Interaction of Soy Protein Isolate and Meat Protein in a Model Emulsion System. Effect of Emulsification Order and Characteristics of Soy Isolate Used

2005 ◽  
Vol 11 (2) ◽  
pp. 79-88 ◽  
Author(s):  
L. G. Santiago ◽  
C. Carrara ◽  
R. J. González
Keyword(s):  
Soy Protein ◽  
Emulsion Stability ◽  
Surface Hydrophobicity ◽  
Soy Proteins ◽  
Emulsion System ◽  
System Effect ◽  
Interfacial Film ◽  
Meat Protein ◽  
Soy Isolate ◽  
Meat Proteins

The compatibility of soy proteins with meat protein (MP) in an emulsion system was examined. Three types of soy protein were employed: a commercial soy isolate (CSPI) and two pilot plant samples, an acid treated (ASPI) and a native soy isolate (NSPI). The incorporation of different isolates and the emulsification order affect in a different way the coalescence stability of emulsions prepared with meat proteins. Physicochemical characteristics (surface hydrophobicity, sulfhydryl content, solubility) of the soy proteins cannot explain the different behaviours towards emulsion stability, although the more native sample (NSPI) performed better than the more denature samples (ASPI or CSPI). The addition of NSPI did not modify the high coalescence stability of meat protein emulsion and the effect of the emulsification order was not significant (p 0.05), which suggested compatibility between both proteins. However, the addition of ASPI or CSPI impaired the emulsion stability. When ASPI was emulsified before MP, ASPI inhibited meat protein adsorption and emulsion became highly stable; while when MP was emulsified before or together with ASPI, meat proteins could be displaced from the interfacial film by the ASPI and the emulsion stability was deteriorated. As regards CSPI, all emulsions were highly unstable to coalescence although fractions of both proteins were found in the interfacial film. It could be suggested a mechanism of competitive adsorption when MP is emulsified together with ASPI or CSPI.(

Increased Heat Resistance of Salmonellae in Beef with Added Soy Proteins

1983 ◽  
Vol 46 (5) ◽  
pp. 380-384 ◽  
Author(s):  
S. E. CRAVEN ◽  
L. C. BLANKENSHIP
Keyword(s):  
Heat Resistance ◽  
Soy Protein ◽  
Soy Proteins ◽  
Plate Count ◽  
Maximum Heat ◽  
Plate Count Agar ◽  
Isolated Soy Protein ◽  
Soy Isolate ◽  
Ph Range ◽  
D Values

Raw beef inoculated with cells of a composite of five Salmonella strains was heated at 54 or 60°C. Survivors were enumerated by plating samples in plate count agar (PCA), XL agar or PCA followed by an XL agar overlay. Best differential recoveries of salmonellae were effected by incubation of PCA plates for 4 h at 37°C followed by overlay with XL agar and incubation for an additional 44 h. D-values of salmonellae at 54 and 60°C were increased significantly when ground beef was supplemented with 30% textured soy protein, soy protein concentrate or isolated soy protein. Increased heat resistance appeared to be caused by an increase in the pH of beef from 5.8–5.9 to 6.1 upon addition of the soy proteins. After adjusting the pH of mixtures of beef and soy proteins with hydrochloric or lactic acid to 5.8 to 5.9, survival of salmonellae to heat was reduced to the level of survival in beef alone. The pH of beef with added structured soy isolate was the same as beef, and heat resistance of salmonellae was not increased in this product. In the pH range 5.9 to 7.1, the maximum heat resistance of salmonellae in beef containing textured soy protein occurred at pH values of 6.5 to 6.8.

Influence of Thermal Treatment and Soy Bean Protein Characteristics on Muscle Protein Emulsion Stability

2006 ◽  
Vol 12 (3) ◽  
pp. 195-204 ◽  
Author(s):  
M. P. Rodríguez ◽  
C. Regue ◽  
A. Bonaldo ◽  
C. Carrara ◽  
L. G. Santiago
Keyword(s):  
Heat Treatment ◽  
Soy Protein ◽  
Emulsion Stability ◽  
Muscle Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Stable Emulsion ◽  
Protein Isolates ◽  
Interfacial Film ◽  
Soy Protein Isolates

The effects of heat treatment on the interaction of salt soluble muscle protein and soy protein isolate in model emulsions were studied. Three soy protein isolates (SPI) were used: a commercial one (CSPI) and two pilot plant samples: a native soy protein isolate (NSPI) and an acid treated soy protein isolate (ASPI). Emulsions were prepared with muscle protein (MP), NSPI, ASPI, CSPI and mixtures of MP and the different SPIs, and then treated at 20, 55, 70, 80 and 90°C. Coalescence, soluble protein and electrophoresis of the aqueous phase of the emulsions were evaluated for each temperature. At 20°C the more native soy protein (NSPI) was compatible with MP, producing a stable emulsion that became more stable during heat treatment. CSPI alone could not form a stable interfacial film through the temperature range, however emulsion stabilisation was achieved at 55°C and 70°C when adding MP. Emulsions prepared with MP ASPI were highly unstable at 20°C, while as the emulsion temperature increased, coalescence decreased abruptly and maintained low values at every temperature. MP, NSPI, ASPI and MP NSPI produced stable emulsions both at 20°C and higher temperatures.

scholarly journals Effect of Surfactant Molecular Structure on Emulsion Stability Investigated by Interfacial Dilatational Rheology

Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1127
Author(s):  
Yuejie Jin ◽  
Dingrong Liu ◽  
Jinhua Hu
Keyword(s):  
Emulsion Stability ◽  
Chain Structure ◽  
Interfacial Film ◽  
Future Design ◽  
Rheological Method ◽  
Viscoelastic Modulus ◽  
Hydrophobic Chain ◽  
Branched Chain ◽  
The Stability ◽  
Branched Structure

Polyglycerol polyricinolate (PGPR) and polyglycerol-2 dioleate were selected as model surfactants to construct water-in-oil (W/O) emulsions, and the effect of interfacial rheological properties of surfactant film on the stability of emulsions were investigated based on the interfacial dilatational rheological method. The hydrophobicity chain of PGPR is polyricinic acid condensed from ricinic acid, and that of polyglycerol-2 dioleate is oleic acid. Their dynamic interfacial tensions in 15 cycles of interfacial compression-expansion were determined. The interfacial dilatational viscoelasticity was analyzed by amplitude scanning in the range of 1–28% amplitude and frequency sweep in the range of 5–45 mHz under 2% amplitude. It was found that PGPR could quickly reach adsorption equilibrium and form interfacial film with higher interfacial dilatational viscoelastic modulus to resist the deformation of interfacial film caused by emulsion coalescence, due to its branched chain structure and longer hydrophobic chain, and the emulsion thus presented good stability. However, polyglycerol-2 dioleate with a straight chain structure had lower interfacial tension, and it failed to resist the interfacial disturbance caused by coalescence because of its lower interfacial dilatational viscoelastic modulus, and thus the emulsion was unstable. This study reveals profound understanding of the influence of branched structure of PGPR hydrophobic chain on the interfacial film properties and the emulsion stability, providing experimental reference and theoretical guidance for future design or improvement of surfactant.

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.

Encapsulated sour cherry pomace extract: Effect on the colour and rheology of cookie dough

2018 ◽  
Vol 25 (2) ◽  
pp. 130-140 ◽  
Author(s):  
Jovana Petrović ◽  
Biljana Pajin ◽  
Ivana Lončarević ◽  
Vesna Tumbas Šaponjac ◽  
Ivana Nikolić ◽  
...  
Keyword(s):  
Rheological Properties ◽  
Wheat Flour ◽  
Soy Protein ◽  
Loss Modulus ◽  
Control Sample ◽  
Sour Cherry ◽  
Soy Proteins ◽  
Blue Colour ◽  
B Values ◽  
Cherry Pomace

In this study, the effect of encapsulated sour cherry pomace extract on the physical characteristics of the cookie dough (colour, textural and rheological properties) was investigated. Sour cherry pomace extract encapsulated in whey (WE) and soy proteins (SE) was incorporated in cookie dough, replacing 10% (WE10 and SE10) and 15% (WE15 and SE15) of wheat flour. The dough samples containing encapsulates had the grey-blue colour ( b* values significantly decreased compared to control sample). Due to the presence of anthocyanins, a* values of the dough colour increased significantly with the addition of encapsulates. The addition of soy protein encapsulate increased hardness, resistance to extension and viscosity of cookie dough and decreased deformation compliance ( J), while the addition of whey encapsulate caused dough softness, higher deformation compliance and lower values of viscosity compared to control sample. Values of storage and loss modulus, G′ and G″, significantly decreased when wheat flour was replaced with WE and increased when the flour was replaced with soy protein encapsulate. The addition of soy protein encapsulate resulted in higher cookie hardness.

scholarly journals Modification of structural and functional properties of sunflower 11S globulin hydrolysates

2016 ◽  
Vol 33 (No. 5) ◽  
pp. 474-479 ◽  
Author(s):  
J. Ren ◽  
Ch. Song ◽  
P. Wang ◽  
S. Li ◽  
N. Kopparapu ◽  
...  
Keyword(s):  
Functional Properties ◽  
Emulsion Stability ◽  
Activity Index ◽  
Binding Capacity ◽  
Surface Hydrophobicity ◽  
Foaming Properties ◽  
Hydrolysis Time ◽  
Structural And Functional Properties ◽  
11S Globulin ◽  
Oil Binding

The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

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