Model studies on the heating of food proteins. Amino acid composition of lysozyme, ribonuclease and insulin after dry heating.
Lysozyme, ribonuclease and insulin were exposed to dry heating for 1 to 24 h at temperatures between 80 and 180 degrees C. Amino acid analyses of the heated samples showed that most of the amino acids are stable up to 120 degrees C. Initially, at higher temperatures, an almost rectilinear decrease took place which reached a critical stage at 160 degrees C. Nonpolar aliphatic, acidic and aromatic amino acids were all relatively stable (maximum loss less than 20% after 24 h at 180 degrees C). The lability of the other amino acids increased in the order proline, arginine, histidine, cysteine, threonine, lysine, tryptophan, serine, and methionine. Methionine was 86% decomposed after 24 h at 180 degrees C. Loss of trinitrobenzene sulfonic acid-reactive lysine ("available lysine") reached 20% at 100 degrees C and essentially 100% after 24 h at 180 degrees C. Maximum loss in weight during heating was 11%, although maximum protein loss was between 20 and 35%. Reaction orders and activation energies were estimated for some of the amino acid losses. Of the atypical amino acids ("hot spots") lysinoalanine, allo-isoleucine and ornithine that were detected, only lysinoalanine is useful as an indicator to detect amino acid damage after dry heating.
D000596:Amino Acids / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D004044:Dietary Proteins; D004355:Drug Stability; D006358:Hot Temperature; D007328:Insulin; D008239:Lysine / Q000032:analysis; D009113:Muramidase; D012260:Ribonucleases; D013997:Time Factors; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D004044:Dietary Proteins; D007328:Insulin; D014364:Tryptophan; D012260:Ribonucleases; D009113:Muramidase; D008239:Lysine