文献类型：期刊文献

英文题名：Preparation, Structural Characterization, and Functional Properties of a Tilapia-Soybean Double Protein System: Effects of Different Complexation Modes

作者：Qin, Xinyi[1]; Hong, Pengzhi[1]; Zhao, Liangyu[1]; Xie, Mengya[1]; Zhou, Chunxia[1]; Liu, Qingguan[1]

机构：[1] College of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Marine Food, Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China

年份：2024

外文期刊名：SSRN

收录：EI(收录号：20240455306)

语种：英文

外文关键词：Explosive bonding

外文摘要：Different assembly methods may influence the structure and function of the double protein system differently.The objective of this study is to investigate the effects of complexation and co-precipitation of TPI and soybean protein isolate (SPI) on the structure and functional properties of the tilapia-soybean double protein system. The structural analysis showed that in the two assembly methods, TPI was mainly connected to SPI by non-covalent forces and disulfide bonds, resulting in structural changes. Compared to the tilapia-soy protein co-precipitate (T-SPCP), tilapia- soybean protein complexes (T-SPC) exhibit a more compact and hydrophilic structure, characterized by increased disulfide bonds, α-helices, and ζ-potential, along with reduced surface hydrophobicity and smaller flake structures. Functional property analysis shows that both processing methods significantly enhance TPI's solubility, emulsifying activity, foaming capacity, and thermal stability. T-SPC demonstrates higher solubility, emulsifying activity, and foaming capacity than T-SPCP; however, T-SPCP exhibits superior thermal stability compared to T-SPC. ? 2024, The Authors. All rights reserved.