文献类型：期刊文献

英文题名：Formation of hydrophilic co-assemblies with improved functional properties between tilapia protein isolate and sodium caseinate

作者：Li, Xiang[1,2,3,4];Hong, Pengzhi[1,2,3,4,5];Xie, Mengya[1,2,3,4];Wang, Yu[6];Liu, Qingguan[1,2,3,4];Zhou, Chunxia[1,2,3,4,5]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[2]Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China;[3]Guangdong Prov Engn Technol Res Ctr Marine Food, Zhanjiang 524088, Peoples R China;[4]Guangdong Prov Modern Agr Sci & Technol Innovat Ct, Zhanjiang 524088, Peoples R China;[5]Southern Marine Sci & Engn Guangdong Lab Zhanjiang, Zhanjiang 524088, Guangdong, Peoples R China;[6]Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Peoples R China

年份：2024

卷号：153

外文期刊名：FOOD HYDROCOLLOIDS

收录：SCI-EXPANDED(收录号：WOS:001219315800001)、、EI(收录号：20241415833503)、Scopus(收录号：2-s2.0-85188881221)、WOS

基金：This work was supported by the Guangdong Modern Agricultural Industrial Technology System Innovation Team Building Project (2023KJ150) , Zhanjiang Science and Technology Program Project (2022A05037) , and Scientific research start-up funds of Guangdong Ocean University (060302042317) .

语种：英文

外文关键词：Tilapia protein isolate; Sodium caseinate; Co-assemblies; Component interactions; Functional properties

外文摘要：Functional enhancement of aquatic proteins still faces great challenges, resulting in their highly under-utilized applications in the field of intensive food processing. In this study, the tilapia protein isolate-sodium caseinate co-assemblies were prepared using a pH cycle strategy. The aggregation properties, component interactions, and functional properties of the formed co-assemblies were investigated. Results of particle size, zeta potential, surface hydrophobicity, and SEM indicated that tilapia protein isolates and sodium caseinate generated coassemblies with reduced aggregation properties. Component interactions revealed that sodium caseinate binds to tilapia protein isolate mainly through hydrogen bonding and hydrophobic interactions, which inhibits the refolding of tilapia protein isolate to form more structurally ordered hydrophilic co-assemblies. Functional properties studies showed that co-assemblies with improved water solubility (reached 77.08%) and emulsification properties compared to tilapia protein isolated when the mass ratio of tilapia protein isolated to sodium caseinate was T/N = 1:1. In this experiment, the functional properties of tilapia protein isolate were enhanced by a simple, green, and efficient method, which is expected to be applied in the food industry.