Mechanisms of heat damage in proteins. 7. The significance lysine-containing isopeptides and of lanthionine in heated 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. epsilon-N-(beta-L-aspartyl)-L-lysine and epsilon-N-(gamma-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.