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The effect of heat treatment on the soluble protein content of oats

Runyon, Ray LU ; Sunilkumar, Bindu A LU ; Nilsson, Lars LU ; Rascon, Ana LU and Bergenståhl, Björn LU (2015) In Journal of Cereal Science 65. p.119-124
Abstract
The effect of heat treatment on the soluble protein content in oat groats (Kerstin commercial variety) was evaluated using asymmetric flow field-flow fractionation (AF4) in combination with online multiangle light scattering (MALS) and UV detection. The AF4 method was used to separate the monomeric proteins from globulin hexamer and aggregate proteins and beta-glucan polysaccharides in the soluble oat protein fraction. The total amount of soluble protein (with respect to total protein) was reduced to 35.7 +/-- 4.5 wt. % in heat treated oats from 74.6 +/- 5.3 wt. % in non-heat treated oats. The ratio of monomeric to globulin hexamer and aggregate proteins was reduced from 1.82 to 1.48 as a result of heat treatment. Sodium-dodecyl-sulfate... (More)
The effect of heat treatment on the soluble protein content in oat groats (Kerstin commercial variety) was evaluated using asymmetric flow field-flow fractionation (AF4) in combination with online multiangle light scattering (MALS) and UV detection. The AF4 method was used to separate the monomeric proteins from globulin hexamer and aggregate proteins and beta-glucan polysaccharides in the soluble oat protein fraction. The total amount of soluble protein (with respect to total protein) was reduced to 35.7 +/-- 4.5 wt. % in heat treated oats from 74.6 +/- 5.3 wt. % in non-heat treated oats. The ratio of monomeric to globulin hexamer and aggregate proteins was reduced from 1.82 to 1.48 as a result of heat treatment. Sodium-dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed the selective elimination of protein bands associated with the albumin and prolamin protein fractions as a result of heat treatment. These results were supported through amino acid analysis by cation exchange chromatography coupled with UV detection which revealed a reduction in amino acid residues associated with prolamin. The globulin proteins were found to be less sensitive to heat treatment. (C) 2015 Elsevier Ltd. All rights reserved. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Light scattering, Field-flow fractionation, Heat treatment, Protein, aggregates, Oat proteins, Beta glucans
in
Journal of Cereal Science
volume
65
pages
119 - 124
publisher
Elsevier
external identifiers
  • wos:000363355600018
  • scopus:84942568492
ISSN
0733-5210
DOI
10.1016/j.jcs.2015.06.008
language
English
LU publication?
yes
id
110bc4e8-7a03-43b4-bdde-f6509605aa57 (old id 8201593)
date added to LUP
2016-04-01 09:59:31
date last changed
2023-11-09 09:22:16
@article{110bc4e8-7a03-43b4-bdde-f6509605aa57,
  abstract     = {{The effect of heat treatment on the soluble protein content in oat groats (Kerstin commercial variety) was evaluated using asymmetric flow field-flow fractionation (AF4) in combination with online multiangle light scattering (MALS) and UV detection. The AF4 method was used to separate the monomeric proteins from globulin hexamer and aggregate proteins and beta-glucan polysaccharides in the soluble oat protein fraction. The total amount of soluble protein (with respect to total protein) was reduced to 35.7 +/-- 4.5 wt. % in heat treated oats from 74.6 +/- 5.3 wt. % in non-heat treated oats. The ratio of monomeric to globulin hexamer and aggregate proteins was reduced from 1.82 to 1.48 as a result of heat treatment. Sodium-dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed the selective elimination of protein bands associated with the albumin and prolamin protein fractions as a result of heat treatment. These results were supported through amino acid analysis by cation exchange chromatography coupled with UV detection which revealed a reduction in amino acid residues associated with prolamin. The globulin proteins were found to be less sensitive to heat treatment. (C) 2015 Elsevier Ltd. All rights reserved.}},
  author       = {{Runyon, Ray and Sunilkumar, Bindu A and Nilsson, Lars and Rascon, Ana and Bergenståhl, Björn}},
  issn         = {{0733-5210}},
  keywords     = {{Light scattering; Field-flow fractionation; Heat treatment; Protein; aggregates; Oat proteins; Beta glucans}},
  language     = {{eng}},
  pages        = {{119--124}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Cereal Science}},
  title        = {{The effect of heat treatment on the soluble protein content of oats}},
  url          = {{http://dx.doi.org/10.1016/j.jcs.2015.06.008}},
  doi          = {{10.1016/j.jcs.2015.06.008}},
  volume       = {{65}},
  year         = {{2015}},
}