Physicochemical Properties and Functionality of Rice Bran Protein Hydrolyzate Prepared from Heat-stabilized Defatted Rice Bran with the Aid of Enzymes

The hypolipidemic properties of defatted rice bran protein (DRBP), fresh rice bran protein (FRBP), DRBP hydrolysates (DRBPH), and FRBP hydrolysates (FRBPH) were determined in mice on high fat diets for four weeks.

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Effects of electrocatalytic treatment on the physicochemical properties of rice bran protein

Journal of Food Measurement & Characterization ◽

10.1007/s11694-021-01227-8 ◽

2021 ◽

Author(s):

Dan Li ◽

Rongchun Wang ◽

Dianyu Yu ◽

WeiHong Lu ◽

Ying Ma

Keyword(s):

Physicochemical Properties ◽

Rice Bran ◽

Rice Bran Protein

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Antioxidant, Angiotensin-Converting Enzyme Inhibitory Properties and Blood-Pressure-Lowering Effect of Rice Bran Protein Hydrolysates

Foods ◽

10.3390/foods9060812 ◽

2020 ◽

Vol 9 (6) ◽

pp. 812

Author(s):

Inajara Beatriz Brose Piotrowicz ◽

Marta Garcés-Rimón ◽

Silvia Moreno-Fernández ◽

Amaya Aleixandre ◽

Myriam Salas-Mellado ◽

...

Keyword(s):

Blood Pressure ◽

Angiotensin Converting Enzyme ◽

Rice Bran ◽

Inhibitory Activity ◽

Converting Enzyme ◽

Ace Inhibitory Activity ◽

Rice Bran Protein ◽

Defatted Rice Bran ◽

Wky Rats ◽

Ace Inhibitory

This research aimed to investigate the biological properties of different hydrolysates derived from industrial and laboratory defatted rice bran proteins. Industrial and laboratory defatted rice bran protein concentrates were hydrolyzed with alcalase or flavorzyme. The degree of hydrolysis (DH), oxygen radical absorbance capacity (ORAC), reducing power, total phenolic compounds (TPC), and angiotensin-converting enzyme (ACE) inhibitory activity, were determined in the hydrolysates and the molecular fractions lower than 3 kDa. Systolic blood pressure (SBP) was measured using the tail-cuff method before and after oral administration of 80 mg/kg of different rice bran protein hydrolysate (RBPH) fractions lower than 3 kDa in male spontaneously hypertensive rats (SHR) and normotensive Wistar–Kyoto (WKY) rats. The highest values of in vitro antioxidant activity and TPC were observed in RBPH with alcalase defatted by industry (RBPH2A), and, in all cases, these bioactivities were higher in the molecular fractions lower than 3 kDa. Once again, fractions lower than 3 kDa obtained with alcalase showed a potent ACE inhibitory activity (RBPH1A<3 and RBPH2A<3). The administration of RBPH1A<3 caused a significant decrease in the SBP in SHR, where the maximum decrease was reached at 8 h after administration. SBP in WKY rats was not modified after the administration of RBPH1A<3. These results suggest that the rice bran protein hydrolysates obtained from industry after treatment with alcalase could be an interesting source of bioactive peptides, with potential action on hypertension and other related pathologies.

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Comparison of Two Methods for the Extraction of Fractionated Rice Bran Protein

Journal of Chemistry ◽

10.1155/2014/546345 ◽

2014 ◽

Vol 2014 ◽

pp. 1-10 ◽

Cited By ~ 8

Author(s):

Changyuan Wang ◽

Dan Li ◽

Feng Xu ◽

Tianshu Hao ◽

Min Zhang

Keyword(s):

Rice Bran ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Surface Hydrophobicity ◽

Denaturation Temperature ◽

Scanning Calorimetry ◽

Rice Bran Protein ◽

Defatted Rice Bran ◽

Protein Surface Hydrophobicity ◽

Extraction Solvents

Two different methods for extracting fractionated rice bran protein (FRBP) from defatted rice bran were investigated according to the solubility of protein in different extraction solvents. The yields of the obtained proteins and their purity were first compared. Sodium dodecyl sulfate polyacrylamide gel electrophoresis, differential scanning calorimetry, protein surface hydrophobicity, and protein secondary molecular structure analyses were subsequently applied to identify and compare the compositional, structural, and functional characteristics of the obtained proteins. The highest yield (13.8%, w/w) and purity (45–47%) of FRBP products were obtained using 0.4 M NaCl, 80% ethanol, and 0.01 M NaOH as extraction solvents to fractionate albumin, globulin, prolamin, and glutelin. Several good properties were exhibited, including good functionality, specific denaturation temperature, and enthalpy values, for FRBP products prepared by the above method.

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