DENATURATION THERMOPROFILES OF SOME PROTEINS
- 1 November 1970
- journal article
- Published by Wiley in Journal of Food Science
- Vol. 35 (6) , 725-727
- https://doi.org/10.1111/j.1365-2621.1970.tb01980.x
Abstract
SUMMARY– Denaturation thermoprofiles of raw beef muscle tissue and egg albumin were determined. Irreversible changes occurred in two stages: the first peak was observed at 65° and 73°C and the second at 82° and 83°C, respectively for beef muscle tissue and egg albumin. Pertinent calculations suggest that the second peak is due to changes in the water structures. It may be hypothesized that protective, semicrystalline water structures surrounding the nonpolar amino acid radicals of proteins were collapsed by heat, followed by the formation of hydrophobic bonding yielding aggregated denatured state. Thermodynamic information was obtained from the thermoprofiles.Keywords
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