Abstract：
Interactions among flavor compounds from spices (FCS) and myofibrillar proteins (MP) were investigated. Fluorescence and Fourier transform infrared spectroscopy showed that hydrogen bonding and hydrophobic interactions were the main binding forces between FCS and MP. The FCS increased the particle size and SH content of MP and caused a reduction of zeta potential from -5.23 to -6.50 mV. Furthermore, FCS could modify the binding ability of MP and aldehydes. Eugenol reduced the ability of MP to bond with aldehydes by 22.70-47.87 %. Molecular dynamics simulations demonstrated that eugenol may combat nonanal to attain binding site of amino acid residue (PHE165) and induce protein conformational changes. Electrostatic interactions and van der Waals forces within myosin-nonanal may be disrupted by these alterations, which could reduce stability of complex and cause release of nonanal. This study could provide new insights into regulating the ability of proteins to release and hold flavors.
摘要：
研究了香料（FCS）和肌原纤维蛋白（MP）的风味化合物之间的相互作用。荧光和傅里叶变换红外光谱表明，氢键和疏水相互作用是FCS与MP之间的主要结合力。FCS增加了MP的粒径和SH含量，并导致ζ电位从-5.23降至-6.50mV。此外，FCS可以改变MP与醛的结合能力。丁香酚使MP与醛的键合能力降低22.70-47.87％。分子动力学模拟表明，丁香酚可以对抗nonanal获得氨基酸残基（PHE165）的结合位点并诱导蛋白质构象变化。肌球蛋白-nonanal内的静电相互作用和范德华力可能会被这些改变所破坏，这会降低复合物的稳定性并导致非肛门释放。这项研究可以为调节蛋白质释放和保持风味的能力提供新的见解。
