The interaction of flavors in food pairings has long been a focal point in food science and sensory research.Particularly in complex food pairings such as wine and seafood,the interplay of flavor compounds can lead to...The interaction of flavors in food pairings has long been a focal point in food science and sensory research.Particularly in complex food pairings such as wine and seafood,the interplay of flavor compounds can lead to enhanced or altered sensory experiences.However,the molecular mechanisms underlying these interactions remain insufficiently elucidated.Therefore,this study aims to investigate the molecular mechanisms behind food pairings,focusing on the impact of pyrazine-based aroma compounds in Sauvignon Blanc wine on the perception of key umami substances in oysters,including glutamic acid(Glu),5′-inosinic acid(IMP),and the umami peptide Phe-Asn-Lys-Glu-Glu(FNKEE),using an electronic tongue,molecular docking,molecular dynamics simulations,and sensory evaluations.The results demonstrate that 3-sec-butyl-2-methoxypyrazine(SBMP),3-isopropyl-2-methoxypyrazine(IPMP),3-isobutyl-2-methoxypyrazine(IBMP),and 3-ethyl-2-methoxypyrazine(EMP)significantly enhanced umami perception through cross-modal interactions.Molecular docking and dynamics simulations revealed that pyrazines reduced the binding free energy between umami ligands and T1R1/T1R3 receptors via hydrogen bonding and hydrophobic interactions.Moreover,the reduction in binding energy correlated with the bulkiness and topological complexity of the substituent at the 3-position of the pyrazine ring,following the trend:SBMP>IPMP>IBMP>EMP.This study provides a preliminary molecular-level explanation for the flavor interaction mechanism between Sauvignon Blanc wine and oysters,offering a scientific rationale for this classic pairing.展开更多
In order to clarify the modulation of microwave and conduction heating on the aroma release and adsorption of meat,the effect of different myofibrillar proteins(MP)on the release ability of pyrazines(2-methylpyrazine,...In order to clarify the modulation of microwave and conduction heating on the aroma release and adsorption of meat,the effect of different myofibrillar proteins(MP)on the release ability of pyrazines(2-methylpyrazine,2,5-dimethylpyrazine,and 2,3,5-trimethylpyrazine)was investigated.The adsorption ability,hydrophobicity of MP,and thermodynamic parameters were analyzed.Conduction heating by water bath exhibited stronger adsorption ability of MP for 2-methylpyrazine(17.17±2.27%)than that of microwave,followed by 2,3,5-trimethylpyrazine(11.50±0.91%)and 2,5-dimethylpyrazine(8.63±5.24%),which accounted for the structures of pyrazines.Water bath heating promoted protein unfolding leading to increased exposure of hydrophobic regions thereby enhancing binding affinity with pyrazine flavor compounds.Furthermore,fluorescence quenching ability was enhanced with increasing substituents on pyrazine flavor compounds.The hydrophobic interaction between 2,5-dimethylpyrazine and MP was dominant in both heat treatments.The interactions of conduction-heated MP with 2-methylpyrazine and 2,3,5-trimethylpyrazine predominantly involved hydrophobic forces,whereas interactions with microwave-heated proteins were primarily driven by van der Waals forces and hydrogen bonding effects.The results obtained from this study provide valuable theoretical insights into understanding the differences in the flavor release of meat product resulting from microwave versus water bath heating.展开更多
基金supported by the National Natural Science Foundation of China[grant number 32160609]the Scientific Research Projects Undertaken by Higher Education Institutions in Gansu Province[grant number 2026CYZC-040]+3 种基金the Longyuan Young Talents Program of Gansu Province[grant number LYYC-2024-03]the Gansu Province Leading Talent Project[grant number LJRC-2024]the Gansu Province Wine Industry Development Special Fund Project[grant number GSPTJZX-2020-4]the Gansu Province Modern Cold and Arid Specialty Agricultural Fruit Industry Technology System Project[grant number GSARS-04-08].
文摘The interaction of flavors in food pairings has long been a focal point in food science and sensory research.Particularly in complex food pairings such as wine and seafood,the interplay of flavor compounds can lead to enhanced or altered sensory experiences.However,the molecular mechanisms underlying these interactions remain insufficiently elucidated.Therefore,this study aims to investigate the molecular mechanisms behind food pairings,focusing on the impact of pyrazine-based aroma compounds in Sauvignon Blanc wine on the perception of key umami substances in oysters,including glutamic acid(Glu),5′-inosinic acid(IMP),and the umami peptide Phe-Asn-Lys-Glu-Glu(FNKEE),using an electronic tongue,molecular docking,molecular dynamics simulations,and sensory evaluations.The results demonstrate that 3-sec-butyl-2-methoxypyrazine(SBMP),3-isopropyl-2-methoxypyrazine(IPMP),3-isobutyl-2-methoxypyrazine(IBMP),and 3-ethyl-2-methoxypyrazine(EMP)significantly enhanced umami perception through cross-modal interactions.Molecular docking and dynamics simulations revealed that pyrazines reduced the binding free energy between umami ligands and T1R1/T1R3 receptors via hydrogen bonding and hydrophobic interactions.Moreover,the reduction in binding energy correlated with the bulkiness and topological complexity of the substituent at the 3-position of the pyrazine ring,following the trend:SBMP>IPMP>IBMP>EMP.This study provides a preliminary molecular-level explanation for the flavor interaction mechanism between Sauvignon Blanc wine and oysters,offering a scientific rationale for this classic pairing.
基金support of National Key R&D Program of China(2021YED2100103)program of“Collaborative innovation center of food safety and quality control in Jiangsu Province”.
文摘In order to clarify the modulation of microwave and conduction heating on the aroma release and adsorption of meat,the effect of different myofibrillar proteins(MP)on the release ability of pyrazines(2-methylpyrazine,2,5-dimethylpyrazine,and 2,3,5-trimethylpyrazine)was investigated.The adsorption ability,hydrophobicity of MP,and thermodynamic parameters were analyzed.Conduction heating by water bath exhibited stronger adsorption ability of MP for 2-methylpyrazine(17.17±2.27%)than that of microwave,followed by 2,3,5-trimethylpyrazine(11.50±0.91%)and 2,5-dimethylpyrazine(8.63±5.24%),which accounted for the structures of pyrazines.Water bath heating promoted protein unfolding leading to increased exposure of hydrophobic regions thereby enhancing binding affinity with pyrazine flavor compounds.Furthermore,fluorescence quenching ability was enhanced with increasing substituents on pyrazine flavor compounds.The hydrophobic interaction between 2,5-dimethylpyrazine and MP was dominant in both heat treatments.The interactions of conduction-heated MP with 2-methylpyrazine and 2,3,5-trimethylpyrazine predominantly involved hydrophobic forces,whereas interactions with microwave-heated proteins were primarily driven by van der Waals forces and hydrogen bonding effects.The results obtained from this study provide valuable theoretical insights into understanding the differences in the flavor release of meat product resulting from microwave versus water bath heating.
