Investigation into the impact of aldehyde dehydrogenase on pig liver proteins and its catalytic degradation of E,E-2,4-heptadienal

Van der Waals forces and hydrogen bonding dominate the interactions between PLvPs and aldehyde. • PLvP conformational changes facilitate ALDH degradation of aldehyde. • ALDH restored PLvP structure and function post-aldehyde binding. • MD simulations confirmed E , E -2,4-heptadienal-induced conformational shifts. Yeast fermentation has been shown to reduce the concentration of aldehydes, characteristic off-flavors in animal livers, although the underlying mechanisms of deodorization remain unclear. This study investigated the oxidative catalytic degradation of E , E -2,4-heptadienal by ALDH (Aldehyde dehydrogenase) from Saccharomyces cerevisiae within a complex system of pig liver proteins (PLvPs) and the aldehyde compound. Fluorescence quenching, thermodynamic, and FTIR analyses demonstrated that E , E -2,4-heptadienal spontaneously bound to PLvPs primarily via van der Waals forces and hydrogen bonding. This binding induced conformational changes in PLvPs, which were found to enhance the susceptibility of E , E -2,4-heptadienal to ALDH-mediated degradation. Subsequent ALDH treatment significantly improved the binding capacity of the complexes (by 13.21–78.18%) and largely restored the functional and structural integrity of PLvPs. Molecular dynamics and docking simulations further supported that E , E -2,4-heptadienal binding to PLvPs facilitates ALDH catalysis via these conformational alterations. This study highlights the crucial role of ALDH-mediated oxidative catalytic degradation in modulating the flavor-binding capacity of PLvPs, offering a novel enzymatic strategy for targeted off-flavor elimination and enhancing the sensory quality and industrial utility of liver-based products. Download: Download high-res image (227KB) Download: Download full-size image