Department of Food Science and Biotechnology, Kyung Hee University, Yongin 17104, Republic of Korea; Research Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of Korea.
Research Group of Food Processing, Korea Food Research Institute, Wanju 55365, Republic of Korea; Division of Animal and Dairy Science, Chungnam National University, Daejeon 34134, Republic of Korea.
Meat Sci. 2023 Feb;196:109032. doi: 10.1016/j.meatsci.2022.109032. Epub 2022 Nov 9.
Here, we investigated the effects of high-pressure homogenization (HPH) on the physicochemical, rheological, and emulsifying properties of myofibrillar proteins (MFPs). The mean particle size of MFPs treated by HPH with different pressures (0-150 MPa) decreased from 886.0 ± 120.2 nm to 172.6 ± 13.7 nm with increasing HPH pressure. In addition, more uniform and homogeneous protein particles were obtained as the HPH pressure was increased. In SDS-PAGE, the band intensities of high molecular weight proteins (200 kDa) decreased and the intensities of some of the smaller molecular fractions (70-120 kDa) increased when the MFPs were subjected to HPH treatment at more than 60 MPa owing to the fragmentation of high molecular weight proteins, such as myosin heavy chains. The surface hydrophobicity of MFPs increased with increasing HPH pressure owing to the exposure of buried hydrophobic groups by protein unfolding. In the rheological study, the MFP dispersions exhibited shear thinning fluid behavior, but the MFP dispersion homogenized at high pressure (120-150 MPa) presented close to Newtonian fluid behavior with low viscosity. The emulsifying activity (EA) and emulsion stability index (ESI) of MFPs improved with increasing HPH pressures. The MFPs treated with HPH at different pressures were used for o/w emulsion preparation, and their dispersion stabilities were investigated during storage. The emulsion systems stabilized with MFPs pressurized at more than 60 MPa showed comparatively less cream formation in the top layer, indicating high dispersion stability.
在这里，我们研究了高压均质（HPH）对肌原纤维蛋白（MFPs）的理化性质、流变学和乳化性能的影响。用不同压力（0-150 MPa）处理的 MFPs 的平均粒径从 886.0 ± 120.2nm 减小到 172.6 ± 13.7nm，随着 HPH 压力的增加。此外，随着 HPH 压力的增加，获得了更均匀和均匀的蛋白质颗粒。在 SDS-PAGE 中，当 MFPs 受到超过 60MPa 的 HPH 处理时，由于高分子量蛋白质（肌球蛋白重链）的断裂，高分子量蛋白质（200kDa）的带强度降低，而一些较小分子分数（70-120kDa）的强度增加。由于蛋白质展开，MFPs 的表面疏水性随着 HPH 压力的增加而增加。在流变学研究中，MFPs 分散体表现出剪切稀化流体行为，但在高压（120-150MPa）下均匀化的 MFP 分散体具有接近牛顿流体行为，其粘度较低。MFPs 的乳化活性（EA）和乳化稳定性指数（ESI）随着 HPH 压力的增加而提高。用不同压力的 HPH 处理的 MFPs 用于制备 o/w 乳液，并在储存期间研究其分散体稳定性。用压力高于 60MPa 的 MFPs 稳定的乳液体系在上层形成的奶油层相对较少，表明分散体稳定性较高。
