Nie Xiaohua, Liu Haizhen, Yu Ningxiang, Tang Qiwen, Wu Congcong, Meng Xianghe
College of Food Science and Technology, Zhejiang University of Technology, Hangzhou, Zhejiang, China.
J Food Sci. 2021 Dec;86(12):5318-5328. doi: 10.1111/1750-3841.15965. Epub 2021 Nov 18.
Fish myofibrillar protein is underutilized due to the formation of insoluble aggregates in low salt media. High pressure homogenization (HPH) at 20, 40, and 60 MPa for four passes was applied on bighead carp myofibrillar protein in order to modify its structure and interfacial properties. Changes in aggregation, conformation, solubility, emulsifying and foaming properties of myofibrillar protein were investigated. The aggregates of myofibrillar protein were obviously disrupted by HPH treatment. The size of myofibrillar protein aggregates became smaller and more uniform as the treating pressure increased, accompanied by notable decreases of cross-sectional height and Rq value in AFM image. Furthermore, the conformation of HPH-treated myofibrillar protein was unfolded into a flexible and open structure. α-helix and β-sheet were converted into β-turn and random coil. Surface hydrophobicity and zeta potential were strengthened, along with the exposure of sulfhydryl groups onto molecule surface. On the other hand, solubility, emulsifying activity index (EAI) and foaming capacity (FC) of HPH-treated myofibrillar protein were markedly enhanced with the increasing pressure. Especially after HPH treatment at 60 MPa, myofibrillar protein was almost dissolved in low salt media (solubility 91.86%) with 4.92 fold for EAI and 3.52 fold for FC. But there was little variation in emulsifying and foaming stabilities. These results suggested that HPH treatment has interesting potential to induce the dissociation and unfolding of myofibrillar protein in low salt media, therefore improving its interfacial properties. PRACTICAL APPLICATION: Carp myofibrillar protein was treated by high pressure homogenization (HPH). Aggregates of myofibrillar protein were disrupted into smaller size form. Conformation of myofibrillar protein was unfolded into open and loose structure. Emulsifying and foaming capacities of myofibrillar protein were improved. HPH treatment modified the structure and interfacial properties of myofibrillar protein.
由于在低盐介质中会形成不溶性聚集体，鱼肉肌原纤维蛋白未得到充分利用。对鳙鱼肌原纤维蛋白施加20、40和60兆帕的高压均质处理4次，以改变其结构和界面性质。研究了肌原纤维蛋白在聚集、构象、溶解性、乳化和发泡性能方面的变化。高压均质处理明显破坏了肌原纤维蛋白的聚集体。随着处理压力的增加，肌原纤维蛋白聚集体的尺寸变得更小且更均匀，同时原子力显微镜图像中的横截面高度和Rq值显著降低。此外，经高压均质处理的肌原纤维蛋白的构象展开为灵活且开放的结构。α-螺旋和β-折叠转变为β-转角和无规卷曲。表面疏水性和zeta电位增强，同时巯基暴露于分子表面。另一方面，经高压均质处理的肌原纤维蛋白的溶解度、乳化活性指数（EAI）和发泡能力（FC）随着压力的增加而显著提高。特别是在60兆帕的高压均质处理后，肌原纤维蛋白几乎可溶解于低盐介质中（溶解度为91.86%），EAI提高了4.92倍，FC提高了3.52倍。但乳化和发泡稳定性变化不大。这些结果表明，高压均质处理在诱导低盐介质中肌原纤维蛋白的解离和展开方面具有潜在价值，从而改善其界面性质。实际应用：对鲤鱼肌原纤维蛋白进行高压均质处理。肌原纤维蛋白聚集体被分解成更小的尺寸形式。肌原纤维蛋白的构象展开为开放且松散的结构。肌原纤维蛋白的乳化和发泡能力得到改善。高压均质处理改变了肌原纤维蛋白的结构和界面性质。
