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The nutritive value of groundnut protein

1. Some effects of heat upon nutritive value, protein composition and enzyme inhibitory activity

Published online by Cambridge University Press:  09 March 2007

A. A. Woodham
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen
R. Dawson
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen
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Abstract

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1. A laboratory-prepared groundnut flour defatted at room temperature (DGF) was subjected to dry heat or to pressure steaming under varying conditions of time and temperature, and its amino acid composition and nutritive value, the latter assessed by a chick growth test—the gross protein value (GPV) test, were compared with those of some commercial groundnut meals. Trypsin inhibitor activity, available lysine value (ALV) and ‘arachin’ and ‘conarachin’ content and, in some instances, GPV were estimated in the heated samples.

2. The amino acid composition of the DGF and of commercial meals of high, medium and low GPV did not differ markedly, and the GPV of the DGF fell within the range of the three commercial samples.

3. Both dry and moist heat under specified conditions lowered ALV in the DGF and in the ‘arachin’ fractions, but had little effect on the ALV of the ‘conarachin’ fraction.

4. Moist, but not dry, heat rapidly removed trypsin inhibitor activity, and dry, but not moist, heat lowered GPV.

5. Neither ‘conarachin’ content nor trypsin inhibitor activity correlated with GPV in a range of commercial groundnut meals.

6. Dry heat (125. for 5 h) lowered nutritive value and ‘conarachin’ content but did not reduce the amount of total nitrogen soluble in sodium chloride solution.

7. No trypsin-inhibiting activity was found in the testa (skins) but these did exhibit growth-depressant properties for chicks. This property was removed by mild moist heat treatment.

8. ‘Arachin’ isolated from a commercial groundnut meal was valueless as a protein supplement for a cereal ration for chicks; ‘conarachin’ by itself, and mixed with arachin (1:3) was equivalent in GPV to the parent meal.

9. A factor other than those considered here, and possibly unassociated with processing, is primarily responsible for the differences in growth-promoting qualities of the commercial groundnut meals used in this work.

Type
Research Article
Copyright
Copyright © The Nutrition Society 1968

References

Anantharaman, K. & Carpenter, K. J. (1965). Proc. Nutr. Soc. 24, xxxii.Google Scholar
Anson, M. L. (1938–9). J. gen. Physiol. 22, 79.CrossRefGoogle Scholar
Baernstein, H. D. (1938). J. biol. Chem. 122, 781.CrossRefGoogle Scholar
Barnes, M. McC. & Woodham, A. A. (1963). J. Sci. Fd Agric. 14, 109.CrossRefGoogle Scholar
Borchers, R. & Ackerson, C. W. (1950). J. Nutr. 41, 339.CrossRefGoogle Scholar
Borchers, R., Ackerson, C. W. & Sandstedt, R. M. (1947). Archs Biochem. 12, 367.Google Scholar
Boyne, A. W., Carpenter, K. J. & Woodham, A. A. (1961). J. Sci. Fd Agric. 12, 832.CrossRefGoogle Scholar
Cama, H. R. & Morton, R. A. (1950). Br. J. Nutr. 4, 297.CrossRefGoogle Scholar
Carpenter, K. J. (1960). Biochem. J. 77, 604.CrossRefGoogle Scholar
Chopra, A. K. & Sidhu, G. S. (1967 a). Br. J. Nutr. 21, 519.CrossRefGoogle Scholar
Chopra, A. K. & Sidhu, G. S. (1967 b). Br. J. Nutr. 21, 583.CrossRefGoogle Scholar
Dawson, R. & Woodham, A. A. (1966). Proc. Nutr. Soc. 25, ix.Google Scholar
Duckworth, J., Woodham, A. A. & MacDonald, I. (1961). J. Sci. Fd Agric. 12, 407.CrossRefGoogle Scholar
Fincher, H. D. (1958). In Processed Plant Protein Foodstuffs, p. 67. [Altschul, A. M., editor.] New York: Academic Press Inc.Google Scholar
Fontaine, T. D., Samuels, C. S. & Irving, G. W. (1944). Ind. Engng Chem. analyt. edn 36, 625.CrossRefGoogle Scholar
Heiman, V., Carver, J. S. & Cook, J. W. (1939). Poult. Sci. 18, 464.CrossRefGoogle Scholar
Johns, C. O. & Jones, D. B. (1916). J. biol. Chem. 28, 77.CrossRefGoogle Scholar
Liener, I. E. (1958). In Processed Plant Protein Foodstuffs, p. 79. [Altschul, A. M., editor.] New York: Academic Press Inc.Google Scholar
Lyman, C. M., Chang, W. Y. & Couch, J. R. (1953). J. Nutr. 49, 679.CrossRefGoogle Scholar
Macheboeuf, M. & Tayeau, F. (1942). C. r. hebd. Séanc. Acad. Sci., Paris 214, 37. Quoted in Nutr. Abstr. Rev. 12, 637.Google Scholar
Mitchell, H. H., Hamilton, T. S. & Beadles, J. R. (1949). J. Nutr. 39, 413.CrossRefGoogle Scholar
Moore, S. (1963). J. biol. Chem. 238, 235.CrossRefGoogle Scholar
Moore, S., Spackman, D. H. & Stein, W. H. (1958). Analyt. Chem. 30, 1185.CrossRefGoogle Scholar
Rosen, G. D. (1958). In Processed Plant Protein Foodstuffs, p. 419. [Altschul, A. M., editor.] New York: Academic Press Inc.Google Scholar
Sure, B. (1920). J. biol. Chem. 43, 443.CrossRefGoogle Scholar
Tombs, M. P. (1965). Biochem. J. 96, 119.CrossRefGoogle Scholar
Woodham, A. A. & Dawson, R. (1966). Proc. Nutr. Soc. 25, viii.Google Scholar
Zuckerman, S. (1959). Nature, Lond. 183, 1303.CrossRefGoogle Scholar