Isothermal gelation behavior of myofibrillar proteins from white and red chicken meat at different temperatures

ABSTRACT This paper provides insights in the isothermal gelation behavior of white and red chicken myofibrillar proteins (CMP) at different temperatures (20 to 80°C) and the underlying aggregation mechanism, allowing understanding of structure formation in poultry products during thermal processing. At low temperatures (20 to 60°C), an increase in aromatic surface hydrophobicity (So ANS) was found, suggesting potential formation of hydrophobic interactions between CMP. At higher temperatures (60 to 80°C), high So ANS and a significant decrease in total sulfhydryl amount (SH-amount) strongly indicate the presence of hydrophobic interactions and disulfide bonding, resulting in aggregation, as suggested by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The elastic modulus G’ after 60 min isothermal heating (G’60min) significantly increased at 70 or 80°C, depending on the type of CMP. Differences in G’60min between white and red CMP were rather small at low temperatures (20 to 60°C). However, at 70°C, white CMP reached higher G’60min compared to red CMP, while the opposite was observed at 80°C. Overall, for every temperature studied, So ANS and SH-amount of red CMP were higher compared to white CMP. The differences in G’60min, So ANS, and SH-amount between white and red CMP were probably due to different isoforms. The results may help to steer quality characteristics of poultry products through intelligent choice of processing conditions.