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Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop (Argopecten irradians)
Ultrasonics Sonochemistry ( IF 8.7 ) Pub Date : 2024-05-31 , DOI: 10.1016/j.ultsonch.2024.106935
Bing Liu , Yuan Wu , Qiu-yan Liang , Hong Zheng

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 (). 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 m/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.

中文翻译:


高强度超声波对海湾扇贝(Argopecten irradians)肌原纤维蛋白理化和凝胶特性的影响



肌原纤维蛋白 (MP) 对凝胶产品的硬度和柔韧性具有显着影响。因此,提高扇贝MP的凝胶和乳化性能对于生产高品质的扇贝鱼糜产品具有重要意义。在这项研究中,我们研究了高强度超声波对海湾扇贝 MP 的理化和凝胶特性的影响 ()。随着超声波功率(150、350 和 550 W)的增加,MP 的羰基含量显着增加,表明超声波诱导 MP 氧化。同时,高强度超声处理(550 W)增强了 MP 的乳化能力和短期稳定性(分别高达 72.05 m/g 和 153.05 min)。随着超声功率的增加,MPs的二硫键含量和表面疏水性显着增加,表明MPs的构象发生了变化。此外,在MPs的二级结构中,α-螺旋含量显着减少,而β-折叠含量增加,从而表明超声诱导MP分子的拉伸和柔韧性。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和扫描电镜分析进一步阐明,高强度超声诱导MP氧化,导致氨基酸侧链修饰、分子内和分子间交联以及MP聚集。因此,我们发现高强度超声处理可以增强 MP 凝胶的粘弹性、凝胶强度和保水能力,因为超声处理有利于蛋白质凝胶中稳定网络结构的形成。因此,本研究为海湾扇贝 MP 的功能修饰及其鱼糜产品的加工提供了理论见解。
更新日期:2024-05-31
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