scholarly journals Role of Disulfide Bonds and Sulfhydryl Blocked by N-Ethylmaleimide on the Properties of Different Protein-Stabilized Emulsions

Foods ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 3079
Author(s):  
Mangang Wu ◽  
Zhikun Li ◽  
Ranran Wei ◽  
Yi Luan ◽  
Juan Hu ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Soybean Protein ◽  
Protein Molecule ◽  
Blocking Agent ◽  
Protein Isolate ◽  
Sulfhydryl Groups ◽  
Subtle Difference ◽  
Soybean Protein Isolate ◽  
Protein Membrane

To investigate the role of sulfhydryl groups and disulfide bonds in different protein-stabilized emulsions, N-ethylmaleimide (NEM) was used as a sulfhydryl-blocking agent added in the emulsion. The addition of NEM to block the sulfhydryl groups resulted in a reduction in disulfide bond formation, which enabled the internal structure of the protein molecule to be destroyed, and then decreased the restriction of protein membrane on the oil droplets. Furthermore, with the NEM content increasing in the emulsion, a reduction in the protein emulsifying activity and emulsion stability also occurred. At the same time, the intermolecular interaction of the protein on the oil droplet interface membrane was destroyed, and the emulsion droplet size increased with the NEM content in the emulsion. Although NEM blocking sulfhydryl groups from forming disulfide bonds has similar effects on three types of protein emulsion, the degree of myofibrillar protein (MP), egg-white protein isolate (EPI), and soybean protein isolate (SPI) used as emulsifiers had a subtle difference.

scholarly journals Role of Disulfide Bonds and Sulfhydryl Blocked by N-Ethylmaleimide on the Properties of Different Protein-Stabilized Emulsions

2021 ◽  
Author(s):  
Mangang Wu ◽  
Zhikun Li ◽  
Ranran Wei ◽  
Yi Luan ◽  
Juan Hu ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Soybean Protein ◽  
Protein Molecule ◽  
Blocking Agent ◽  
Protein Isolate ◽  
Sulfhydryl Groups ◽  
Subtle Difference ◽  
Soybean Protein Isolate ◽  
Protein Membrane

To investigate the role of sulfhydryl groups and disulfide bonds in different protein-stabilized emulsions, N-ethylmaleimide (NEM) was used as sulfhydryl-blocking agent to be added in the emulsion. The addition of NEM to block the sulfhydryl groups resulted in a reduction of the content of disulfide bonds formation, which enabled destruction of the internal structure of the protein molecule, and then decreased the restriction of protein membrane on the oil droplets. Furthermore, with NEM content increasing in the emulsion, a reduction of protein emulsifying activity and emulsion stability also occurred. At the same time, the intermolecular interaction of the protein on the oil droplet interface membrane was destroyed, and the emulsion droplet size increased with the NEM content in the emulsion. Although NEM blocking sulfhydryl groups not to form disulfide bonds has similar effects on three types of protein emulsion, the degree of myofibrillar protein (MP), egg-white protein isolate (EPI), and soybean protein isolate (SPI) as emulsifier had a subtle difference.

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.

Effect of 11S/7S Ratios on Mechanical and Barrier Properties of Edible Films Based on Soybean Protein Isolate

2011 ◽  
Vol 335-336 ◽  
pp. 312-319
Author(s):  
Xiao Yan Zhao ◽  
Kuan Guo ◽  
Chao Zhang ◽  
Yue Ma ◽  
Xi Hong Li
Keyword(s):  
Disulfide Bonds ◽  
Soybean Protein ◽  
Water Vapor Permeability ◽  
Barrier Properties ◽  
Edible Films ◽  
Protein Isolate ◽  
Vapor Permeability ◽  
Soybean Protein Isolate ◽  
The Matrix ◽  
11S Globulin

The effect of 11S/7S ratios on mechanical and barrier properties of soybean-protein-isolate films was evaluated. The tensile strength increased with an increase of 11S globulin ratio when it was higher than 50 % in soybean-protein-isolate films, and decreased with an increase of 11S globulin ratio when it was lower than 50%. Moreover, the total soluble matter of soybean-protein-isolate films decreased with an increase of 11S globulin ratio, while the elongation at break, moisture content, and optical transparency of soybean-protein-isolate films increased with an increase of 11S globulin ratio. Furthermore, 11S/7S ratios had no influence on the water vapor permeability of soybean-protein-isolate films. These phenomenon mainly resulted from that the matrix of soybean-protein-isolate films was mainly maintained by disulfide bonds when 11S globulin ratio was higher than 50%, while that was maintained by intermolecular hydrogen bonds when 11S globulin ratio was lower than 50%.

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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