Characterization of gliadin, secalin and hordein fractions using analytical techniques

Characterization of gliadin, secalin and hordein fractions using analytical techniques

Abstract Prolamins, alcohol soluble storage proteins of the Triticeae tribe of Gramineae family, are known as gliadin, secalin and hordein in wheat, rye and barley respectively. Prolamins were extracted from fifteen cultivars using DuPont protocol to study their physiochemical, morphological and str...

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Autores principales: Monika Rani, Dalbir Singh Sogi, Balmeet Singh Gill
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
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R
Science
Q
Acceso en línea:https://doaj.org/article/5d567f4fecab467ab2012d2b78293cc4
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spelling oai:doaj.org-article:5d567f4fecab467ab2012d2b78293cc42021-12-05T12:14:56ZCharacterization of gliadin, secalin and hordein fractions using analytical techniques10.1038/s41598-021-02099-02045-2322https://doaj.org/article/5d567f4fecab467ab2012d2b78293cc42021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-02099-0https://doaj.org/toc/2045-2322Abstract Prolamins, alcohol soluble storage proteins of the Triticeae tribe of Gramineae family, are known as gliadin, secalin and hordein in wheat, rye and barley respectively. Prolamins were extracted from fifteen cultivars using DuPont protocol to study their physiochemical, morphological and structural characteristics. SDS-PAGE of prolamins showed well resolved low molecular weight proteins with significant amount of albumin and globulin as cross-contaminant. The β-sheet (32.72–37.41%) and β-turn (30.36–37.91%) were found higher in gliadins, while α-helix (20.32–28.95%) and random coil (9.05–10.28%) in hordeins. The high colloidal stability as depicted by zeta-potential was observed in gliadins (23.5–27.0 mV) followed secalins (11.2–16.6 mV) and hordeins (4.1–7.8 mV). Surface morphology by SEM illustrated the globular particle arrangement in gliadins, sheet like arrangement in secalins and stacked flaky particle arrangement in hordeins fraction. TEM studies showed that secalin and hordein fractions were globular in shape while gliadins in addition to globular structure also possessed rod-shaped particle arrangement. XRD pattern of prolamin fractions showed the ordered crystalline domain at 2θ values of 44.1°, 37.8° and 10.4°. The extracted prolamins fractions showed amorphous as well as crystalline structures as revealed by XRD and TEM analysis. Space saving hexagonal molecular symmetry was also observed in TEM molecular arrangement of prolamins which has profound application in development of plant-based polymers and fibres.Monika RaniDalbir Singh SogiBalmeet Singh GillNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-19 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Monika Rani
Dalbir Singh Sogi
Balmeet Singh Gill
Characterization of gliadin, secalin and hordein fractions using analytical techniques
description Abstract Prolamins, alcohol soluble storage proteins of the Triticeae tribe of Gramineae family, are known as gliadin, secalin and hordein in wheat, rye and barley respectively. Prolamins were extracted from fifteen cultivars using DuPont protocol to study their physiochemical, morphological and structural characteristics. SDS-PAGE of prolamins showed well resolved low molecular weight proteins with significant amount of albumin and globulin as cross-contaminant. The β-sheet (32.72–37.41%) and β-turn (30.36–37.91%) were found higher in gliadins, while α-helix (20.32–28.95%) and random coil (9.05–10.28%) in hordeins. The high colloidal stability as depicted by zeta-potential was observed in gliadins (23.5–27.0 mV) followed secalins (11.2–16.6 mV) and hordeins (4.1–7.8 mV). Surface morphology by SEM illustrated the globular particle arrangement in gliadins, sheet like arrangement in secalins and stacked flaky particle arrangement in hordeins fraction. TEM studies showed that secalin and hordein fractions were globular in shape while gliadins in addition to globular structure also possessed rod-shaped particle arrangement. XRD pattern of prolamin fractions showed the ordered crystalline domain at 2θ values of 44.1°, 37.8° and 10.4°. The extracted prolamins fractions showed amorphous as well as crystalline structures as revealed by XRD and TEM analysis. Space saving hexagonal molecular symmetry was also observed in TEM molecular arrangement of prolamins which has profound application in development of plant-based polymers and fibres.
format article
author Monika Rani
Dalbir Singh Sogi
Balmeet Singh Gill
author_facet Monika Rani
Dalbir Singh Sogi
Balmeet Singh Gill
author_sort Monika Rani
title Characterization of gliadin, secalin and hordein fractions using analytical techniques
title_short Characterization of gliadin, secalin and hordein fractions using analytical techniques
title_full Characterization of gliadin, secalin and hordein fractions using analytical techniques
title_fullStr Characterization of gliadin, secalin and hordein fractions using analytical techniques
title_full_unstemmed Characterization of gliadin, secalin and hordein fractions using analytical techniques
title_sort characterization of gliadin, secalin and hordein fractions using analytical techniques
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/5d567f4fecab467ab2012d2b78293cc4
work_keys_str_mv AT monikarani characterizationofgliadinsecalinandhordeinfractionsusinganalyticaltechniques
AT dalbirsinghsogi characterizationofgliadinsecalinandhordeinfractionsusinganalyticaltechniques
AT balmeetsinghgill characterizationofgliadinsecalinandhordeinfractionsusinganalyticaltechniques
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