scholarly journals Effects of High Hydrostatic Pressure Pretreatment on the Functional and Structural Properties of Rice Bran Protein Hydrolysates

Foods ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 29
Author(s):  
Shirang Wang ◽  
Tengyu Wang ◽  
Yue Sun ◽  
Yingju Cui ◽  
Guoping Yu ◽  
...  

Rice bran protein (RBP) hydrolysis was conducted after high hydrostatic pressure (HHP) pretreatment. The structural and functional properties of HHP-pretreated rice bran protein hydrolysates (RBPH) were investigated. HHP pretreatments were conducted at 100, 200, and 300 MPa; then, enzymatic hydrolysis at atmospheric pressure was performed using trypsin. An RBPH sample that had not been pretreated by HHP was used as a control. Free sulfhydryl (SH) content, SDS-PAGE profiles, high-performance size exclusion chromatography (HPSEC), Fourier transform infrared (FTIR) spectrum, scanning electron microscopy (SEM), intrinsic fluorescence spectrum, solubility, and emulsifying and foaming properties were evaluated. Changes in particle size and ζ-potential were monitored. Compared with the control, the results of solubility, the emulsifying activity index (EAI) and the emulsifying stability index (ESI) increased significantly (p < 0.05) at 200 MPa. The content of free SH increased significantly (p < 0.05) at 100 MPa. FTIR spectrum and fluorescence analysis confirmed the changes in the secondary and tertiary structures. The experimental results indicated that the structural and functional properties of HHP-pretreated RBPH improved.

2008 ◽  
Vol 87 (3) ◽  
pp. 363-370 ◽  
Author(s):  
J. Octavio Rodiles-López ◽  
Ma. Eugenia Jaramillo-Flores ◽  
Gustavo F. Gutiérrez-López ◽  
Andrés Hernández-Arana ◽  
Rosa E. Fosado-Quiroz ◽  
...  

2016 ◽  
Vol 33 (No. 5) ◽  
pp. 474-479 ◽  
Author(s):  
J. Ren ◽  
Ch. Song ◽  
P. Wang ◽  
S. Li ◽  
N. Kopparapu ◽  
...  

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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