冻融与冻藏对乌鳢肌原纤维蛋白与酸菜鱼汤中特征风味物质结合特性的影响

Effects of Freeze-Thaw Treatment and Freeze Storage on the Binding Characteristics of Snakehead Myofibrillar Protein to Characteristic Flavor Substances in Fish Soup with Pickled Mustard Greens

为探究冷冻处理对于鱼片与酸菜鱼汤中风味物质的结合特性影响,以乌鳢的肌原纤维蛋白为对象,研究冻融及冻藏处理对其理化特性及与己醛、辛醛、芳樟醇、月桂烯结合能力的变化。结果表明经过7 d贮藏后,冻融组肌原纤维蛋白溶解度降低了约26%,相较于冻藏组,蛋白质氧化和三级结构变化程度更高,产生了更多可溶性聚集体;冻藏组溶解度降低了约33%,相较于冻融组,溶解度降低更加显著(P<0.05),产生了更多不溶性聚集体。影响肌原纤维蛋白冷冻聚集的主要作用力是非共价键。分子对接结果表明,芳樟醇、己醛和辛醛通过疏水作用和氢键与蛋白质结合,月桂烯与蛋白结合的主要驱动力为疏水相互作用。冷冻处理通过减少蛋白质与醛类化合物结合的巯基基团和氢键,降低了对己醛和辛醛的结合能力,蛋白质表面疏水性的提高,增加了对月桂烯和芳樟醇的结合能力,冻融处理后蛋白质对于月桂烯的结合能力强于冻藏处理组。研究结果可以为冷冻酸菜鱼预制品的风味控制提供理论依据和参考。

The purpose of this study was to explore the effect of freeze treatment on the binding characteristics of fillets to flavor substances in fish soup with pickled mustard greens.The study focused on the effects of freeze-thaw treatment and freeze storage on the physicochemical properties of snakehead myofibrillar protein and its binding characteristics to hexanal,octanal,linalool and myrcene.The results showed that after 7 days of storage,the solubility of myofibrillar protein decreased by about 26%in the freeze-thaw group.Compared with the freeze storage group,the oxidation degree and tertiary structural changes of myofibrillar protein were higher and more soluble aggregates were formed in the freeze-thaw group.The solubility of myofibrillar protein decreased by about 33%in the freeze storage group,which showed a more significant decrease compared to the freeze-thaw treatment(P<0.05),resulting in more insoluble aggregates.The major force for the aggregation of myofibrillar proteins after freezing was non-covalent bonding.Molecular docking results indicated that linalool,hexanal and octanal could bind to myofibrillar proteins through hydrophobic interactions and hydrogen bonds,while the major driving force for the binding of myrcene to myofibrillar proteins was hydrophobic interaction.Freeze treatment reduced the binding capacity of hexanal and octanal to sulfhydryl groups in myofibrillar proteins through hydrogen bonds,improved the surface hydrophobicity of myofibrillar proteins,but increased the binding ability of myrcene and linalool to myofibrillar proteins.Freeze-thaw treatment increased the binding capacity of myofibrillar proteins to myrcene compared with freeze storage treatment.The results of this research provide a theoretical basis and reference for flavor control of frozen prepared fish soup with pickled mustard greens.