风味
吡嗪
化学
吸附
微波食品加热
肌原纤维
食品科学
热传导
生物化学
有机化学
材料科学
电信
复合材料
计算机科学
作者
Yucen Chen,Xinshuo Wang,Yahui Gao,Caleb John Swing,Jingyang Yu,Heping Cui,Shuqin Xia
标识
DOI:10.1016/j.fbio.2024.104127
摘要
In order to clarify the modulation of microwave and conduction heating on the aroma perception of meat, the effect of different myofibrillar proteins (MP) on the adsorption 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 aroma perception of meat product resulting from microwave versus water bath heating.
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