Effect of high intensity ultrasound on the structure and physicochemical properties of soy protein isolates produced by different denaturation methods

2019 ◽  
Vol 97 ◽  
pp. 105216 ◽  
Author(s):  
Ting Zheng ◽  
Xiaohui Li ◽  
Ahmed Taha ◽  
Yue Wei ◽  
Tan Hu ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Soy Protein ◽  
High Intensity ◽  
High Intensity Ultrasound ◽  
Protein Isolates ◽  
Soy Protein Isolates

scholarly journals Physicochemical properties of soy protein isolates-acacia gum conjugates

2011 ◽  
Vol 29 (No. 2) ◽  
pp. 129-136 ◽  
Author(s):  
L. Mu ◽  
H. Zhao ◽  
M. Zhao ◽  
Ch. Cui ◽  
L. Liu
Keyword(s):  
Physicochemical Properties ◽  
Soy Protein ◽  
Time Course ◽  
Activity Index ◽  
Stability Index ◽  
Heating Method ◽  
Protein Isolates ◽  
Soy Protein Isolates ◽  
Acacia Gum ◽  
Graft Reaction

Protein-polysaccharide conjugates were generally prepared by dry-heating. However, it was time-consuming and the sample gained was inhomogeneous. A faster way of preparing protein-polysaccharide conjugates is needed. Accordingly, soy protein isolates (SPI)-Acacia gum (GA) conjugates prepared by the wet-heating method were studied in the present work. Physicochemical properties of SPI-GA conjugates were also determined. The results showed that the wet-heating method could improve the rate of the graft reaction of protein and polysaccharide. The solubility of SPI-GA conjugates was significantly (P < 0.05) higher than that of unreacted SPI-GA mixtures and SPI at the same pH values. The emulsion activity index (EAI) of the grafted SPI increased remarkably. Moreover, a significant (P < 0.05) improvement on the emulsifying stability index (ESI) was observed and emulsions with a smaller droplet size were obtained. No visible flocculation during extended storage (30 days) was observed. The time course of the development of the graft reaction of SPI with GA was also shown by SDS-PAGE.

Water uptake by dehydrated soy protein isolates

2003 ◽  
Vol 56 (4) ◽  
pp. 331-338 ◽  
Author(s):  
Germán Jovanovich ◽  
Marı́a C Puppo ◽  
Sergio A Giner ◽  
Marı́a C Añón
Keyword(s):  
Water Uptake ◽  
Soy Protein ◽  
Protein Isolates ◽  
Soy Protein Isolates

Gel properties and interactions of Mesona blumes polysaccharide-soy protein isolates mixed gel: The effect of salt addition

2018 ◽  
Vol 192 ◽  
pp. 193-201 ◽  
Author(s):  
Wenjie Wang ◽  
Mingyue Shen ◽  
Suchen Liu ◽  
Lian Jiang ◽  
Qianqian Song ◽  
...  
Keyword(s):  
Soy Protein ◽  
Gel Properties ◽  
Protein Isolates ◽  
Soy Protein Isolates ◽  
Salt Addition

scholarly journals High-Intensity Ultrasound Treatment on Soy Protein after Selectively Proteolyzing Glycinin Component: Physical, Structural, and Aggregation Properties

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 839
Author(s):  
Wenjie Xia ◽  
Siyi Pan ◽  
Zhe Cheng ◽  
Yan Tian ◽  
Xingjian Huang
Keyword(s):  
Soy Protein ◽  
High Intensity ◽  
Disulfide Bonds ◽  
Hydrophobic Interactions ◽  
Early Stage ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
High Intensity Ultrasound ◽  
Gelling Properties ◽  
Novel Method

In this study, a novel method called selective proteolysis was applied to the glycinin component of soy protein isolate (SPI), and a degraded glycinin hydrolysate (DGH) was obtained. The effects of high-intensity ultrasound (HIU) treatment (20 kHz at 400 W, 0, 5, 20, and 40 min) on the physical, structural, and aggregation properties of DGH were investigated with the aim to reveal the influence of the selectively hydrolyzing glycinin component on the HIU treatment of soy protein. The effects of HIU on DGH and a control SPI (CSPI) were both time-dependent. HIU induced the formation of soluble aggregates in both samples at an early stage, while it dissociated these newly formed aggregates after a longer duration. Selectively hydrolyzing glycinin contributed to the soluble aggregation by exposing the compact protein structure and producing small protein fractions. The larger extent of hydrophobic interactions and disulfide bonds imparted a higher stability to the soluble protein aggregates formed in DGH. As a result, DGH displayed more ordered secondary structures, a higher solubility, and better gelling properties after the HIU treatment, especially at 20 min. The results of this study will be beneficial to the scientific community as well as industrial application.

Design of novel edible hydrocolloids by structural interplays between wheat gluten proteins and soy protein isolates

2020 ◽  
Vol 100 ◽  
pp. 105395 ◽  
Author(s):  
Jian He ◽  
Ren Wang ◽  
Wei Feng ◽  
Zhengxing Chen ◽  
Tao Wang
Keyword(s):  
Soy Protein ◽  
Wheat Gluten ◽  
Protein Isolates ◽  
Gluten Proteins ◽  
Soy Protein Isolates
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