Effects of temperature on the denaturation and aggregation of (Lateolabrax japonicus) myosin from sea bass surimi

文献类型： 外文期刊

第一作者： Liu, Fangfang

作者： Liu, Fangfang;Huang, Hui;Lin, Wanling;Li, Laihao;Wu, Yanyan;Yang, Shaoling;Yang, Xianqing;Wang, Yueqi;Liu, Fangfang;Lin, Wanling

作者机构：

期刊名称：JOURNAL OF FOOD PROCESSING AND PRESERVATION （ 影响因子：1.405； 五年影响因子：1.517 ）

ISSN： 0145-8892

年卷期： 2021 年 45 卷 5 期

页码：

收录情况： SCI

摘要： This study aimed to investigate the effects of temperatures of 30-90 degrees C on myosin denaturation and aggregation in sea bass (Lateolabrax japonicus) during setting. The result indicated that the myosin of sea bass began to form gels at 60 degrees C, and surface hydrophobicity increased by around 8.9% at 40 degrees C and reached its maximun at 60 degrees C. During setting at 40 degrees C and 60 degrees C, the ratios of alpha-helix of myosin reduced gradually and finally decreasing by 17.1% and 25.2%, respectively. Incubating at 90 degrees C, alpha-helix continued to transform into random coil. Association with the results of surface morphology, it further confirmed that the temperatures of 40 degrees C and 60 degrees C were two important denaturation and aggregation temperatures. At 90 degrees C, myosin of sea bass formed a fine and dense gel network under the joint action of nondisulfide covalent bond, disulfide bond and hydrophobic interaction. Practical applications The raw materials for marine surimi are becoming scarcer with marine overfishing and the increasing demand for surimi. Sea bass, an important economic mariculture fish in China, has white meat and less bone spur and is advantageous for the development of surimi products as raw materials. During heating of surimi, the change of myosin structure is a main important key to forming a gel network. This research revealed the changes of sea bass myosin from denaturation, aggregation to gel formation during heating and provided a theoretical basis for the processing of sea bass surimi.

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