Authors: D G Dyer J A Blackledge B M Katz C J Hull H D Adkisson S R Thorpe T J Lyons J W Baynes
Publish Date: 1991/02/01
Volume: 30, Issue: 1, Pages: 29-45
Abstract
The Maillard or browning reaction between reducing sugars and protein contributes to the chemical deterioration and loss of nutritional value of proteins during food processing and storage This article presents and discusses evidence that the Maillard reaction is also involved in the chemical aging of longlived proteins in human tissues While the concentration of the Amadori adduct of glucose to lens protein and skin collagen is relatively constant with age products of sequential glycation and oxidation of protein termed glycoxidation products accumulate in these longlived proteins with advancing age and at an accelerated rate in diabetes Among these products are the chemically modified amino acids Nɛcarboxymethyllysine CML Nɛcarboxymethylhydroxylysine CMhL and the fluorescent crosslink pentosidine While these glycoxidation products are present at only trace levels in tissue proteins there is strong evidence for the presence of other browning products which remain to be characterized Mechanisms for detoxifying reactive intermediates in the Maillard reaction and catabolism of extensively browned proteins are also discussed along with recent approaches for therapeutic modulation of advanced stages of the Maillard reaction
Keywords: