Mechanisms of heat damage in proteins

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 H 2 S; 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.