Abstract：
Dried-bonito (Katsuobushi) exhibits a unique uniform \"glass-like\" texture after traditional smoke-drying. Herein, we developed a novel processing method for dried-bonito and elucidated the mechanism of transformation of loose muscle into a \"glass-like\" texture in terms of texture, microstructure, and protein properties. Our findings showed that the unfolding and aggregation of proteins after thermal induction was a key factor in shaping the \"glass-like\" texture in bonito muscle. During processing, myofibrils aggregated, the originally alternating thick and thin filaments contracted laterally and aligned into a straight line, and protein cross-linking increased. Secondary structural analysis revealed a reduction in unstable β-turn content from 26.28% to 15.06%. Additionally, an increase in the content of SS bonds was observed, and the conformation changed from g-g-t to a stable g-g-g conformation, enhanced protein conformational stability. Taken together, our findings provide a theoretical basis for understanding the mechanism of formation of the uniform \"glass-like\" texture in dried-bonito.
摘要：
干bonito（Katsuobushi）在传统的烟雾干燥后表现出独特的均匀“玻璃状”质地。在这里，我们开发了一种新的处理方法，用于干bonito，并阐明了在纹理方面将松弛肌肉转化为“玻璃样”纹理的机制，微观结构，和蛋白质特性。我们的发现表明，热诱导后蛋白质的展开和聚集是塑造骨骼肌肉“玻璃样”质地的关键因素。在处理过程中,肌原纤维聚集，最初交替的粗细细丝横向收缩并排成一条直线，和蛋白质交联增加。二级结构分析显示，不稳定的β转角含量从26.28％降低到15.06％。此外,观察到SS键的含量增加，构象从g-g-t变为稳定的g-g-g构象，增强蛋白质构象稳定性。一起来看,我们的研究结果为理解干bonito中均匀的“玻璃样”纹理的形成机理提供了理论基础。
