Authors
Jin Luo, Kaina Qiao, Shihao Sun, Baoguo Sun, Li Liang, Yuyu Zhang
Published in
Food chemistry. Volume 525. Issue Pt 3. Pages 150552. Jul 24, 2026. Epub Jul 24, 2026.
Abstract
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.
PMID:
42508122
Bibliographic data and abstract were imported from PubMed on 28 Jul 2026.
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