转谷氨酰胺酶对鲤鱼肌原纤维蛋白乳化活性和凝胶特性的影响

Effect of Transglutaminase on the Emulsifying Activity Index and Gel Properties of Common Carp Myofibrillar Protein

目的:研究添加转谷氨酰胺酶(Transglutaminase,TG)对鲤鱼肌原纤维蛋白乳化活性和凝胶特性的影响,为改善鱼糜制品的品质特性提供理论依据。方法:肌原纤维蛋白溶液浓度为40 mg/mL,TG添加量为蛋白溶液的0%、0.1%、0.2%、0.3%、0.4%(W/V),测定蛋白溶液的乳化活性及凝胶特性指标。结果:随着TG添加量的增加肌原纤维蛋白溶液乳化活性降低(p <0.05); TG添加增大了蛋白浊度(p <0.05);蛋白流变结果表明,随着TG添加量的增加显著增大储能模量(G')(p <0.05),降低起始凝胶温度,并提高蛋白变性温度;与对照相比,添加0.1%的TG会降低凝胶持水性,但是进一步增加TG对凝胶持水性影响不显著(p> 0.05);添加TG显著降低了凝胶白度(p <0.05);凝胶质构测定结果显示,随着TG添加量的增加,会改进蛋白质的凝胶特性,显著增加凝胶弹性和硬度(p <0.05)。结论:肌原纤维蛋白中添加TG到能够降低蛋白的乳化特性,但会改进肌原纤维蛋白的凝胶特性。

Objective: The aim of this study was to investigate the impact of transglutaminase (TG) on the emulsifying properties and heat-induced gelation properties of myofibrillar proteins from common carp so as to provide theoretical basis for improvement the quality characteristics of surimi products. Methods: Myofibrillar proteins suspensions (final protein concentration of 40 mg/mL) were prepared.TG were added to the suspensions to obtain final concentrations of 0,0.1%,0.2%,0.3%,and 0.4%(w/v) after mixing,emulsification activity and gel property index of the protein solution were measured.Results: Emulsifying activity decreased (p < 0.05) as TG concentration increased,however turbidity greatly increased (p < 0.05)when TG was added.The results of protein rheological properties suggested that the TG increased the storage modulus (G’)(p <0.05),decreased initial gel temperature and increased the protein denaturation temperature.Compared to control,the gel water holding capacity first decreased (p < 0.05) when TG concentrations at 0.1% and then had no significant difference with increased TG concentrations.TG addition significantly decreased the gel whiteness (p < 0.05).Gel texture results showed that gel quality was greatly improved (p < 0.05) with the TG addition.As the TG levels increased,gel hardness and springiness increased significantly (p < 0.05). Conclusion: TG addition decreased emulsifying ability and improved the Gel properties of myofibrillar protein.