文献类型：期刊文献

英文题名：Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

作者：Tan, Li[1,2,3,4];Hong, Pengzhi[1,2,3,4,5];Yang, Ping[1,2,3,4];Zhou, Chunxia[1,2,3,4,5];Xiao, Dinghao[1,2,3,4];Zhong, Tanjun[1,2,3,4]

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 C, Zhanjiang 524088, Peoples R China;[5]Southern Marine Sci & Engn Guangdong Lab Zhanjian, Zhanjiang 524088, Peoples R China

年份：2019

卷号：24

期号：23

外文期刊名：MOLECULES

收录：SCI-EXPANDED(收录号：WOS:000507294400136)、、Scopus(收录号：2-s2.0-85075779170)、WOS

基金：This research was funded by the Science and Technology Planning Project of Guangdong Province (2015A020209168, 2017A020208067), Innovation and Development Project about Marine Economy Demonstration of Zhanjiang City (2017C8B1), Southern Marine Science and Engineering Guangdong Laboratory (Zhanjiang) (ZJW-2019-07).

语种：英文

外文关键词：tilapia; soybean; protein co-precipitates; protein secondary structure; water solubility; correlation coefficients

外文摘要：The secondary structure of a protein has been identified to be a crucial indicator that governs its water solubility. Tilapia protein isolate (TPI), soybean protein isolate (SPI), and tilapia-soybean protein co-precipitates (TSPC3:1, TSPC2:1, TSPC1:1, TSPC1:2, and TSPC1:3) were prepared by mixing tilapia meat and soybean meal at different mass ratios. The results demonstrated that the water solubility of TSPCs was significantly greater than that of TPI (p < 0.05). The changes in ultraviolet-visible and near-ultraviolet circular dichroism spectra indicated that the local structure of TSPCs was different from that of TPI and SPI. Fourier transform infrared Spectroscopy revealed the co-existence of TPI and SPI structures in TSPCs. The secondary structures of TSPCs were predominantly alpha-helix and beta-sheet. TSPC1:1 was unique compared to the other TSPCs. In addition, there was a good correlation between the water solubility and secondary structure of TSPCs, in which the correlation coefficients of alpha-helix and beta-sheet were -0.964 (p < 0.01) and 0.743, respectively. TSPCs displayed lower alpha-helix contents and higher beta-sheet contents compared to TPI, which resulted in a significant increase in their water solubility. Our findings could provide insight into the structure-function relationship of food proteins, thus creating more opportunities to develop innovative applications for mixed proteins.