Abstract

The aim of this work was to investigate the influence of dielectric barrier discharge cold plasma (DBD-CP) on the structure and aroma compounds binding capacity of myofibrillar proteins (MPs) extracted from Chinese dry-cured bacon. MPs were treated with DBD-CP at 0, 50, 60 and 70 kV for 150s to monitor the binding ability with aroma compounds such as 3-methyl-butanal, 2-methyl-butanal, nonanal, heptanal and octanal, microstructure, primary and secondary structure changes of MPs using GC-MS, SDS-PAGE, scanning electron microscope (SEM) and FTIR spectroscopy. FTIR spectroscopy revealed a decrease in the α-helices structure while an increasing portion of β-sheets and random coils for all treatments, the relative contents of β-turns had no significant difference between treatments. The flavor compounds binding capacity of MPs enhanced from 50 kV to 70 kV treatment, probably due to the different modifications in protein structure and surface, also the oxidation systems generated by DBD-CP treatment increased hydrophobicity and unfolding of MPs. The result also showed that hydrophobic amino acids increased from 50 kV to 70 kV treatment which could be related to the improvement of binding ability. This study demonstrated that DBD-CP could be exploited to modify the functionality of MPs and improve the flavor of meat products.

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