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

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
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.

Effects of ultrasound extraction on the physicochemical and emulsifying properties of rice bran protein

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Li-Hui Sun ◽  
Feng Yu ◽  
Yu-Ying Wang ◽  
Shi-Wen Lv ◽  
Lei-Yu He
Keyword(s):  
Rice Bran ◽  
Protein Solubility ◽  
Surface Hydrophobicity ◽  
Absorption Capacity ◽  
Emulsifying Properties ◽  
Ultrasound Assisted Extraction ◽  
Suitable Alternative ◽  
Rice Bran Protein ◽  
Assisted Extraction ◽  
Ultrasound Assisted

Abstract In this study, rice bran protein was prepared by ultrasound-assisted extraction, and its physicochemical and emulsifying properties were also evaluated. Results demonstrated that a significant increase in protein yield was observed when ultrasound-assisted method was employed for extracting protein. Noticeably, obtained rice bran protein possessed excellent physicochemical properties, such as oil absorption capacity, protein solubility and foaming property. More hydrophobic groups were exposed in the process of ultrasound-assisted extraction, which led to the increase of surface hydrophobicity. More importantly, the ultrasound-assisted extraction could improve emulsifying properties of rice bran protein, and the emulsions prepared using protein samples exhibited the great stability. Besides, it was also found that emulsifying properties of protein samples presented a decrease trend with increasing ultrasound power and time. All in all, ultrasound-assisted extraction is a suitable alternative process for preparing rice bran protein.

scholarly journals Simultaneous Ultrasound and Heat Enhance Functional Properties of Glycosylated Lactoferrin

Molecules ◽  
2020 ◽  
Vol 25 (23) ◽  
pp. 5774
Author(s):  
Zhipeng Li ◽  
Dexue Ma ◽  
Yiyang He ◽  
Siqi Guo ◽  
Fuguo Liu ◽  
...  
Keyword(s):  
Functional Properties ◽  
Maillard Reaction ◽  
Spatial Configuration ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Surface Hydrophobicity ◽  
Orthogonal Experimental Design ◽  
Maillard Reaction Products ◽  
Reaction Products ◽  
Ultrasound Assisted

Protein-polysaccharide covalent complexes exhibit better physicochemical and functional properties than single protein or polysaccharide. To promote the formation of the covalent complex from lactoferrin (LF) and beet pectin (BP), we enhanced the Maillard reaction between LF and BP by using an ultrasound-assisted treatment and studied the structure and functional properties of the resulting product. The reaction conditions were optimized by an orthogonal experimental design, and the highest grafting degree of 55.36% was obtained by ultrasonic treatment at 300 W for 20 min and at LF concentration of 20 g/L and BP concentration of 9 g/L. The formation of LF-BP conjugates was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FTIR) spectroscopy. Ultrasound-assisted treatment can increase the surface hydrophobicity, browning index, 1,1-diphenyl-2-picryl-hydrazyl (DPPH) and 2,2’-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) free radicals scavenging activity of LF due to the changes in the spatial configuration and formation of Maillard reaction products. The thermal stability, antioxidant activity and emulsifying property of LF were significantly improved after combining with BP. These findings reveal the potential application of modified proteins by ultrasonic and heat treatment.

scholarly journals Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

Marine Drugs ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 178 ◽  
Author(s):  
Baosheng Ge ◽  
Haonan Wang ◽  
Jie Li ◽  
Hengheng Liu ◽  
Yonghao Yin ◽  
...  
Keyword(s):  
Wound Dressing ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wound Dressings ◽  
Type I ◽  
Rheological Characterization ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Collagen Hydrogels

Collagen plays an important role in the formation of extracellular matrix (ECM) and development/migration of cells and tissues. Here we report the preparation of collagen and collagen hydrogel from the skin of tilapia and an evaluation of their potential as a wound dressing for the treatment of refractory wounds. The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) analysis. Both ASC and PSC belong to type I collagen and have a complete triple helix structure, but PSC shows lower molecular weight and thermal stability, and has the inherent low antigenicity. Therefore, PSC was selected to prepare biomedical hydrogels using its self-aggregating properties. Rheological characterization showed that the mechanical strength of the hydrogels increased as the PSC content increased. Scanning electron microscope (SEM) analysis indicated that hydrogels could form a regular network structure at a suitable PSC content. Cytotoxicity experiments confirmed that hydrogels with different PSC content showed no significant toxicity to fibroblasts. Skin repair experiments and pathological analysis showed that the collagen hydrogels wound dressing could significantly accelerate the healing of deep second-degree burn wounds and the generation of new skin appendages, which can be used for treatment of various refractory wounds.

Rice bran proteins and their hydrolysates modulate cholesterol metabolism in mice on hypercholesterolemic diets

2016 ◽  
Vol 7 (6) ◽  
pp. 2747-2753 ◽  
Author(s):  
Huijuan Zhang ◽  
Jing Wang ◽  
Yingli Liu ◽  
Lingxiao Gong ◽  
Baoguo Sun
Keyword(s):  
Rice Bran ◽  
Cholesterol Metabolism ◽  
High Fat ◽  
Rice Bran Protein ◽  
Defatted Rice Bran ◽  
High Fat Diets ◽  
Fat Diets

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.

Effect of rice bran protein concentrate as wall material adjunct on selected physicochemical and release properties of microencapsulated β-carotene

2021 ◽  
pp. 108201322110496
Author(s):  
Maria Jannell Feliz A Magnaye ◽  
Lotis E Mopera ◽  
Floirendo P Flores
Keyword(s):  
Protein Content ◽  
Rice Bran ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Wall Material ◽  
Scanning Calorimetry ◽  
Rice Bran Protein ◽  
Rice Milling ◽  
Emulsifying Capacity ◽  
Β Carotene

Rice bran protein is an emerging protein source from rice milling that possesses health benefits and emulsifying capacity suitable for hypoallergenic encapsulation applications, especially for lipophilic compounds such as β-carotene. The purpose of this study is to develop and characterize β-carotene encapsulates with maltodextrin and rice bran protein. Rice bran protein was prepared using conventional alkali extraction. β-carotene was added to the composite wall materials (50:50 of 4%, 8%, 12%, and 16% solids content) and spray-dried. Encapsulation efficiency (85–98%) and radical scavenging activity (11–43%) varied proportionally with rice bran protein. Across increasing maltodextrin and rice bran protein content of the feed, carbohydrate content of the microcapsules varied proportionally (50–66%) but protein content was uniform (10–13%). Scanning electron microscopy, differential scanning calorimetry, and Fourier transform infrared spectroscopy data suggested successful encapsulation. Release profiles showed decreasing trend with increasing rice bran protein content; co-digestion with rice mitigated negative impacts of rice bran protein. Microcapsules with nutritive potential and health-promoting properties were developed as potential carotenoid delivery systems.

scholarly journals Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity

2019 ◽  
Vol 20 (16) ◽  
pp. 3931 ◽  
Author(s):  
Arely León-López ◽  
Lucía Fuentes-Jiménez ◽  
Alma Delia Hernández-Fuentes ◽  
Rafael G. Campos-Montiel ◽  
Gabriel Aguirre-Álvarez
Keyword(s):  
Molecular Weight ◽  
Antioxidant Activity ◽  
Isoelectric Point ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Amino Acid Content ◽  
Good Alternative ◽  
Hydrolysis Time ◽  
Scanning Calorimetry ◽  
Sem Images

The extraction and enzymatic hydrolysis of collagen from sheepskins at different times of hydrolysis (0, 10, 15, 20, 30 min, 1, 2, 3 and 4 h) were investigated in terms of amino acid content (hydroxyproline), isoelectric point, molecular weight (Mw) by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method, viscosity, Fourier-transform infrared (FTIR) spectroscopy, antioxidant capacity by 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) assays, thermal properties (Differential Scanning Calorimetry) and morphology by scanning electron microscopy (SEM) technique. The kinetics of hydrolysis showed an increase in the protein and hydroxyproline concentration as the hydrolysis time increased to 4 h. FTIR spectra allowed us to identify the functional groups of hydrolysed collagen (HC) in the amide I region for collagen. The isoelectric point shifted to lower values compared to the native collagen precursor. The change in molecular weight and viscosity from time 0 min to 4 h promoted important antioxidant activity in the resulting HC. The lower the Mw, the greater the ability to donate an electron or hydrogen to stabilize radicals. From the SEM images it was evident that HC after 2 h had a porous and spongy structure. These results suggest that HC could be a good alternative to replace HC from typical sources like pigs, cows and fish.

scholarly journals Two-Step Size-Exclusion Nanofiltration of Prothrombin Complex Concentrate Using Nanocellulose-Based Filter Paper

Biomedicines ◽  
2020 ◽  
Vol 8 (4) ◽  
pp. 69 ◽  
Author(s):  
Levon Manukyan ◽  
Athanasios Mantas ◽  
Mikhail Razumikhin ◽  
Andrey Katalevsky ◽  
Eugen Golubev ◽  
...  
Keyword(s):  
Filter Paper ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Coagulation Factor ◽  
Factor Ix ◽  
Size Exclusion ◽  
Step Size ◽  
Scanning Calorimetry ◽  
Virus Removal

Coagulation Factor IX-rich protrhombin complex concentrate (FIX-PCC) is a therapeutic biologic product that consists of a mixture of several human plasma-derived proteins, useful for treating hemophilia B. Due to its complex composition, FIX-PCC is very challenging to bioprocess through virus removing nanofilters in order to ensure its biosafety. This article describes a two-step filtration process of FIX-PCC using a nanocellulose-based filter paper with tailored porosity. The filters were characterized with scanning electron microscopy (SEM), cryoporometry with differential scanning calorimetry, and nitrogen gas sorption. Furthermore, in order to probe the filter’s cut-off size rejection threshold, removal of small- and large-size model viruses, i.e., ΦX174 (28 nm) and PR772 (70 nm), was evaluated. The feed, pre-filtrate, and permeate solutions were characterized with mass-spectrometric proteomic analysis, dynamic light scattering (DLS), sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and analytical size-exclusion high-performance liquid chromatography (SEHPLC). By sequential filtration through 11 μm pre-filter and 33 μm virus removal filter paper, it was possible to achieve high product throughput and high virus removal capacity. The presented approach could potentially be applied for bioprocessing other protein-based drugs.

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

Foods ◽  
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.

scholarly journals Heat-Induced Interactions between Whey Protein and Inulin and Changes in Physicochemical and Antioxidative Properties of the Complexes

2019 ◽  
Vol 20 (17) ◽  
pp. 4089
Author(s):  
Wang ◽  
Wang ◽  
Sun ◽  
Sun ◽  
Guo
Keyword(s):  
Whey Protein ◽  
Structural Changes ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Lower Surface ◽  
Surface Hydrophobicity ◽  
Antioxidative Properties ◽  
Dpph Scavenging ◽  
Far Ultraviolet

Whey protein and inulin at various weight ratios were dry heated at 60 °C for 5 days under relative humidity of 63%. The heated mixtures were found to have significant changes in browning intensity and zeta-potential compared to untreated mixture. Heated samples showed significantly lower surface hydrophobicity than untreated mixtures. Compared with untreated samples, dry-heated samples showed significantly higher 2,2-Diphenyl-1-Picrylhydrazyl (DPPH) scavenging ability with whey protein to inulin mass ratios of 1:2 and 1:3 and significantly higher 2,2′-Azinobis(2-Ethylbenzothiazoline-6-Sulfonate) (ABTS) scavenging abilities and oxygen radical absorbance capacity (ORAC) at all weight ratios. Dry heat-induced interactions between whey protein and inulin was confirmed by changes in Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) protein profile, Fourier Transform Infrared Spectroscopy (FT-IR) and Far-ultraviolet Circular Dichroism (Far-UV CD) spectra. Dry heating caused physicochemical and structural changes of whey protein and therefore the complexes can be used to improve the antioxidative properties of the mixture under certain conditions.

Sign in / Sign up

Export Citation Format

Share Document