The mechanism of peptide bonds cleavage and volatile compounds generated from pentapeptide to heptapeptide via Maillard reaction

This study is focused on the mechanism of peptide bond cleavage and volatile Maillard reaction products (MRPs) following reaction of 10 artificial oligopeptides with cysteine, xylose and thiamine. LC-TOF/MS was used to detect the chemistry of peptide bond cleavage in liquid media. GC–O–MS and a carbohydrate module labelling (CAMOLA) method were used to analyse and identify the formation pathways of volatile and semi-volatile MRPs. In this study, the theoretical foundation of seven principles of influencing factors acting on peptide chain cleavage has initially been summarised. At the start of this study assumptions were also made relating to heat resistance of peptide chain positions. A universal formation pathway map and a model of possible mechanisms of common product formation were proposed. This model was authenticated by this scientific study.