Binding of Selected Aroma Compounds to Myofibrillar Protein, Sarcoplasmic Protein, and Collagen during Thermal Treatment: Role of Conformational Changes and Degradation of Proteins.

Abstract

To investigate the effects of conformational changes and thermal degradation of myofibrillar protein (MP), sarcoplasmic protein (SP), and collagen (CO) on the binding ability for aroma compounds during heating. Using SDS-PAGE, HPLC, and LC-MS/MS, a consistent rise in the total concentration of peptides and free amino acids formed by the thermal degradation of proteins was observed. The surface hydrophobicity, total sulfhydryl content, particle size, and secondary structure content of proteins changed significantly over time. Furthermore, the aroma binding ability of proteins was determined by gas chromatography-mass spectrometry. The results revealed an increase in binding ability during 5 or 10 min of heating due to protein unfolding and the accumulation of degradation products. However, the binding ability decreased due to protein aggregation with prolonged heating. Notably, all proteins exhibited strong affinity toward (E)-2-octenal, (E,E)-2,4-decadienal, 2-methyl-3-furanthiol, and dimethyl trisulfide. The binding ability of MP and SP was similar but differed significantly from that of CO, which had lower binding ability for hexanal, (E)-2-octenal, (E,E)-2,4-decadienal, and dimethyl trisulfide compared to MP and SP.