In the present study, the formation of cross-links in processed pork was assessed through the analysis of two chemical structures: Schiff bases and disulphide bonds (Fig. 4a, b, respectively). Schiff bases are conjugated fluorophores formed as a result of the reaction between protein carbonyls and secondary amines (Este ´vez 2011). On the other hand, the oxidation of two cysteines leads to the formation of disulphide bonds (Soladoye et al. 2015). The formation of both protein cross-links was promoted during cooking and remained stable during the following chilled storage. Chelh et al. (2007) reported the formation of fluorescent pigments during meat cooking and linked their formation to the reaction of meat proteins with aldehydic products from lipid peroxidation. Later reports argued that the reaction between protein carbonyls and the d-amino groups located in the side-chains of alkaline amino acids may be the more plausible formation pathway for Schiff bases in oxidized meat proteins (Este ´vez 2011; Utrera and Este ´vez 2012b). These fluorescent products are believed to contribute to the formation of insoluble protein aggregates