Proteomics analysis of the influence of proteolysis on the subsequent glycation of myofibrillar protein.

Proteomics was used to study the influence of proteolysis on the glycation of myofibrillar proteins (MPs). Proteolysis by papain and proteinase K generated the highest level of amino acids (AAs) and peptides, respectively. Both the glycation degree (A value increased from 0.173 to 0.202-0.348) and speed (k value increased from 0.0099 to 0.0132-0.0145) were enhanced by proteolysis using papain and proteinase K. Proteomics analysis revealed that proteolysis largely enhanced the glycation site number in Lys, Arg and N-terminal residues (eg. Leu, Gly, Thr, Ala, Met, Ile, Phe and Val residues in myosin light chain). Proteolysis by papain preferentially acted on actin and therefore specifically increased the glycation sites from actin. Proteolysis reduced the level of aldehydes but enhanced the aromatic E-nose signals, possibly due to the combination of aldehydes with released AAs/peptides. The proteomics analysis helped to detail the relationship between proteolysis and subsequent glycation/flavour formation.

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Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.