Effect of pH on the interaction of porcine myofibrillar proteins with pyrazine compounds

The influence of pH-induced structural modifications of myofibrillar proteins (MPs) on their interaction mechanisms with pyrazine compounds was investigated. At a lower pH (4.9, 5.5), MPs aggregated to larger particle sizes due to enhanced the protein–protein interactions. The binding with pyrazine compounds was strongly affected by pH and the nature of flavor compounds. MPs exhibited flavor releasing behavior, probably due to protein–protein interactions and surface tension. Fluorescence analysis revealed that the interaction of pyrazine compounds with MPs followed a combination of static and dynamic quenching. The changes in quenching constant ( K sv ) might be attributed to a dynamic quenching, probably due to protein aggregation. The percentages of free 2,5-Dimethylpyrazine (2,5-DMP) were similar to K sv . Thermodynamic parameters indicated that electrostatic interactions and hydrophobic interactions were the major acting forces in the binding of MPs to 2,5-DMP. The binding of 2,5-DMP increased the α-helix content of MPs.