Mechanisms of heat damage in proteins

Abstract

1. Studies have been made with solvent-extracted chicken muscle, bovine plasma albumin (BPA) and other proteins, all severely heated in the absence of carbohydrates so as to cause a large decrease in their fluorodinitrobenzene (FDNB)-reactive lysine contents.2. ɛ-N-(β-L-aspartyl)-L-lysine and ɛ-N-(γ-L-glutamyl)-L-lysine isopeptides were determined after enzymic digestion of heated chicken muscle, and their content was found to increase as the material was subjected to more heat treatment. Heated chicken muscle was not found to contain lanthionine. Heated BPA, on the other hand, was found to contain lanthionine but not the isopeptides. Both lanthionine and isopeptide cross-linkages were detected in most of the other heated proteins. There was some difficulty in quantifying the amounts of isopeptides formed on heat treatment, because the enzymic digestion procedure used in their isolation appeared to be incomplete. Neither lysinoalanine nor ornithinoalanine was detected in any of the test materials.3. The severely heated chicken muscle was fed to rats, and ileal and faecal digestibilities were studied. Protein digestibility was found to be greatly reduced after heat treatment, although the isopeptides themselves appeared to be at least as digestible as the total N component, total lysine, or FDNB-reactive lysine. However, the reduction in ileal N digestibility only partly accounted for the much larger reduction in nutritive value, as measured by net protein ratio ((weight loss of N-free animals + weight gain of test animals) ÷ weight of crude protein (N × 6.25) consumed by test animals). Possible reasons for this are discussed.