Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions

Introduction. Gliadin proteins are one of the gluten fractions. They are soluble in alcoholic solution and divided into four groups (α + β, γ, ω1.2, and ω5-gliadins). In this paper gliadins were extracted from wheat flour, and optimal conditions for their separation were determined. Study objects a...

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Main Authors: Radoslav Grujić, Vesna Gojković Cvjetković, Željka Marjanović-Balaban
Format: Article
Language:English
Published: Kemerovo State University 2020-10-01
Series:Foods and Raw Materials
Subjects:
Online Access:http://jfrm.ru/files/archive/16/Gruji%C4%87.pdf
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spelling doaj-2ddae65c30d24155b72bc5f59aa1b7852020-11-25T04:00:00ZengKemerovo State UniversityFoods and Raw Materials2308-40572310-95992020-10-018241142110.21603/2308-4057-2020-2-411-421Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditionsRadoslav Grujić0Vesna Gojković Cvjetković1https://orcid.org/0000-0003-1118-4565Željka Marjanović-Balaban2State High School of Medical ScienceUniversity of East SarajevoUniversity of Banja LukaIntroduction. Gliadin proteins are one of the gluten fractions. They are soluble in alcoholic solution and divided into four groups (α + β, γ, ω1.2, and ω5-gliadins). In this paper gliadins were extracted from wheat flour, and optimal conditions for their separation were determined. Study objects and methods. The separation was performed by capillary gel electrophoresis on Agilent apparatus, CE 7100 (a capillary with an inner diameter of 50 μm, a total length of 33 cm, and an effective length of 23.50 cm). In order to determine the optimal conditions, different solvent concentrations (50, 60, and 70% ethanol), capillary temperatures (20, 25, 30, 35, and 40°C), and electrode voltages (–14.5, –16.5, –17.5 and –18.5 kV) were applied. Migration time and relative concentration of each protein molecules within gliadin fractions in the electrophoregram were analysed using Agilent ChemStation Software. Results and discussion. The optimal conditions for gliadin separation were: solvent 70% (v/v) ethanol, capillary temperature of 25°C, and electrode voltage of –16.5 kV. Under these conditions, the total proteins were indetified as Xav = 23.50, including α + β gliadin fraction (Xav = 7.50 and relative concentration RC = 28.29%), γ-gliadins (Xav = 5.00, RC = 26.66%), ω1.2-gliadins (Xav = 4.33, RC = 14.93%), and ω5-gliadins (Xav = 6.67, RC = 30.98%). Conclusion. The results of the research can be of fundamental importance in the study of gluten proteins and the influence of technological procedures on their change and the possibility of reducing the allergic effect of gluten during processing.http://jfrm.ru/files/archive/16/Gruji%C4%87.pdfproteinswheatextractionethanolelectrophoresisgluten
collection DOAJ
language English
format Article
sources DOAJ
author Radoslav Grujić
Vesna Gojković Cvjetković
Željka Marjanović-Balaban
spellingShingle Radoslav Grujić
Vesna Gojković Cvjetković
Željka Marjanović-Balaban
Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions
Foods and Raw Materials
proteins
wheat
extraction
ethanol
electrophoresis
gluten
author_facet Radoslav Grujić
Vesna Gojković Cvjetković
Željka Marjanović-Balaban
author_sort Radoslav Grujić
title Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions
title_short Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions
title_full Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions
title_fullStr Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions
title_full_unstemmed Separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions
title_sort separation of gliadins from wheat flour by capillary gel electrophoresis: optimal conditions
publisher Kemerovo State University
series Foods and Raw Materials
issn 2308-4057
2310-9599
publishDate 2020-10-01
description Introduction. Gliadin proteins are one of the gluten fractions. They are soluble in alcoholic solution and divided into four groups (α + β, γ, ω1.2, and ω5-gliadins). In this paper gliadins were extracted from wheat flour, and optimal conditions for their separation were determined. Study objects and methods. The separation was performed by capillary gel electrophoresis on Agilent apparatus, CE 7100 (a capillary with an inner diameter of 50 μm, a total length of 33 cm, and an effective length of 23.50 cm). In order to determine the optimal conditions, different solvent concentrations (50, 60, and 70% ethanol), capillary temperatures (20, 25, 30, 35, and 40°C), and electrode voltages (–14.5, –16.5, –17.5 and –18.5 kV) were applied. Migration time and relative concentration of each protein molecules within gliadin fractions in the electrophoregram were analysed using Agilent ChemStation Software. Results and discussion. The optimal conditions for gliadin separation were: solvent 70% (v/v) ethanol, capillary temperature of 25°C, and electrode voltage of –16.5 kV. Under these conditions, the total proteins were indetified as Xav = 23.50, including α + β gliadin fraction (Xav = 7.50 and relative concentration RC = 28.29%), γ-gliadins (Xav = 5.00, RC = 26.66%), ω1.2-gliadins (Xav = 4.33, RC = 14.93%), and ω5-gliadins (Xav = 6.67, RC = 30.98%). Conclusion. The results of the research can be of fundamental importance in the study of gluten proteins and the influence of technological procedures on their change and the possibility of reducing the allergic effect of gluten during processing.
topic proteins
wheat
extraction
ethanol
electrophoresis
gluten
url http://jfrm.ru/files/archive/16/Gruji%C4%87.pdf
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