Effects of Microfluidization Treatment and Transglutaminase Cross-Linking on Physicochemical, Functional, and Conformational Properties of Peanut Protein Isolate

2011 ◽  
Vol 59 (16) ◽  
pp. 8886-8894 ◽  
Author(s):  
Xiao Hu ◽  
Mouming Zhao ◽  
Weizheng Sun ◽  
Guangli Zhao ◽  
Jiaoyan Ren
Keyword(s):  
Protein Isolate ◽  
Peanut Protein ◽  
Cross Linking ◽  
Peanut Protein Isolate ◽  
Conformational Properties

Study on Mechanism of Cross-Linking of Peanut Protein Isolate Modified with Transglutaminase

2012 ◽  
Vol 550-553 ◽  
pp. 1304-1308 ◽  
Author(s):  
Qing Jie Sun ◽  
Liu Xiong ◽  
Xiang Hui Bu ◽  
Yan Liu
Keyword(s):  
Ir Spectra ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Isolate ◽  
Peanut Protein ◽  
Cross Linking ◽  
Banding Patterns ◽  
Peanut Protein Isolate ◽  
Sds Page ◽  
Ft Ir

The mechanism of cross-linking of peanut protein isolate (PPI) modified with transglutaminase was investigated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier Transformation Infrared (FT-IR) spectra. SDS-PAGE banding patterns indicated that the contents of arachin and conarachin after transglutaminase (TGase) modification were decreased and high molecular weight polymers were formed. SDS-PAGE banding patterns also suggested that cross-linking effects were accomplished in the presence of transglutaminase and the main component participating in cross-linking was arachin. The representative FT-IR spectra of arachin, conarachin modified with TGase treatment appeared the sharp peak at 1680~1630cm-1 region, which showed that intramolecular cross-linking was occurred, respectively. Compared with FT-IR spectra of arachin, conarachin modified with TGase treatment, the spectra of PPI modified with TGase treatment appeared two characteristic absorption at 1546.29cm-1 and 1330.75cm-1, suggesting that cross-linking was occurred between arachin and conarachin and the ε-(γ-glutamyl) isopeptide bond generated.

scholarly journals Effect of Protein Oxidation on the Conformational Properties of Peanut Protein Isolate

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Lin Ye ◽  
Yu Liao ◽  
Mouming Zhao ◽  
Weizheng Sun
Keyword(s):  
Protein Aggregation ◽  
Conformational Changes ◽  
Protein Oxidation ◽  
Protein Solubility ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Peanut Protein ◽  
Peroxyl Radicals ◽  
Peanut Protein Isolate ◽  
Conformational Properties

Peanut protein isolate (PPI) was oxidized by peroxyl radicals derived from 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH), and the conformational properties of oxidized PPI were investigated. Oxidation of PPI resulted in gradual carbonyl generation and free sulfydryl group degradation. The analysis of the maximum emission wavelength indicated change in the tertiary conformation of PPI after oxidation. Lower level oxidation could generate soluble protein aggregates with more flexible structure, while higher level oxidation would induce the formation of insoluble aggregates. Result from dynamic light scattering (DLS) and protein solubility showed that protein aggregation was correlated with protein surface hydrophobicity, indicating that protein oxidation and heat treatment could induce protein aggregation, leading to PPI conformational changes.

Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate

2016 ◽  
Vol 170 ◽  
pp. 33-40 ◽  
Author(s):  
Kui-Jie Gong ◽  
Ai-Min Shi ◽  
Hong-Zhi Liu ◽  
Li Liu ◽  
Hui Hu ◽  
...  
Keyword(s):  
Protein Isolate ◽  
Peanut Protein ◽  
Emulsifying Properties ◽  
Peanut Protein Isolate ◽  
Structure Changes ◽  
Freeze Dried

Preparation and characterisation of films from xylose-glycosylated peanut protein isolate powder

2015 ◽  
Vol 50 (7) ◽  
pp. 1538-1544 ◽  
Author(s):  
Wei-Jing Lin ◽  
Hong-Zhi Liu ◽  
Ai-Min Shi ◽  
Li Liu ◽  
Benu Adhikari ◽  
...  
Keyword(s):  
Protein Isolate ◽  
Peanut Protein ◽  
Peanut Protein Isolate

Mechanism of the discrepancy in the enzymatic hydrolysis efficiency between defatted peanut flour and peanut protein isolate by Flavorzyme

2015 ◽  
Vol 168 ◽  
pp. 100-106 ◽  
Author(s):  
Lin Zheng ◽  
Yijun Zhao ◽  
Chuqiao Xiao ◽  
Dongxiao Sun-Waterhouse ◽  
Mouming Zhao ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Protein Isolate ◽  
Peanut Protein ◽  
Peanut Flour ◽  
Peanut Protein Isolate

Optimization of the Ultrasonic Wave-Assisted Extraction Condition of Peanut Protein Isolate

2011 ◽  
Vol 189-193 ◽  
pp. 3904-3911 ◽  
Author(s):  
Hui Cui Zhang ◽  
Lin Tang ◽  
Qing Li Yang
Keyword(s):  
Ultrasonic Wave ◽  
Protein Isolate ◽  
Extraction Yield ◽  
Peanut Protein ◽  
Ultrasonic Power ◽  
Liquid Ratio ◽  
Extraction Condition ◽  
Peanut Protein Isolate ◽  
Assisted Extraction ◽  
Ultrasonic Time

Ultrasonic Wave was used to assist alkali extraction and acid precipitation of peanut protein isolate from defatted peanut powder. Based on the single factor test, the response surface analysis results shows that the Ultrasonic Wave-assisted Extraction condition is: ultrasonic power 210W, ultrasonic time 30min, ultrasonic temperature 40°C ,solid to liquid ratio 1:10.7, and under this improved condition the extraction yield could reach 80.09%.

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