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

Molecules ◽  
2019 ◽  
Vol 24 (23) ◽  
pp. 4337 ◽  
Author(s):  
Li Tan ◽  
Pengzhi Hong ◽  
Ping Yang ◽  
Chunxia Zhou ◽  
Dinghao Xiao ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Water Solubility ◽  
Soybean Protein ◽  
Correlation Coefficients ◽  
Protein Isolate ◽  
Soybean Protein Isolate ◽  
Near Ultraviolet ◽  
Function Relationship ◽  
Α Helix ◽  
Β Sheet

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.

Drying Temperature Affect Secondary Structure of Soybean Protein-Isolate/Carboxymethyl Cellulose/Stearic Acid Composite Films

2015 ◽  
Vol 1092-1093 ◽  
pp. 1525-1528
Author(s):  
Chao Zhang ◽  
Xiao Fei Guo ◽  
Yue Ma ◽  
Xiao Yan Zhao
Keyword(s):  
Secondary Structure ◽  
Stearic Acid ◽  
Carboxymethyl Cellulose ◽  
Soybean Protein ◽  
Composite Films ◽  
Protein Isolate ◽  
Soybean Protein Isolate ◽  
Drying Temperature ◽  
The Fourier Transform ◽  
Β Sheet

The effect of the drying temperature on the secondary structure of the soybean protein-isolate/carboxymethyl cellulose/stearic acid composite films was evaluated. The Fourier transform-infrared spectra showed that the stearic acid lose some characteristic absorptions. Hence, the stearic acid was well integrated with the other ingredients. The absorption band (1600~1700 cm-1) of the composite film was deconvoluted into 9 peaks for the calculation of their secondary structure. The β-sheet content of the composite films dried at 90 oC was significant higher than that of the control. Hence, the composite films dried at 90 oC was more stable than the control.

scholarly journals Effect of Secondary Structure determined by FTIR Spectra on Surface Hydrophobicity of Soybean Protein Isolate

2011 ◽  
Vol 15 ◽  
pp. 4819-4827 ◽  
Author(s):  
Chen Wang ◽  
Lianzhou Jiang ◽  
Dongxu Wei ◽  
Yang Li ◽  
Xiaonan Sui ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Soybean Protein ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Ftir Spectra ◽  
Soybean Protein Isolate

scholarly journals Relationship between Secondary Structure and Surface Hydrophobicity of Soybean Protein Isolate Subjected to Heat Treatment

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Zhongjiang Wang ◽  
Yang Li ◽  
Lianzhou Jiang ◽  
Baokun Qi ◽  
Linyi Zhou
Keyword(s):  
Heat Treatment ◽  
Secondary Structure ◽  
Soybean Protein ◽  
Soy Protein Isolate ◽  
Inverse Correlation ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Heat Denaturation ◽  
Soybean Protein Isolate ◽  
Sheet Structure

This study investigated relationship between secondary structure and surface hydrophobicity of soy protein isolate (SPI) subjected to a thermal treatment at 70~90°C. Heat denaturation increased the surface hydrophobicity and surface hydrophobicity decreased as aggregate formed. Heat caused an increase in the relative amount ofα-helix structures and an overall decrease in the amount ofβ-sheet structures when compared with nontreated SPI. The relative amounts of secondary structures varied with time, temperature, and intensity of heat treatment applied. Theβ-sheet structure was most important for its significant role in denaturation of 7S globulin and following formed aggregates and even in denaturation of 11S globulin. The amount ofβ-sheet structure in SPI had an inverse correlation with the surface hydrophobicity when the temperature was kept below 90°C. Besides,β-turn structure increased asβ-7S/B-11S aggregate formated.

scholarly journals Physicochemical Properties and Storage Stability of Food Protein-Stabilized Nanoemulsions

Nanomaterials ◽  
2018 ◽  
Vol 9 (1) ◽  
pp. 25 ◽  
Author(s):  
Yangyang Li ◽  
Hua Jin ◽  
Xiaotong Sun ◽  
Jingying Sun ◽  
Chang Liu ◽  
...  
Keyword(s):  
Corn Oil ◽  
Soybean Protein ◽  
Droplet Diameter ◽  
Protein Isolate ◽  
Random Coil ◽  
Food Protein ◽  
Soybean Protein Isolate ◽  
Bivariate Correlation ◽  
The Mean ◽  
Α Helix

This study investigated the preparation and properties of corn oil nanoemulsions stabilized by peanut protein isolate (PPI), rice bran protein isolate (RBPI), soybean protein isolate (SPI), and whey protein isolate (WPI). The mean droplet diameter of four protein-stabilized nanoemulsions prepared via ultrasound method was less than 245 nm. PPI-stabilized nanoemulsions showed better stability for 4 weeks, while the mean droplet diameter of RBPI-stabilized nanoemulsions had exceeded 1000 nm during the third week of storage. Fourier transform infrared and interfacial tension (IT) analysis showed that the higher level of disordered structure and lower IT of proteins made the stability of nanoemulsions better. Moreover, bivariate correlation analysis discovered that α-helix (p < 0.01) and β-turn (p < 0.05) of proteins were related to the mean droplet diameter of nanoemulsions, the random coil (p < 0.05) was related to the zeta potential of nanoemulsions. This study provided new idea for the relationship between the structure of protein and properties of protein-stabilized nanoemulsions.

Study on the gel properties and secondary structure of soybean protein isolate/egg white composite gels

2014 ◽  
Vol 240 (2) ◽  
pp. 367-378 ◽  
Author(s):  
Yujie Su ◽  
Yiting Dong ◽  
Fuge Niu ◽  
Chenying Wang ◽  
Yuntao Liu ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Soybean Protein ◽  
Egg White ◽  
Protein Isolate ◽  
Gel Properties ◽  
Soybean Protein Isolate ◽  
Composite Gels

scholarly journals Optimization of High Hydrostatic Pressure Treatments on Soybean Protein Isolate to Improve Its Functionality and Evaluation of Its Application in Yogurt

Foods ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 667
Author(s):  
Chenxiao Wang ◽  
Hao Yin ◽  
Yanyun Zhao ◽  
Yan Zheng ◽  
Xuebing Xu ◽  
...  
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Activity Index ◽  
Soybean Protein ◽  
Protein Isolate ◽  
Water Holding Capacity ◽  
Holding Time ◽  
Emulsifying Activity ◽  
Soybean Protein Isolate ◽  
Water Holding

This work aimed to improve the functional properties of soybean protein isolate (SPI) by high hydrostatic pressure (HHP) and develop SPI incorporated yogurt. Response surface methodology (RSM) was used to optimize the HHP treatment parameters, including pressure, holding time, and the ratio of SPI/water. Water holding capacity, emulsifying activity index, solubility, and hardness of SPI gels were evaluated as response variables. The optimized HPP treatment conditions were 281 MPa of pressure, 18.92 min of holding time, and 1:8.33 of SPI/water ratio. Water and oil holding capacity, emulsifying activity, and stability of SPI at different pH were improved. Additionally, relative lipoxygenase (LOX) activity of HHP treated SPI (HHP-SPI) was decreased 67.55 ± 5.73%, but sulphydryl group content of HHP-SPI was increased 12.77%, respectively. When incorporating 8% of SPI and HHP-SPI into yogurt, the water holding capacity and rheological properties of yogurt were improved in comparison with yogurt made of milk powders. Moreover, HHP-SPI incorporated yogurt appeared better color and flavor.

Use of synchrotron-based FTIR microspectroscopy to determine protein secondary structures of raw and heat-treated brown and golden flaxseeds: A novel approach

2005 ◽  
Vol 85 (4) ◽  
pp. 437-448 ◽  
Author(s):  
P. Yu ◽  
J. J. McKinnon ◽  
H. W. Soita ◽  
C. R. Christensen ◽  
D. A. Christensen
Keyword(s):  
Secondary Structure ◽  
Matrix Protein ◽  
Protein Secondary Structure ◽  
Secondary Structures ◽  
Heat Processing ◽  
Lower Percentage ◽  
Protein Secondary Structures ◽  
Novel Approach ◽  
Α Helix ◽  
Β Sheet

The objectives of the study were to use synchrotron Fourier transform infrared microspectroscopy (S-FTIR) as a novel approach to: (1) reveal ultra-structural chemical features of protein secondary structures of flaxseed tissues affected by variety (golden and brown) and heat processing (raw and roasted), and (2) quantify protein secondary structures using Gaussian and Lorentzian methods of multi-component peak modeling. By using multi-component peak modeling at protein amide I region of 1700–1620 cm-1, the results showed that the golden flaxseed contained relatively higher percentage of α-helix (47.1 vs. 36.9%), lower percentage of β-sheet (37.2 vs. 46.3%) and higher (P < 0.05) ratio of α-helix to β-sheet than the brown flaxseed (1.3 vs. 0.8). The roasting reduced (P < 0.05) percentage of α-helix (from 47.1 to 36.1%), increased percentage of β-sheet (from 37.2 to 49.8%) and reduced α-helix to β-sheet ratio (1.3 to 0.7) of the golden flaxseed tissues. However, the roasting did not affect percentage and ratio of α-helix and β-sheet in the brown flaxseed tissue. No significant differences were found in quantification of protein secondary structures between Gaussian and Lorentzian methods. These results demonstrate the potential of highly spatially resolved S-FTIR to localize relatively pure protein in the tissue and reveal protein secondary structures at a cellular level. The results indicated relative differences in protein secondary structures between flaxseed varieties and differences in sensitivities of protein secondary structure to the heat processing. Further study is needed to understand the relationship between protein secondary structure and protein digestion and utilization of flaxseed and to investigate whether the changes in the relative amounts of protein secondary structures are primarily responsible for differences in protein availability. Key words: Synchrotron, FTIR microspectrosopy, flaxseeds, intrinsic structural matrix, protein secondary structures, protein nutritive value

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