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

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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 (SoANS) was found, suggesting potential formation of hydrophobic interactions between CMP. At higher temperatures (60 to 80°C), high SoANS 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, SoANS and SH-amount of red CMP were higher compared to white CMP. The differences in G'60min, SoANS, 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.

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