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

doi:10.1016/j.jcs.2015.04.010

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

VTT Technical Research Centre of Finland

University of Helsinki

Research output: Contribution to journal › Article › Scientific › peer-review

103 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 language	English
Pages (from-to)	126-132
Journal	Journal of Cereal Science
Volume	64
DOIs	https://doi.org/10.1016/j.jcs.2015.04.010
Publication status	Published - 2015
MoE publication type	A1 Journal article-refereed

Keywords

deamidation
emulsions
oat proteins
solubility

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10.1016/j.jcs.2015.04.010

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title = "Oat protein solubility and emulsion properties improved by enzymatic deamidation",

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.",

keywords = "deamidation, emulsions, oat proteins, solubility",

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",

year = "2015",

doi = "10.1016/j.jcs.2015.04.010",

language = "English",

volume = "64",

pages = "126--132",

journal = "Journal of Cereal Science",

issn = "0733-5210",

publisher = "Elsevier",

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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

Y1 - 2015

N2 - 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.

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.

KW - deamidation

KW - emulsions

KW - oat proteins

KW - solubility

U2 - 10.1016/j.jcs.2015.04.010

DO - 10.1016/j.jcs.2015.04.010

M3 - Article

SN - 0733-5210

VL - 64

SP - 126

EP - 132

JO - Journal of Cereal Science

JF - Journal of Cereal Science

ER -

Oat protein solubility and emulsion properties improved by enzymatic deamidation

Abstract

Keywords

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