Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed

Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed

Abstract In this work, we sequentially extracted water (CSPw)- and alkali (CSPa)-soluble protein fractions from glandless cottonseed. SDS-Gel electrophoresis separated CSPw and CSPa to 8 and 14 dominant polypeptide bands (110–10 kDa), respectively. Liquid chromatography-electrospray ionization-tande...

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Autores principales: Zhongqi He, Christopher P. Mattison, Dunhua Zhang, Casey C. Grimm
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/fc6ca81c4f354467b2ff393a935735ce
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spelling oai:doaj.org-article:fc6ca81c4f354467b2ff393a935735ce2021-12-02T16:55:24ZVicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed10.1038/s41598-021-88527-72045-2322https://doaj.org/article/fc6ca81c4f354467b2ff393a935735ce2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-88527-7https://doaj.org/toc/2045-2322Abstract In this work, we sequentially extracted water (CSPw)- and alkali (CSPa)-soluble protein fractions from glandless cottonseed. SDS-Gel electrophoresis separated CSPw and CSPa to 8 and 14 dominant polypeptide bands (110–10 kDa), respectively. Liquid chromatography-electrospray ionization-tandem mass spectrometry identified peptide fragments from 336 proteins. While the majority of peptides were identified as belonging to vicilin and legumin storage proteins, peptides from other functional and uncharacterized proteins were also detected. Based on the types (unique peptide count) and relative abundance (normalized total ion current) of the polypeptides detected by mass spectrometry, we found lower levels (abundance) and types of legumin isoforms, but higher levels and more fragments of vicilin-like antimicrobial peptides in glandless samples, compared to glanded samples. Differences in peptide fragment patterns of 2S albumin and oleosin were also observed between glandless and glanded protein samples. These differences might be due to the higher extraction recovery of proteins from glandless cottonseed as proteins from glanded cottonseed tend to be associated with gossypol, reducing extraction efficiency. This work enriches the fundamental knowledge of glandless cottonseed protein composition. For practical considerations, this peptide information will be helpful to allow better understanding of the functional and physicochemical properties of glandless cottonseed protein, and improving the potential for food or feed applications.Zhongqi HeChristopher P. MattisonDunhua ZhangCasey C. GrimmNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Zhongqi He
Christopher P. Mattison
Dunhua Zhang
Casey C. Grimm
Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed
description Abstract In this work, we sequentially extracted water (CSPw)- and alkali (CSPa)-soluble protein fractions from glandless cottonseed. SDS-Gel electrophoresis separated CSPw and CSPa to 8 and 14 dominant polypeptide bands (110–10 kDa), respectively. Liquid chromatography-electrospray ionization-tandem mass spectrometry identified peptide fragments from 336 proteins. While the majority of peptides were identified as belonging to vicilin and legumin storage proteins, peptides from other functional and uncharacterized proteins were also detected. Based on the types (unique peptide count) and relative abundance (normalized total ion current) of the polypeptides detected by mass spectrometry, we found lower levels (abundance) and types of legumin isoforms, but higher levels and more fragments of vicilin-like antimicrobial peptides in glandless samples, compared to glanded samples. Differences in peptide fragment patterns of 2S albumin and oleosin were also observed between glandless and glanded protein samples. These differences might be due to the higher extraction recovery of proteins from glandless cottonseed as proteins from glanded cottonseed tend to be associated with gossypol, reducing extraction efficiency. This work enriches the fundamental knowledge of glandless cottonseed protein composition. For practical considerations, this peptide information will be helpful to allow better understanding of the functional and physicochemical properties of glandless cottonseed protein, and improving the potential for food or feed applications.
format article
author Zhongqi He
Christopher P. Mattison
Dunhua Zhang
Casey C. Grimm
author_facet Zhongqi He
Christopher P. Mattison
Dunhua Zhang
Casey C. Grimm
author_sort Zhongqi He
title Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed
title_short Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed
title_full Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed
title_fullStr Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed
title_full_unstemmed Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed
title_sort vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/fc6ca81c4f354467b2ff393a935735ce
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AT christopherpmattison vicilinandleguminstorageproteinsareabundantinwaterandalkalisolubleproteinfractionsofglandlesscottonseed
AT dunhuazhang vicilinandleguminstorageproteinsareabundantinwaterandalkalisolubleproteinfractionsofglandlesscottonseed
AT caseycgrimm vicilinandleguminstorageproteinsareabundantinwaterandalkalisolubleproteinfractionsofglandlesscottonseed
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