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Genomic identification of expressed globulin storage proteins in oat

Gil-González, Aina Belén ; Sjögren, Lars L.E. ; Bernfur, Katja LU ; Olsson, Olof LU and Zambrano, Jose Alfredo LU (2024) In Frontiers in Plant Science 15.
Abstract

Introduction: Oats, a highly nutritious cereal known for their health benefits, contain various macromolecules of significant biological value, including abundant and highly digestible proteins. Despite their importance, oat proteins have not been extensively studied. Here, we present a complete set of the expressed globulins genes, which code for the main storage protein in oats as well as their chromosomal positions. Methods: Published expressed sequence tags for globulins were used as queries in the Sang oat genome. In addition, globulin proteins were fractionated from oat flour by solvent extraction based on differential solubility with other classes of cereal proteins. The protein fractions were separated by gel electrophoresis and... (More)

Introduction: Oats, a highly nutritious cereal known for their health benefits, contain various macromolecules of significant biological value, including abundant and highly digestible proteins. Despite their importance, oat proteins have not been extensively studied. Here, we present a complete set of the expressed globulins genes, which code for the main storage protein in oats as well as their chromosomal positions. Methods: Published expressed sequence tags for globulins were used as queries in the Sang oat genome. In addition, globulin proteins were fractionated from oat flour by solvent extraction based on differential solubility with other classes of cereal proteins. The protein fractions were separated by gel electrophoresis and analyzed by tandem mass spectrometry to confirm their identity and expression in seed. Results and discussion: In total 32 globulin gene sequences were identified on the oat genome. Out of these, the expression on RNA level could be confirmed and 27 were also detected as expressed proteins by MS. Our results provide the most extensive set of salt-soluble oat globulin sequences to date, paving the way for further understanding their implications for human nutrition. In addition, a simple methodology to fractionate oat proteins is presented.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Avena sativa, cereal proteins, globulins, mass spectrometry, Osborne fractionation, protein isolation
in
Frontiers in Plant Science
volume
15
article number
1418658
publisher
Frontiers Media S. A.
external identifiers
  • scopus:85200483293
  • pmid:39109060
ISSN
1664-462X
DOI
10.3389/fpls.2024.1418658
language
English
LU publication?
yes
id
16ae525b-27e7-4f80-ae01-add25687f6f0
date added to LUP
2024-11-11 14:25:55
date last changed
2025-07-08 09:59:08
@article{16ae525b-27e7-4f80-ae01-add25687f6f0,
  abstract     = {{<p>Introduction: Oats, a highly nutritious cereal known for their health benefits, contain various macromolecules of significant biological value, including abundant and highly digestible proteins. Despite their importance, oat proteins have not been extensively studied. Here, we present a complete set of the expressed globulins genes, which code for the main storage protein in oats as well as their chromosomal positions. Methods: Published expressed sequence tags for globulins were used as queries in the Sang oat genome. In addition, globulin proteins were fractionated from oat flour by solvent extraction based on differential solubility with other classes of cereal proteins. The protein fractions were separated by gel electrophoresis and analyzed by tandem mass spectrometry to confirm their identity and expression in seed. Results and discussion: In total 32 globulin gene sequences were identified on the oat genome. Out of these, the expression on RNA level could be confirmed and 27 were also detected as expressed proteins by MS. Our results provide the most extensive set of salt-soluble oat globulin sequences to date, paving the way for further understanding their implications for human nutrition. In addition, a simple methodology to fractionate oat proteins is presented.</p>}},
  author       = {{Gil-González, Aina Belén and Sjögren, Lars L.E. and Bernfur, Katja and Olsson, Olof and Zambrano, Jose Alfredo}},
  issn         = {{1664-462X}},
  keywords     = {{Avena sativa; cereal proteins; globulins; mass spectrometry; Osborne fractionation; protein isolation}},
  language     = {{eng}},
  publisher    = {{Frontiers Media S. A.}},
  series       = {{Frontiers in Plant Science}},
  title        = {{Genomic identification of expressed globulin storage proteins in oat}},
  url          = {{http://dx.doi.org/10.3389/fpls.2024.1418658}},
  doi          = {{10.3389/fpls.2024.1418658}},
  volume       = {{15}},
  year         = {{2024}},
}