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Mechanisms of heat damage in proteins

2.* Chemical changes in pure proteins

Published online by Cambridge University Press:  09 March 2007

J. Bjarnason  and
K. J. Carpenter
J. Bjarnason
Affiliation:
Department of Agricultural Science and Applied Biology, University of Cambridge
K. J. Carpenter
Affiliation:
Department of Agricultural Science and Applied Biology, University of Cambridge
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Abstract

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1. Bovine plasma albumin (BPA) containing approximately 14% moisture, when heated for 27 h at 115° suffered an appreciable loss of cystine and a small loss of lysine; at 145° all the amino acids except glutamic acid and those with paraffin side-chains, showed considerable losses. Isoleucine also showed some loss through racemization to alloisoleucine.

2. BPA heated at 115° evolved H2S; at 145° other sulphur compounds were released as well, all coming from the breakdown of cystine. Possible mechanisms for this are discussed.

3. Ammonia was also liberated from BPA heated at 115°. The degree of correlation of lysine binding in different proteins with ammonia liberation and amide changes has led us to suggest that the main reaction of ε-amino lysine groups is with amide groups of asparagine and glutamine. Reaction of ε-amino groups with carboxylic groups is thought to be less important.

4. Model experiments have shown that a reaction between amide groups and the e-amino group of lysine in proteins can occur at practical drying temperatures.

5. Reactions of the ε-amino group of lysine with destruction products of cystine is also considered to be partially responsible for the lysine binding in heated proteins.

Type
Research Article
Information
British Journal of Nutrition , Volume 24 , Issue 1 , March 1970 , pp. 313 - 329
Copyright
Copyright © The Nutrition Society 1970

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