Jiao Xu , Qiuming Chen , Yan Qiu , Zhaojun Wang , Maomao Zeng , Fang Qin , Jie Chen , Zhiyong He
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引用次数: 0
Abstract
Competitive binding of flavor compounds to proteins offers a strategy for mitigating off-flavors in soy protein isolate (SPI). We hypothesized that highly competitive pleasant flavor compounds can facilitate the release of off-flavors by occupying their binding sites during SPI preparation. Molecular docking identified four binding pockets on β-conglycinin (7S) and glycinin (11S) proteins interacting with off-flavors. From 54 pleasant flavors, 30 were screened, focusing on seven: δ-nonalactone, δ-decalactone, δ-undecalactone, furaneol, geraniol, nerol, and geranyl acetate. Sensory evaluation and gas chromatography–mass spectrometry (GC–MS) analysis demonstrated that these compounds significantly reduced the intensity of unpleasant flavor attributes and decreased off-flavor content under high concentration neutral conditions (10 % w/v, pH 7.0) and low concentration acidic conditions (3 % w/v, pH 4.0). Structural differences influenced binding efficacy, with shorter-chain compounds like furaneol outperforming long-chain lactones. These findings provide a novel strategy for off-flavor removal in SPI, supporting the development of consumer-preferred soy products.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.