Effects of flexibility and surface hydrophobicity on emulsifying properties: Ultrasound-treated soybean protein isolate

LWT ◽  
2021 ◽  
Vol 142 ◽  
pp. 110881
Author(s):  
Shizhang Yan ◽  
Jingwen Xu ◽  
Shuang Zhang ◽  
Yang Li
Keyword(s):  
Soybean Protein ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Soybean Protein Isolate

scholarly journals Effect of Secondary Structure determined by FTIR Spectra on Surface Hydrophobicity of Soybean Protein Isolate

2011 ◽  
Vol 15 ◽  
pp. 4819-4827 ◽  
Author(s):  
Chen Wang ◽  
Lianzhou Jiang ◽  
Dongxu Wei ◽  
Yang Li ◽  
Xiaonan Sui ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Soybean Protein ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Ftir Spectra ◽  
Soybean Protein Isolate

scholarly journals Relationship between Secondary Structure and Surface Hydrophobicity of Soybean Protein Isolate Subjected to Heat Treatment

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Zhongjiang Wang ◽  
Yang Li ◽  
Lianzhou Jiang ◽  
Baokun Qi ◽  
Linyi Zhou
Keyword(s):  
Heat Treatment ◽  
Secondary Structure ◽  
Soybean Protein ◽  
Soy Protein Isolate ◽  
Inverse Correlation ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Heat Denaturation ◽  
Soybean Protein Isolate ◽  
Sheet Structure

This study investigated relationship between secondary structure and surface hydrophobicity of soy protein isolate (SPI) subjected to a thermal treatment at 70~90°C. Heat denaturation increased the surface hydrophobicity and surface hydrophobicity decreased as aggregate formed. Heat caused an increase in the relative amount ofα-helix structures and an overall decrease in the amount ofβ-sheet structures when compared with nontreated SPI. The relative amounts of secondary structures varied with time, temperature, and intensity of heat treatment applied. Theβ-sheet structure was most important for its significant role in denaturation of 7S globulin and following formed aggregates and even in denaturation of 11S globulin. The amount ofβ-sheet structure in SPI had an inverse correlation with the surface hydrophobicity when the temperature was kept below 90°C. Besides,β-turn structure increased asβ-7S/B-11S aggregate formated.

scholarly journals Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate

Molecules ◽  
2018 ◽  
Vol 23 (9) ◽  
pp. 2127 ◽  
Author(s):  
Yinglei Zhang ◽  
Yanyang Yin ◽  
Shuwen Lu ◽  
Xinmiao Yao ◽  
Xianzhe Zheng ◽  
...  
Keyword(s):  
Zeta Potential ◽  
Protein Modification ◽  
Structural Changes ◽  
Soybean Protein ◽  
Surface Hydrophobicity ◽  
Protein Isolate ◽  
Soybean Protein Isolate ◽  
Black Soybean ◽  
Natural Protein ◽  
Enzymatic Glycosylation

To explore better methods of natural protein modification for black soybean, comparisons among the effects of different modified methods on structural changes of the modified products of black soybean protein isolate (BSPI) were carried out in this study. The modified products used in this study included enzymatic crossing-link black soybean protein isolate (ECBSPI), wet heating treatment glycosylation black soybean protein isolate (WHTGBSPI) and especially enzymatic glycosylation black soybean protein isolate catalyzed by transglutaminase (EGBSPI). The effects of the modification methods on structural changes were analyzed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), amino acid content and circular dichroism (CD) analysis. Moreover, the processing properties changes caused by structural changes of BSPI were detected by thermogravimetric analysis, particle size analysis, zeta-potential, surface hydrophobicity, solubility, emulsification, gelation, and rheological properties. The results show that the modified BSPI products were protein polymers, and among them, EGBSP and WHTGBSPI are covalently bonded glycation products. Products modified by Maillard reactions and transglutaminase (TG) display partly destroyed α-helix and β-sheet structures that form more open secondary BSPI structures. For ECBSPI, the proportion of irregular crimp structure reduces to form a high order secondary structure. All the modified products form fine aggregations in dispersion, except WHTGBSPI has most negative zeta-potential and least molecular stability due to the hydrophobic amino acids embedded in the protein molecules. The zeta-potentials of BSPI, ECBSPI, WHTGBSPI and EGBSPI are respectively −21.5, −23.8, −18.1 and −20.2 mV. The surface hydrophobicity of EGBSPI (5.07 ± 0.07) and WHTGBSPI (7.02 ± 0.05) decrease, while the surface hydrophobicity of ECBSPI (19.5 ± 0.06) increases. The solubility and rheological properties of EGBSPI, ECBSPI and WHTGBSPI after modification are all better than those of BSPI, especially EGBSPI. Emulsification of EGBSPI and WHTGBSPI increase (by 24.5% and 12.2%, respectively) while ECBSPI decrease (by 17.0), and there is similar emulsion stability trend. Moreover, the properties of ECBSPI increase except cohesiveness compared to BSPI. In conclusion, as a safe and efficient method for natural protein modification, enzymatic glycosylation catalyzed by TG has great potential in improving food processing characteristics.

Improvement of Emulsifying Properties of Soybean Protein Isolate through Glycosylation Modification

2013 ◽  
Vol 781-784 ◽  
pp. 1495-1499 ◽  
Author(s):  
Xi Bo Wang ◽  
Ying Hua Zhang ◽  
Lian Zhou Jiang
Keyword(s):  
Reaction Time ◽  
Reaction Temperature ◽  
Soybean Protein ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Single Factor ◽  
Soybean Protein Isolate ◽  
Operation Conditions ◽  
Single Factor Experiment

In order to improve EAI and ESI of Soybean protein isolate (SPI), Glycosylation modification was studied by adding lactose and the operation conditions for modification were established by single factor experiment. On the basis, Box-Behnken model was used to optimize technological conditions, test and analyze the EAI and ESI of modified products under various conditions. The best glycosylation modification was as follows: the augmenter of lactose was 6.9%, reaction temperature was 70.5°C, reaction time was 38.6h, and the EAI and ESI could achieve 0.754 and 24.00 which was 2.32 and 2.67 times of the unmodified SPI. The experiment proved that the modification technology can effectively increase EAI and ESI of SPI.

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