Characterization of protein aggregates following a heating and freezing process

Proteomic study of the effect of different cooking methods on protein oxidation in fish fillets

“…Not surprisingly, samples subjected to the harshest treatment had the lowest content of MHC as was consistent with MHC being distinctively intolerant to heating reported by many authors. 32,33 The aforementioned results could be explained both by formation of polymerized protein aggregates of which some were too large to get into the gels, 33 and by fragmentation of MHC into smaller protein molecules which, in our study, was conrmed by the detection of MHC-derived peptides in the digest of actin from cooked samples (data not shown).…”

Effect of green tea or rosemary extract on protein oxidation in Bologna type sausages prepared from oxidatively stressed pork

“…Thus, whether the loss of thiols and increased protein polymerization is caused by a prooxidative effect from phenol addition or by the formation of thiol-quinone adducts cannot be concluded based on experiments conducted in the present study. However, polymerization of actin by disulfide cross-link formation has been found to be less pronounced compared to MHC in model systems under accelerated oxidation conditions (Decker, Xiong, Calvert, Crum, & Blanchard, 1993;Morzel, Gatellier, Sayd, Renerre, & Laville, 2006;Xiong, Park, & Ooizumi, 2009), and no loss in actin was observed in fresh pork processed at 100°C for up to 60 min, indicating that actin is rather stable at temperatures below 100°C (Kajak-Siemaszko et al, 2011). This suggests that the distinct loss of actin observed in Fig.…”

Protein oxidation and proteolysis during roasting and in vitro digestion of fish (Acipenser gueldenstaedtii)

“…Most of the protein bands above 55 kDa weakened and gradually vanished with prolonged roasting time, which could be explained by the loss of solubility due to protein denaturation and breakdown of these large proteins during heating treatment. In addition, aggregation of protein could happen as well, rendering the molecule too large to enter the gel . It is noteworthy that certain proteins (e.g.…”

“…In addition, aggregation of protein could happen as well, rendering the molecule too large to enter the gel. 32 It is noteworthy that certain proteins (e.g. molecular weight (MW) around 40 kDa), in terms of their intensity, remained almost unchanged throughout roasting time, indicating that these proteins were fairly robust even upon lengthy roasting.…”