文献类型：期刊文献

英文题名：pH-induced interface protein structure changes to adjust the stability of tilapia protein isolate emulsion prepared by high-pressure homogenization

作者：Liu, Qingguan[1];Chen, Ailin[1];Hong, Pengzhi[1];Zhou, Chunxia[1];Li, Xiang[1];Xie, Mengya[1]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China

年份：2024

卷号：24

外文期刊名：FOOD CHEMISTRY-X

收录：SCI-EXPANDED(收录号：WOS:001322566000001)、、EI(收录号：20243917088462)、Scopus(收录号：2-s2.0-85204484587)、WOS

基金：This work was supported by the Zhanjiang Science and Technology Program Project (2022A05037) , and Guangdong Modern Agricultural Industrial Technology System Innovation Team Building Project (2023KJ150) .

语种：英文

外文关键词：Tilapia protein isolate; pH; Secondary structure; Emulsion stability; Correlation analysis

外文摘要：The pH is a crucial external factor affecting the structure and emulsification characteristics of proteins. The current study aimed to reveal the correlation between the secondary structure changes and tilapia protein isolate (TPI) emulsion stability under different pH (3.0-10.0) prepared by high-pressure homogenization. The results showed that TPI with significantly increased solubility and emulsifying properties when the pH keep away from the isoelectric point (pH 5.0). Meanwhile, TPI emulsions presented significantly enhanced stability (with decreased particle size, increased zeta potential, creaming index close to 0, and uniform dispersion of droplets) at pH 3.0 and 10.0. Interface-adsorbed protein mainly consists of a myosin-heavy chain and actin, and the secondary structure was significantly influenced by pH and high-pressure homogenization. The alpha-helix will be transformed into beta-sheet and beta-turn when pH is closer to pH 5.0. However, the high-pressure homogenization induced alpha-helix conversion to beta-sheet. The correlation analysis revealed that emulsion stability is positively correlated with alpha-helix and negatively correlated with beta-sheet. This work provides a deep insight into the correlation between secondary structure changes and the stability of TPI emulsion as affected by pH to offer an alternative way to enhance TPI emulsion stability.