Exploration of interaction between porcine myofibrillar proteins and selected ketones by GC-MS, multiple spectroscopy, and molecular docking approaches

Abstract

Myofibrillar proteins (MPs) are the major components of meat and meat products, which can affect the flavour perception by interacting with volatile compounds. Therefore, the interaction between ketones (2-pentanone, 2-hexanone, and 2-heptanone) and porcine MPs was investigated in this work. The results showed that the binding ability of ketones to MPs was significantly enhanced with increasing protein concentration (p < 0.05); moreover, larger ketone carbon chains resulted in a stronger binding between MPs and ketones (p < 0.05). The MP-ketone interaction occurred through irreversible covalent binding and reversibly physicochemical binding, in which hydrophobic interactions may play a more predominant role. Furthermore, static and dynamic quenching occurred during the binding between MPs and ketones, leading to changes in the secondary structure and microenvironment of MPs. Finally, the results of molecular docking further confirmed that the hydrophobic interaction was the main driving force in the myosin-ketones systems. This work improves our understanding of the interaction mechanism between ketones and MPs at the molecular level.

Keywords: Fluorescence quenching; Interaction mechanism; Ketones; Molecular docking; Porcine myofibrillar proteins; Synchronous fluorescence spectra.