文献类型：期刊文献

英文题名：Preparation and Characterization of Tilapia Protein Isolate - Hyaluronic Acid Complexes Using a Ph-Driven Method for Improving the Stability of Tilapia Protein Isolate Emulsion

作者：Xie, Mengya[1,2,3,4]; Zhou, Chunxia[1,2,3,4,5]; Li, Xiang[1,2,3,4]; Ma, Huanta[1,2,3,4]; Liu, Qingguan[1,2,3]; Hong, Pengzhi[1,2,3,4,5]

机构：[1] College ofFoodScience andTechnology, Guangdong Ocean University, Zhanjiang, 524088, China; [2] Guangdong Provincial Key Laboratory of Aquatic Product Processing andSafety, Zhanjiang, 524088, China; [3] Guangdong Provincial Engineering Technology Research Center of Marine Food, Zhanjiang, 524088, China; [4] Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China; [5] Southern Marine Science and Engineering Guangdong Laboratory [Zhanjiang], Guangdong, Zhanjiang, 524088, China

年份：2023

外文期刊名：SSRN

收录：EI(收录号：20240010667)

语种：英文

外文关键词：Complexation - Emulsification - Hydrogen bonds - Hydrophobicity - Organic acids - Proteins - Stability

外文摘要：This study aimed to investigate the non-covalent complexation between hyaluronic acid (HA) and tilapia protein isolate (TPI) on the stability of oil-in-water (O/W) TPI emulsion. The results showed that HA bound to TPI mainly through hydrogen bonding and hydrophobic interactions, forming a homogeneous hydrophilic complex. The binding of HA promoted the structural folding of TPI and altered its secondary structure during pH neutralization, leading to an increase in the emulsification of the protein. Emulsion characterization showed that HA promoted the transfer of TPI to the O/W interface, forming a viscoelastic interfacial membrane structure, which, combined with the high surface charge and strong spatial site resistance effect of HA, improved TPI emulsion stability. Therefore, non-covalent complexation with HA is an effective strategy to improve the stability of TPI emulsion. ? 2023, The Authors. All rights reserved.