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.

scholarly journals Effect of Soybean Soluble Polysaccharide on the Formation of Glucono-δ-Lactone-Induced Soybean Protein Isolate Gel

Polymers ◽  
2019 ◽  
Vol 11 (12) ◽  
pp. 1997 ◽  
Author(s):  
Qiuyu Lan ◽  
Lin Li ◽  
Hongmin Dong ◽  
Dingtao Wu ◽  
Hong Chen ◽  
...  
Keyword(s):  
Electrostatic Interaction ◽  
Disulfide Bonds ◽  
Color Change ◽  
Soybean Protein ◽  
Sulfhydryl Group ◽  
Protein Isolate ◽  
Random Coil ◽  
Infrared Analysis ◽  
Soybean Protein Isolate ◽  
Soluble Polysaccharide

The effect of soybean soluble polysaccharide (SSPS) on the formation of glucono-δ-lactone (GDL)-induced soybean protein isolate (SPI) gel was investigated. Electrophoretic analysis showed the SSPS did not change the electrophoretic behavior of SPI during the formation of SPI gel. However, infrared analysis indicated the β-sheet content increased, and the contents of random coil and α-helix decreased in both cooked SPI and SPI gel. The SSPS and SPI might conjugate via the Maillard reaction according to the results of grafting degree, color change, and infrared analyses. The main interactions during the formation of SPI gel changed from non-covalent to electrostatic interaction after adding SSPS. Sulfhydryl group content also increased in both cooked SPI and SPI gel. The water-holding capacity and gel strength of SPI gel decreased as the SSPS concentration increased. Larger aggregate holes were observed in the microstructure of SPI gel at higher SSPS concentration. Thus, SSPS could covalently conjugate with SPI and influence the formation of hydrogen bonds, disulfide bonds, and electrostatic interaction among SPI molecules to eventually form a loose gel network.

scholarly journals The Molecular Properties of Peanut Protein: Impact of Temperature, Relative Humidity and Vacuum Packaging during Storage

Molecules ◽  
2018 ◽  
Vol 23 (10) ◽  
pp. 2618 ◽  
Author(s):  
Xiaotong Sun ◽  
Hua Jin ◽  
Yangyang Li ◽  
Haiying Feng ◽  
Chunhong Liu ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Functional Properties ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Peanut Protein ◽  
Molecular Properties ◽  
Random Coil ◽  
Bivariate Correlation ◽  
Protein Particle ◽  
Α Helix

This study aimed to investigate the variation of molecular functional properties of peanut protein isolate (PPI) over the storage process and reveal the correlation between the PPI secondary structure and properties in the storage procedure. After storage, the molecular properties of PPI changed significantly (p < 0.05). Extending storage time resulted in a decrease in free sulfhydryl content, fluorescence intensity, surface hydrophobicity and emulsifying properties, which was accompanied by an increase in protein particle size. The results of infrared spectroscopy suggested the content decline of α-helix and β-sheet, and the content rise of β-turn and random coil. Based on bivariate correlation analysis, it was revealed that surface hydrophobicity and emulsifying activity of PPI was significantly affected by α-helix and by β-turn (p < 0.05), respectively. This research supplied more information for the relationship between the peanut protein’s secondary structure and functional properties over the stored process.

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.

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.

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