Mechanisms of heat damage in proteins. 8. The role of sucrose in the susceptibility of protein foods to heat damage
- 1 September 1977
- journal article
- research article
- Published by Cambridge University Press (CUP) in British Journal of Nutrition
- Vol. 38 (2) , 285-297
- https://doi.org/10.1079/bjn19770089
Abstract
1. A high-protein yeast cake, based on ovalbumin and lactalbumin, and containing 200 g sucrose/kg was baked and toasted as previously described by Block, Cannon, Wissler, Steffe, Straube, Frazier & Woolridge (1946). This caused a severe reduction in its protein quality for rats, and in its fluorodinitrobenzene (FDNB)-reactive lysine content. The damage appeared to be caused by inversion of sucrose to glucose and fructose during fermentation by the yeast followed by Maillard reactions. Processing an albumin-sucrose mixture in a similar way but without fermentation caused no loss in nutritional value for rats and a small reduction in FDNB-reactive lysine.2. Sucroselysine solutions were prepared and heated as previously described by El-Nockrashy & Frampton (1967). Contrary to their findings, we detected no loss of lysine after storage for 16 h at 35° or after heating for 2 h at 100°, although after heating for 4 h at 121° about 0.7 of the original lysine remained. At an alkaline pH, sucrose hydrolyses only slowly even at 121°, and this is catalysed to some extent by the presence of lysine.3. A ‘dry’ albumin-sucrose mixture (10-200 mg moisture/g) was heated in sealed glass ampoules under a range of conditions. The loss of FDNB-reactive lysine was stongly dependent on the processing conditions; in particular it was decreased by an increase in pH. After 2 h at 121°, lysine damage caused by sucrose was similar to that caused by glucose. Lysine damage due to sucrose was believed to follow on from its breakdown to glucose and fructose.4. Although the presence of sucrose does not make proteins highly sensitive to Maillard reactions and loss of nutritive value, it must not be considered entirely inert. Our results confirm earlier work indicating that its presence at relatively high levels in oil seeds may be largely responsible for the damage to protein quality observed when they are severely processed.This publication has 20 references indexed in Scilit:
- Le blocage de la lysine par la réaction de Maillard. II. Propriétés chimiques des dérivés N‐(désoxy‐1‐D‐fructosyl‐1) et N‐(désoxy‐1‐D‐lactulosyl‐1) de la lysineHelvetica Chimica Acta, 1972
- Problems in the determination of FDNB‐available lysineJournal of the Science of Food and Agriculture, 1971
- Effects of heat processing on the nutritional value of groundnut products II.-Individual amino acidstJournal of the Science of Food and Agriculture, 1971
- Destruction of lysine by nonreducing sugarsBiochemical and Biophysical Research Communications, 1967
- The differential determination of lysine in heated milk II.—Comparison of thein vitro methods with the biological evaluationJournal of the Science of Food and Agriculture, 1967
- Chemical and nutritional changes in stored herring mealBritish Journal of Nutrition, 1962
- Biological evaluation of proteins: a new aspectBritish Journal of Nutrition, 1957
- Studies of the reaction between proteins and reducing sugars in the ‘dry’ state III. Nature of the protein groups reactingBiochimica et Biophysica Acta, 1950
- Inactivation of Amino Acids by AutoclavingScience, 1949
- Studies of the reaction between proteins and reducing sugars in the “dry” stateBiochimica et Biophysica Acta, 1949