Oat protein solubility and emulsion properties improved by enzymatic deamidation

Zhongqing Jiang, Tuula S. Sontag-Strohm, Hannu O. Salovaara, Juhani K. Sibakov, Päivi M. Kanerva, Jussi Loponen

Research output: Contribution to journalArticleScientificpeer-review

15 Citations (Scopus)

Abstract

Oat protein produced by a dry milling process was enzymatically deamidated by a food-grade protein-glutaminase (PG), and the effects on structure, solubility and emulsifying properties of oat proteins were studied. The reactions were conducted at neutral pH and low salt concentration conditions. Oat proteins were deamidated up to a deamidation degree of 59%. The solubility of proteins doubled. Oil-in-water emulsions prepared with the native and deamidated oat proteins differed as the emulsions prepared from oat proteins with high deamidation degree had a more uniform oil droplet particle size and longer stability. Fourier transform infrared (FT-IR) analysis demonstrated that oat protein secondary structure became more flexible by deamidation. Protein-glutaminase mediated deamidation appeared to be a promising technique to improve oat protein functionality such as emulsifying ability and solubility.
Original languageEnglish
Pages (from-to)126-132
JournalJournal of Cereal Science
Volume64
DOIs
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed

Fingerprint

oat protein
deamidation
emulsifying properties
protein solubility
Emulsions
Solubility
Proteins
glutaminase
Glutaminase
emulsions
solubility
dry milling
protein secondary structure
Oils
food grades
emulsifying
Secondary Protein Structure
Avena
salt concentration
droplets

Keywords

  • deamidation
  • emulsions
  • oat proteins
  • solubility

Cite this

Jiang, Z., Sontag-Strohm, T. S., Salovaara, H. O., Sibakov, J. K., Kanerva, P. M., & Loponen, J. (2015). Oat protein solubility and emulsion properties improved by enzymatic deamidation. Journal of Cereal Science, 64, 126-132. https://doi.org/10.1016/j.jcs.2015.04.010
Jiang, Zhongqing ; Sontag-Strohm, Tuula S. ; Salovaara, Hannu O. ; Sibakov, Juhani K. ; Kanerva, Päivi M. ; Loponen, Jussi. / Oat protein solubility and emulsion properties improved by enzymatic deamidation. In: Journal of Cereal Science. 2015 ; Vol. 64. pp. 126-132.
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abstract = "Oat protein produced by a dry milling process was enzymatically deamidated by a food-grade protein-glutaminase (PG), and the effects on structure, solubility and emulsifying properties of oat proteins were studied. The reactions were conducted at neutral pH and low salt concentration conditions. Oat proteins were deamidated up to a deamidation degree of 59{\%}. The solubility of proteins doubled. Oil-in-water emulsions prepared with the native and deamidated oat proteins differed as the emulsions prepared from oat proteins with high deamidation degree had a more uniform oil droplet particle size and longer stability. Fourier transform infrared (FT-IR) analysis demonstrated that oat protein secondary structure became more flexible by deamidation. Protein-glutaminase mediated deamidation appeared to be a promising technique to improve oat protein functionality such as emulsifying ability and solubility.",
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author = "Zhongqing Jiang and Sontag-Strohm, {Tuula S.} and Salovaara, {Hannu O.} and Sibakov, {Juhani K.} and Kanerva, {P{\"a}ivi M.} and Jussi Loponen",
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Jiang, Z, Sontag-Strohm, TS, Salovaara, HO, Sibakov, JK, Kanerva, PM & Loponen, J 2015, 'Oat protein solubility and emulsion properties improved by enzymatic deamidation', Journal of Cereal Science, vol. 64, pp. 126-132. https://doi.org/10.1016/j.jcs.2015.04.010

Oat protein solubility and emulsion properties improved by enzymatic deamidation. / Jiang, Zhongqing; Sontag-Strohm, Tuula S.; Salovaara, Hannu O.; Sibakov, Juhani K.; Kanerva, Päivi M.; Loponen, Jussi.

In: Journal of Cereal Science, Vol. 64, 2015, p. 126-132.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Oat protein solubility and emulsion properties improved by enzymatic deamidation

AU - Jiang, Zhongqing

AU - Sontag-Strohm, Tuula S.

AU - Salovaara, Hannu O.

AU - Sibakov, Juhani K.

AU - Kanerva, Päivi M.

AU - Loponen, Jussi

PY - 2015

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AB - Oat protein produced by a dry milling process was enzymatically deamidated by a food-grade protein-glutaminase (PG), and the effects on structure, solubility and emulsifying properties of oat proteins were studied. The reactions were conducted at neutral pH and low salt concentration conditions. Oat proteins were deamidated up to a deamidation degree of 59%. The solubility of proteins doubled. Oil-in-water emulsions prepared with the native and deamidated oat proteins differed as the emulsions prepared from oat proteins with high deamidation degree had a more uniform oil droplet particle size and longer stability. Fourier transform infrared (FT-IR) analysis demonstrated that oat protein secondary structure became more flexible by deamidation. Protein-glutaminase mediated deamidation appeared to be a promising technique to improve oat protein functionality such as emulsifying ability and solubility.

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KW - emulsions

KW - oat proteins

KW - solubility

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