肌原纤维蛋白(MPs)对基于凝胶的产品的硬度和柔韧性有显著的影响。因此,提高扇贝MP的凝胶化和乳化性能对于生产优质扇贝鱼糜产品具有至关重要的意义。在这项研究中,我们研究了高强度超声对海湾扇贝(Argopectenirrhans)MP的物理化学和凝胶化特性的影响。随着超声功率(150、350和550W)的增加,MPs的羰基含量显着增加,表明超声诱导的MP氧化。同时,高强度超声处理(550W)增强了MPs的乳化能力和短期稳定性(高达72.05m2/g和153.05min,分别)。随着超声波功率的增加,MPs的二硫键含量和表面疏水性显着增加,表明MP的构象变化。此外,在议员的二级结构中,α-螺旋含量显著下降,而β-折叠含量增加,从而表明超声诱导的MP分子的拉伸和柔性。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和扫描电子显微镜分析进一步阐明了高强度超声诱导MP氧化,导致氨基酸侧链的修饰,分子内和分子间交联,和MP聚合。因此,发现高强度超声治疗可以增强粘弹性,凝胶强度,和MP凝胶的保水能力,因为超声处理促进了蛋白质凝胶中稳定网络结构的形成。因此,这项研究为海湾扇贝MPs的功能修饰及其鱼糜产品的加工提供了理论见解。
Myofibrillar proteins (MPs) have a notable impact on the firmness and flexibility of gel-based products. Therefore, enhancing the gelation and emulsification properties of scallop MPs is of paramount significance for producing high-quality scallop surimi products. In this study, we investigated the effects of high-intensity ultrasound on the physicochemical and gelation properties of MPs from bay scallops (Argopecten irradians). The carbonyl content of MPs significantly increased with an increase in ultrasound power (150, 350, and 550 W), indicating ultrasound-induced MP oxidation. Meanwhile, high-intensity ultrasound treatment (550 W) enhanced the emulsifying capacity and the short-term stability of MPs (up to 72.05 m2/g and 153.05 min, respectively). As the ultrasound power increased, the disulfide bond content and surface hydrophobicity of MPs exhibited a notable increase, indicating conformational changes in MPs. Moreover, in the secondary structure of MPs, the α-helix content significantly decreased, whereas the β-sheet content increased, thereby suggesting the ultrasound-induced stretching and flexibility of MP molecules. Sodium-dodecyl sulfate-polyacrylamide gel electrophoresis and scanning electron microscopy analysis further elucidated that high-intensity ultrasound induced MP oxidation, leading to modification of amino acid side chains, intra- and intermolecular cross-linking, and MP aggregation. Consequently, high-intensity ultrasound treatment was found to augment the viscoelasticity, gel strength, and water-holding capacity of MP gels, because ultrasound treatment facilitated the formation of a stable network structure in protein gels. Thus, this study offers theoretical insights into the functional modification of bay scallop MPs and the processing of its surimi products.