scholarly journals Improved Oxidation Stability of Camellia Oil-in-Water Emulsions Stabilized by the Mixed Monolayer of Soy Protein Isolate/Bamboo Shoot Protein Complexes

2021 ◽  
Vol 8 ◽  
Author(s):  
Yuhang Xi ◽  
Aiping Zhang ◽  
Zhongjiang Wang ◽  
Shahzad Farooq ◽  
Cen Zhang ◽  
...  
Keyword(s):  
Soy Protein ◽  
Layer Structure ◽  
Soy Protein Isolate ◽  
Oxidation Stability ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Bamboo Shoot ◽  
Emulsifying Activity ◽  
Camellia Oil ◽  
Oil In Water

The complex of soy protein isolate (SPI)/bamboo shoot protein concentrate (BPC) was developed to stabilize camellia oil-in-water (O/W) emulsions. The surface hydrophobicity of the BPC/SPI complex driven by hydrogen bonds and electrostatic attractions was improved. With the increasing ratio of BPC in the complex, a tighter network layer structure of the complex was formed due to the rearrangement of proteins, and the emulsions showed a progressive enhancement in the gel-like structures. At the SPI/BPC ratio of 2:1, the emulsions had smaller droplet size and lower creaming index of 230 nm and 30%, and the emulsifying activity and stability indices of the emulsions were 803.72 min and 11.85 g/m2, respectively, indicating a better emulsifying activity and stability of emulsions. Meanwhile, the emulsions stabilized by the complex at the ratio of 2:1 showed better storage and antioxidant stability. These findings are expected to develop the application of bamboo shoots in emulsion-based food products such as mayonnaise, salad dressings, and sauces.

Comparison of plant-based emulsifier performance in water-in-oil-in-water emulsions: Soy protein isolate, pectin and gum Arabic

2021 ◽  
Vol 307 ◽  
pp. 110625
Author(s):  
Jinning Liu ◽  
Hualu Zhou ◽  
Yunbing Tan ◽  
Jorge L. Muriel Mundo ◽  
David Julian McClements
Keyword(s):  
Soy Protein ◽  
Soy Protein Isolate ◽  
Gum Arabic ◽  
Protein Isolate ◽  
Oil In Water

scholarly journals Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-O-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition

Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1721
Author(s):  
Yaru Wu ◽  
Zhucheng Yin ◽  
Xuejiao Qie ◽  
Yao Chen ◽  
Maomao Zeng ◽  
...  
Keyword(s):  
Antioxidant Capacity ◽  
Soy Protein ◽  
Average Particle Size ◽  
Soy Protein Isolate ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Antagonistic Effect ◽  
Masking Effect ◽  
Average Particle

The interaction of soy protein isolate (SPI) and its hydrolysates (SPIHs) with cyanidin-3-O-glucoside (C3G) at pH 7.0 were investigated to clarify the changes in the antioxidant capacity of their complexes. The results of intrinsic fluorescence revealed that C3G binds to SPI/SPIHs mainly through hydrophobic interaction, and the binding affinity of SPI was stronger than that of SPIHs. Circular dichroism and Fourier-transform infrared spectroscopy analyses revealed that the interaction with C3G did not significantly change the secondary structures of SPI/SPIHs, while the surface hydrophobicity and average particle size of proteins decreased. Furthermore, the SPI/SPIHs-C3G interaction induced an antagonistic effect on the antioxidant capacity (ABTS and DPPH) of the complex system, with the masking effect on the ABTS scavenging capacity of the SPIHs-C3G complexes being lower than that of the SPI-C3G complexes. This study contributes to the design and development of functional beverages that are rich in hydrolysates and anthocyanins.

scholarly journals Stabilization of oil-in-water emulsions via soy protein and soy soluble polysaccharide interactions

2021 ◽  
Author(s):  
Tu Tran
Keyword(s):  
Phase Separation ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Acidic Ph ◽  
Steric Repulsion ◽  
Sedimentation Analysis ◽  
Oil In Water ◽  
Soluble Polysaccharide ◽  
Over Time

The stabilizing behaviour of soluble soy polysaccharide (SSPS) on acidified dispersions of soy protein isolate (SPI) and SPI-stabilized emulsions was studied. SPI and SSPS suspensions were characterized via light scattering, surface charge measurement, turbidity, sedimentation analysis, and light microscopy. At acidic pH (pH 6-3), it was found the addition of at least 0.25 wt% SSPS was required to stabilize 0.75 wt% SPI suspensions against aggregation and phase separation, likely via steric repulsion. The mechanism of SPI-SSPS interaction was shown to be electrostatic in nature by testing the effects of increased ionic strength of the suspensions. The stabilizing effect of SSPS on SPI was then applied to 5% oil-in-water emulsions. The presence of SSPS stabilized the emulsions against droplet size increases and phase separation over time. Overall, the results demonstrated that it was possible for SSPS to stabilize SPI suspensions and that SPI-SSPS interactions may be used as a tool to stabilize O/W emulsions.

scholarly journals Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate  

2017 ◽  
Vol 35 (No. 1) ◽  
pp. 57-66 ◽  
Author(s):  
Pan Mingzhe ◽  
Meng Xianjun ◽  
Jiang Lianzhou ◽  
Yu Dianyu ◽  
Liu Tianyi
Keyword(s):  
Soy Protein ◽  
Structural Changes ◽  
Foam Stability ◽  
Soy Protein Isolate ◽  
Tryptophan Fluorescence ◽  
Surface Hydrophobicity ◽  
Cd Spectroscopy ◽  
Protein Isolate ◽  
Foaming Properties ◽  
Intrinsic Tryptophan Fluorescence

Effect of polyols (mannitol, sorbitol, and xylitol) at three concentrations (5, 10, and 15% w/w) on the structure of soy protein isolates (SPI) was investigated. Changes in foaming properties of SPI were then examined with the addition of polyols at different concentrations. The interactions between SPI and polyols resulted in a substantial decrease in protein surface hydrophobicity and intrinsic tryptophan fluorescence intensity, along with the covering of tyrosine. Furthermore, circular dichroism (CD) spectroscopy of SPI suggested that a more ordered and compact conformation was induced by polyols. Consequently, these structural changes led to lower foamability of SPI. An increase in the viscosity of SPI suspension seemed to be advantageous for improving the foam stability of SPI.

Freeze-Thaw Stability of Oil-in-Water Prepared with Soy Protein Isolate-Maltodextrin Conjugates

2012 ◽  
Vol 602-604 ◽  
pp. 1206-1210
Author(s):  
Guo Ping Yu ◽  
Chao Ran Dou ◽  
Yan Song ◽  
Hao Wu ◽  
Zhu Gong
Keyword(s):  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Freeze Thaw ◽  
Covalent Coupling ◽  
Oil In Water ◽  
The Impact

The objective of the study was to investigate the impact of soy protein isolate (SPI)-maltodextrin conjugates on the freeze-thaw stability of oil-in-water emulsions. Covalent coupling of maltodextrin to SPI was achieved by wet heating of SPI- maltodextrin mixtures of different weight ratios and different protein contents at 70,80,90,100°C for 1 to 5 h. The freeze-thaw stability was characterized by measurements of creaming index and oiling off after isothermal storage at -20 °C for 24 h and further thawing. Compared with those stabilized by SPI alone, o/w emulsions stabilized by SPI-maltodextrin conjugates showed a higher stability against freeze-thaw treatment, exhibiting a lower creaming index and oiling off.

Fabrication and emulsifying properties of non-covalent complexes between soy protein isolate fibrils and soy soluble polysaccharides

2021 ◽  
Author(s):  
Hekai Zhao ◽  
Shengnan Wang ◽  
Guilan Zhao ◽  
Yangyang Li ◽  
Xiulin Liu ◽  
...  
Keyword(s):  
Ir Spectroscopy ◽  
Zeta Potential ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Oil In Water ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Non-covalent complexes (SPIF/SSPS) between soy protein isolate fibrils (SPIF) and soy soluble polysaccharides (SSPS) were fabricated and used to stabilize oil-in-water (O/W) emulsions. FT-IR spectroscopy and zeta potential results demonstrated...

Research on Soluble Protein Surface Hydrophobicity of Biomaterial Solution from Soy Protein Isolate - Polysaccharide System

2011 ◽  
Vol 183-185 ◽  
pp. 1094-1099
Author(s):  
Chun Xia Sui ◽  
Guo Ping Yu ◽  
Lian Zhou Jiang ◽  
Yi Hong Bao ◽  
De Jun Mei ◽  
...  
Keyword(s):  
Soy Protein ◽  
Salt Concentration ◽  
Soluble Protein ◽  
Guar Gum ◽  
Soy Protein Isolate ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Quadratic Model ◽  
Box Behnken Design ◽  
Protein Surface Hydrophobicity

The work attempts to study the surface hydrophobicity (S0) of soy protein isolate（SPI）-guar gum(GG) systems for biomaterial. Effect of four factors on the S0 values of the mixtures were studied. A response surface analysis was carried out using the Box-Behnken Design (BBD)method in order to determine the effects and interactions of pH (6.0, 8.0, 10.0), salt(0.05, 0.15, 0.25M), guar gum(0.10, 0.30, 0.50% w/v) and SPI concentrations (3, 4, 5% w/v) on the S0 values of mixtures. The datas were fitted into second order quadratic model. Salt concentration, pH and SPI concentration, interactions between pH and salt concentration, pH and GG concentration, pH and SPI concentration, GG and SPI concentrations were significant(P<0.05).

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