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Stability of tryptophan during food processing and storage

1. Comparative losses of tryptophan, lysine and methionine in different model systems

Published online by Cambridge University Press:  24 July 2007

Henrik K. Nielsen ,
D. De Weck ,
P. A. Finot ,
R. Liardon  and
R. F. Hurrell
Henrik K. Nielsen
Affiliation:
Research Department, Nestlé Products Technical Assistance Co. LtdCH-1814 La-Tour-de-Peilz, Switzerland
D. De Weck
Affiliation:
Research Department, Nestlé Products Technical Assistance Co. LtdCH-1814 La-Tour-de-Peilz, Switzerland
P. A. Finot
Affiliation:
Research Department, Nestlé Products Technical Assistance Co. LtdCH-1814 La-Tour-de-Peilz, Switzerland
R. Liardon
Affiliation:
Research Department, Nestlé Products Technical Assistance Co. LtdCH-1814 La-Tour-de-Peilz, Switzerland
R. F. Hurrell
Affiliation:
Research Department, Nestlé Products Technical Assistance Co. LtdCH-1814 La-Tour-de-Peilz, Switzerland
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Abstract

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1. The stability of tryptophan was evaluated in several different food model systems using a chemical method (high pressure liquid chromatography after alkaline-hydrolysis) and rat assays. Losses of tryptophan were compared with the losses of lysine and methionine.

2. Whey proteins stored in the presence of oxidizing lipids showed large losses of lysine and extensive methionine oxidation but only minor losses of tryptophan as measured chemically. The observed decrease in bioavailable tryptophan was explained by a lower protein digestibility.

3. Casein treated with hydrogen peroxide to oxidize all methionine to methionine sulphoxide showed a 9% loss in bioavailable tryptophan.

4. When casein was reacted with caffeic acid at pH 7 in the presence of monophenol monooxygenase (tyrosinase; EC 1.14.18.l), no chemical loss of tryptophan occurred, although fluorodinitrobenzene-reactive lysine fell by 23%. Tryptophan bioavailability fell IS%, partly due to an 8% reduction in protein digestibility.

5. Alkali-treated casein (0.15 M-sodium hydroxide, 80°,4 h) did not support rat growth. Chemically-determined tryptophan, available tryptophan and true nitrogen digestibility fell 10, 46 and 23% respectively. Racemization of tryptophan was found to be 10% (D/(D+L)).

6. In whole-milk powder, which had undergone ‘early’ or ‘advanced’ Maillard reactions, tryptophan, determined chemically or in rat assays, was virtually unchanged. Extensive lysine losses occurred.

7. It was concluded that losses of tryptophan during food processing and storage are small and of only minor nutritional importance, especially when compared with much larger losses of lysine and the more extensive oxidation of methionine.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 53 , Issue 2 , March 1985 , pp. 281 - 292
Copyright
Copyright © The Nutrition Society 1985

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