Effect of incubation temperature on the binding capacity of flavor compounds to myosin.

This study was aimed to investigate the effect of incubation temperature on the binding of hexanal, octanal and 3-methylbutyraldehyde to myosin. Fluorescence quenching, Fourier transform infrared spectroscopy, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC) and gas chromatography-mass spectrometry (GC-MS) were employed. An increase in aldehyde concentration led to a reduction in fluorescence intensity in myosin. SPR revealed that the interactions were involved in a rapid combination and dissociation, and the dissociation constants significantly decreased from 25 to 37 °C. ITC showed that the values of entropy, enthalpy and Gibbs free energy were negative. The interactions were driven by hydrogen bonds and van der Waals forces. GC-MS further demonstrated that the highest binding capacity occurred at 37 °C between myosin and aldehydes. The findings provide a new insight into the mechanism on controlling or maintaining meat flavor.