Crosslinkage of proteins by dehydroascorbic acid and its degradation products

• Published in: Food chemistry Vol. 70; no. 2; pp. 193 - 198
• Main Authors: Fayle, S.E., Gerrard, J.A., Simmons, L., Meade, S.J., Reid, E.A., Johnston, A.C.
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.08.2000
• Subjects: Crosslinking; Dehydroascorbic acid; Maillard reaction; Ribonuclease; OPA, o-phthaldialdehyde; RNAse A, ribonuclease A; DHA, dehydroascorbic acid; Dehydroascorbic acid; SE-HPLC, size exclusion high performance liquid chromatography; Maillard reaction; Crosslinking; Ribonuclease; SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/S0308-8146(00)00077-7

Protein crosslinking can have a profound effect on the structure and function of proteins in food. Dehydroascorbic acid (DHA) has been shown to be involved in Maillard type chemistry that leads to protein crosslinking. In this study, the effect of temperature on the rate of this reaction was studied. The reaction was shown to proceed rapidly at temperatures that may be encountered during food processing. In order to assess the relative reactivity of DHA and its breakdown products, five known degradation products were reacted with protein and their crosslinking ability, via Maillard chemistry, was assessed. Oxalic acid did not effect protein crosslinking. Threose, glyoxal, diacetyl and methyl glyoxal all reacted faster than DHA. The main crosslinking reaction observed was shown to involve a lysine residue. Our results suggest that these molecules may be important in determining the modification of protein functionality during food processing.