College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, Guangdong, China.
J Agric Food Chem. 2011 Aug 24;59(16):8886-94. doi: 10.1021/jf201781z. Epub 2011 Jul 22.
Peanut protein isolate (PPI) was treated by high-pressure microfluidization (40, 80, 120, and 160 MPa) and/or transglutaminase (TGase) cross-linking. It was found that individual microfluidization at 120 MPa was more effective in improving the solubility, emulsifying properties, and surface hydrophobicity of PPI than at other pressures (e.g., 40, 80, or 160 MPa). Individual TGase cross-linking also effectively changed the physicochemical and functional properties of PPI. Microfluidization (120 MPa) or TGase cross-linking caused the unfolding of PPI structure, resulting in the decrease of α-helix and β-turns levels and the increase of β-sheet and random coil levels, as proved by Fourier transform infrared (FTIR) and circular dichroism (CD) spectra. Compared with individual treatments, microfluidization followed by TGase cross-linking significantly (p < 0.05) improved the emulsion stability during long-term storage (20 days). Moreover, the combined treatments led to looser structure of PPI and resulted in more obvious changes in physicochemical properties.
花生蛋白分离物（PPI）经高压微射流（40、80、120 和 160 MPa）和/或转谷氨酰胺酶（TGase）交联处理。结果发现，与其他压力（例如 40、80 或 160 MPa）相比，120 MPa 的单独微射流更有效地提高了 PPI 的溶解度、乳化性能和表面疏水性。单独的 TGase 交联也有效地改变了 PPI 的物理化学和功能特性。微射流（120 MPa）或 TGase 交联导致 PPI 结构展开，从而导致 α-螺旋和 β-转角水平降低，β-折叠和无规卷曲水平升高，这一点通过傅里叶变换红外（FTIR）和圆二色性（CD）光谱得到证实。与单独处理相比，微射流后 TGase 交联显著（p < 0.05）提高了长期储存（20 天）期间乳液的稳定性。此外，联合处理导致 PPI 结构更加疏松，导致其物理化学性质发生更明显的变化。
