Butterworths: University Park Press.Google Scholar
Konijn, A. M., Birk, Y. & Guggenheim, K. (1970). J. Nutr. 100, 361.CrossRefGoogle Scholar
Liener, I. E. (1972). In Soyabeans: Chemistry and Technology, vol. 1, p. 203 [Smith, A. K. and Circle, S. J., editors]. Westport Conn: Avi Publishing Co.Google Scholar
Maayani, S. & Kulka, R. S. (1968). J. Nutr. 96, 363.CrossRefGoogle Scholar
Madar, Z., Tencer, Y., Gertler, A. & Birk, Y. (1976). Nutr. Metab. 20, 234.CrossRefGoogle Scholar
Moor, S., Spackman, D. H. & Stein, W. H. (1958). Analyt. Chem. 30, 1185.CrossRefGoogle Scholar
Naim, M., Brand, J. G., Kare, M. R., Kaufmann, N. A. & Kratz, C. M. (1980). Physiol. Behav. 25, 609.CrossRefGoogle Scholar
Niess, E., Ivy, C. A. & Nesheim, M. C. (1972). Proc. Soc. exp. Biol. Med. 140, 6.CrossRefGoogle Scholar
Nitsan, Z. & Gertler, A. (1972). Br. J. Nutr. 27, 337.CrossRefGoogle Scholar
Nitsan, Z. & Liener, I. E. (1976). J. Nutr. 106, 300.CrossRefGoogle Scholar
Rackis, J. J. (1974). J. Am. Oil Chem. Soc. 51, 161A.CrossRefGoogle Scholar
Rackis, J. J., Smith, A. K., Nash, A. M., Robbins, D. J. & Booth, A. N. (1963). Cereal Chem. 40, 531.Google Scholar
Rama Reo, P. B., Metta, V. C., Morton, H. W. & Johnson, B. C. (1960). J. Nutr. 71, 361.Google Scholar
Rothman, S. S. & Wells, H. (1967). Am. J. Physiol. 213, 215.CrossRefGoogle Scholar
Saxena, H. C., Jensen, L. S. & McGinnis, J. (1963). Proc. Soc. exp. Biol. Med. 112, 101.CrossRefGoogle Scholar
Schingoethe, D. J., Aust, S. D. & Thomas, J. W. (1970). J. Nutr. 100, 739.CrossRefGoogle Scholar
Spackman, D. H. (1963). Fedn Proc. Fedn Am. Socs exp. Biol. 22, 244.Google Scholar