Nutritional and chemical changes in heated casein
- 1 September 1974
- journal article
- Published by Oxford University Press (OUP) in International Journal of Food Science & Technology
- Vol. 9 (3) , 301-308
- https://doi.org/10.1111/j.1365-2621.1974.tb01777.x
Abstract
Summary: Samples of commercial casein were processed either in solution or dry at temperatures between 100° and 130° for up to 8 hr. Denaturation (loss of solubility) occurred mainly at 120° and 130° and was preceded by darkening and by changes in gel filtration pattern, which indicated that molecular association had taken place. In samples subjected to severe heat treatment there were significant losses of aspartic acid, threonine, serine, cystine, histidine and lysine but apparent increases in glycine and alanine. The relationships between the various changes are discussed.Keywords
This publication has 5 references indexed in Scilit:
- Mechanisms of heat damage in proteinsBritish Journal of Nutrition, 1970
- Milk ProteinsPublished by Elsevier ,1967
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- Automatic Recording Apparatus for Use in Chromatography of Amino AcidsAnalytical Chemistry, 1958
- Effect of Dry Heat on ProteinsIndustrial & Engineering Chemistry, 1947