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Research Article
MONIKA Rani
Guru Nanak Dev University
Corresponding Author
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Prolamins extracted from wheat, rye and barley cultivars were analysed for colour characteristics, SDS-PAGE, Amino Acid, Dynamic Light Scattering (DLS), Zeta Potential, Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX), Transmission Electron Microscopy (TEM) and X-ray Diffraction (XRD) to elucidate the structure. Amino acid analysis showed significant variation among the prolamins and the predominant essential amino acids were found to be leucine, phenylalanine and valine whereas predominant non-essential amino acids were glutamic acid, arginine and aspartic acid. All the prolamins exhibited positive zeta-potential, however gliadin had a significantly higher zeta potential value. TEM studies of prolamins revealed the compact globular structure but gliadin also had rod-shaped structure. Morphology by SEM illustrated the globular particle arrangement in gliadin and sheet like arrangement in secalin and hordein. XRD pattern of prolamin showed the ordered crystalline domain of prolamin at 44.1°, 37.8° and 10.4°. The d-spacing obtained from XRD and TEM analysis also supports the crystalline domain of prolamin apart from amorphous domain.
Keywords
Prolamin, SDS-PAGE, Amino acid, Dynamic light scattering, SEM, TEM, X-Ray Diffraction
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Reviewer #5 agreed
On 22 Mar, 2021
Reviewer #8 agreed
On 22 Mar, 2021
Reviewer #3 agreed
On 22 Mar, 2021
Reviewer #4 agreed
On 22 Mar, 2021
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This preprint is under consideration at Scientific Reports. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research Article
MONIKA Rani
Guru Nanak Dev University
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 11 Mar, 2021
No community comments so far
Review #3 received
Received 07 Apr, 2021
Review #1 received
Received 07 Apr, 2021
Review #2 received
Received 07 Apr, 2021
Reviewer #9 agreed
On 22 Mar, 2021
Reviewer #2 agreed
On 22 Mar, 2021
Reviewer #1 agreed
On 22 Mar, 2021
Reviewer #12 agreed
On 22 Mar, 2021
Reviewer #7 agreed
On 22 Mar, 2021
Reviewer #6 agreed
On 22 Mar, 2021
Reviewer #10 agreed
On 22 Mar, 2021
Reviewer #11 agreed
On 22 Mar, 2021
Reviewer #5 agreed
On 22 Mar, 2021
Reviewer #8 agreed
On 22 Mar, 2021
Reviewer #3 agreed
On 22 Mar, 2021
Reviewer #4 agreed
On 22 Mar, 2021
Reviewers invited
Invitations sent on 22 Mar, 2021
Editor assigned
On 19 Mar, 2021
Editor invited
On 09 Mar, 2021
Submission checks complete
On 08 Mar, 2021
First submitted
On 26 Feb, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
Prolamins extracted from wheat, rye and barley cultivars were analysed for colour characteristics, SDS-PAGE, Amino Acid, Dynamic Light Scattering (DLS), Zeta Potential, Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX), Transmission Electron Microscopy (TEM) and X-ray Diffraction (XRD) to elucidate the structure. Amino acid analysis showed significant variation among the prolamins and the predominant essential amino acids were found to be leucine, phenylalanine and valine whereas predominant non-essential amino acids were glutamic acid, arginine and aspartic acid. All the prolamins exhibited positive zeta-potential, however gliadin had a significantly higher zeta potential value. TEM studies of prolamins revealed the compact globular structure but gliadin also had rod-shaped structure. Morphology by SEM illustrated the globular particle arrangement in gliadin and sheet like arrangement in secalin and hordein. XRD pattern of prolamin showed the ordered crystalline domain of prolamin at 44.1°, 37.8° and 10.4°. The d-spacing obtained from XRD and TEM analysis also supports the crystalline domain of prolamin apart from amorphous domain.
Figure 1
Figure 2
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