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Article

Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

by 1,2,3,4, 1,2,3,4,5, 1,2,3,4, 1,2,3,4,5,*, 1,2,3,4 and 1,2,3,4
1
College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
2
Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, 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), Zhanjiang 524088, China
*
Author to whom correspondence should be addressed.
Molecules 2019, 24(23), 4337; https://doi.org/10.3390/molecules24234337
Received: 23 October 2019 / Revised: 16 November 2019 / Accepted: 26 November 2019 / Published: 27 November 2019
(This article belongs to the Collection Advances in Food Analysis)
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 α-helix and β-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 α-helix and β-sheet were −0.964 (p <0.01) and 0.743, respectively. TSPCs displayed lower α-helix contents and higher β-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. View Full-Text
Keywords: tilapia; soybean; protein co-precipitates; protein secondary structure; water solubility; correlation coefficients tilapia; soybean; protein co-precipitates; protein secondary structure; water solubility; correlation coefficients
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MDPI and ACS Style

Tan, L.; Hong, P.; Yang, P.; Zhou, C.; Xiao, D.; Zhong, T. Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates. Molecules 2019, 24, 4337. https://doi.org/10.3390/molecules24234337

AMA Style

Tan L, Hong P, Yang P, Zhou C, Xiao D, Zhong T. Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates. Molecules. 2019; 24(23):4337. https://doi.org/10.3390/molecules24234337

Chicago/Turabian Style

Tan, Li, Pengzhi Hong, Ping Yang, Chunxia Zhou, Dinghao Xiao, and Tanjun Zhong. 2019. "Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates" Molecules 24, no. 23: 4337. https://doi.org/10.3390/molecules24234337

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