Modification of foaming properties of soy protein isolate by high ultrasound intensity: Particle size effect

2015 ◽  
Vol 26 ◽  
pp. 48-55 ◽  
Author(s):  
Rocío Morales ◽  
Karina D. Martínez ◽  
Víctor M. Pizones Ruiz-Henestrosa ◽  
Ana M.R. Pilosof
Keyword(s):  
Particle Size ◽  
Size Effect ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Particle Size Effect ◽  
Protein Isolate ◽  
Foaming Properties ◽  
Ultrasound Intensity

Improving the Foaming Properties of Soy Protein Isolate Through Partial Enzymatic Hydrolysis

2013 ◽  
Vol 31 (13-14) ◽  
pp. 1545-1552 ◽  
Author(s):  
Maomao Zeng ◽  
Benu Adhikari ◽  
Zhiyong He ◽  
Fang Qin ◽  
Xiaolin Huang ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Foaming Properties

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.

scholarly journals Effects of Cavitation Jet Treatment on the Structure and Emulsification Properties of Oxidized Soy Protein Isolate

Foods ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 2
Author(s):  
Mingyu He ◽  
Changling Wu ◽  
Lijia Li ◽  
Li Zheng ◽  
Tian Tian ◽  
...  
Keyword(s):  
Particle Size ◽  
Soy Protein ◽  
Activity Index ◽  
Soy Protein Isolate ◽  
Sulfhydryl Group ◽  
Stability Index ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Atomic Force ◽  
Α Helix

This study examined the ability of cavitation jet processing to regulate the oxidation concentrations with 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH) (0.2, 1, and 5 mmol/L) and the structure and emulsification of soy protein isolate (SPI). The tested properties included particle size distribution, hydrophobic properties (sulfhydryl group (SH) and disulfide bond (S-S) contents, surface hydrophobicity (H0)), emulsifying properties (particle size and ζ-potential of emulsions, emulsification activity index (EAI), and emulsification stability index (ESI)), as well as conformational characteristics. The high shear force of cavitation jet treatment reduced the particle size of oxidized SPI and distributed uniformly. Cavitation jet (90 MPa)-treated SPI (AAPH with 1 mmol/L) demonstrated a high H0 (4688.70 ± 84.60), high EAI (71.78 ± 1.52 m2/g), and high ESI (86.73 ± 0.97%). The ordered secondary structure (α-helix and β-turn content) of SPI was enhanced by the cavitation jet. Meanwhile, the distribution of SPI-oxidized aggregates was observed under an atomic force microscope. Therefore, cavitation jet processing combined with oxidation treatment is an effective method to improve the characteristics of SPI and has potential industrial application prospects.

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