Unlocking the gelling potential of oat protein: Synergistic effects of sonication and disulfide cleavage

Runnan Li; Youling L. Xiong; Vivekanandan Subramanian; Surendranath P. Suman; Alma D. True

doi:10.1016/j.foodhyd.2024.110241

Unlocking the gelling potential of oat protein: Synergistic effects of sonication and disulfide cleavage

Runnan Li
, Youling L. Xiong
, Vivekanandan Subramanian
, Surendranath P. Suman
, Alma D. True

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

11 Scopus citations

Abstract

The high thermal stability of oat globulin, attributed to inter-subunit disulfide bonds and strong hydrophobic interactions, poses a challenge to its gelling capacity. This study investigated the heat-induced gelling properties of oat protein isolate (OPI), focusing on the synergistic effect of physical (high-intensity ultrasound, HIU) and chemical (cysteine-assisted disulfide bond disruption) treatments. Creep-recovery and viscoelasticity (Gʹ/Gʹʹ) tests revealed decreased deformability and enhanced rigidity of OPI intermolecular structure upon cysteine treatment (100–400 mg/g protein), especially for HIU-treated protein. The HIU + cysteine process substantially increased the gel hardness (from 0.005 to 0.69 N) over the individual treatments with a synergy up to 432%. Correspondingly, cooking loss was reduced by 28–98% due to the move of free water into a restricted state (protein-bound protons) within the gel matrix as detected by ¹H NMR. These findings suggest new possibilities for utilizing oat protein in gel-based food products.

Original language	English
Article number	110241
Journal	Food Hydrocolloids
Volume	155
DOIs	https://doi.org/10.1016/j.foodhyd.2024.110241
State	Published - Oct 2024

Bibliographical note

Publisher Copyright:
© 2024 Elsevier Ltd

Funding

This work is supported by the USDA National Institute of Food and Agriculture, Hatch project 1020736. This work is supported by the USDA National Institute of Food and Agriculture, Hatch project 1020736. The authors thank the College of Pharmacy PharmNMR Center for analytical support. PharmNMR is supported in part by NIH grants S10 OD28690 and P20 GM130456.

Funders	Funder number
US Department of Agriculture National Institute of Food and Agriculture, Agriculture and Food Research Initiative	1020736
US Department of Agriculture National Institute of Food and Agriculture, Agriculture and Food Research Initiative
National Institutes of Health (NIH)	P20 GM130456, S10 OD28690
National Institutes of Health (NIH)

Keywords

Cysteine (Cys)
Heat-induced gels
High-intensity ultrasound (HIU)
Nuclear magnetic resonance (NMR)
Oat protein isolate (OPI)
Rheological properties

ASJC Scopus subject areas

Food Science
General Chemistry
General Chemical Engineering

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10.1016/j.foodhyd.2024.110241

Cite this

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title = "Unlocking the gelling potential of oat protein: Synergistic effects of sonication and disulfide cleavage",

abstract = "The high thermal stability of oat globulin, attributed to inter-subunit disulfide bonds and strong hydrophobic interactions, poses a challenge to its gelling capacity. This study investigated the heat-induced gelling properties of oat protein isolate (OPI), focusing on the synergistic effect of physical (high-intensity ultrasound, HIU) and chemical (cysteine-assisted disulfide bond disruption) treatments. Creep-recovery and viscoelasticity (Gʹ/Gʹʹ) tests revealed decreased deformability and enhanced rigidity of OPI intermolecular structure upon cysteine treatment (100–400 mg/g protein), especially for HIU-treated protein. The HIU + cysteine process substantially increased the gel hardness (from 0.005 to 0.69 N) over the individual treatments with a synergy up to 432\%. Correspondingly, cooking loss was reduced by 28–98\% due to the move of free water into a restricted state (protein-bound protons) within the gel matrix as detected by 1H NMR. These findings suggest new possibilities for utilizing oat protein in gel-based food products.",

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author = "Runnan Li and Xiong, \{Youling L.\} and Vivekanandan Subramanian and Suman, \{Surendranath P.\} and True, \{Alma D.\}",

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doi = "10.1016/j.foodhyd.2024.110241",

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AU - Suman, Surendranath P.

AU - True, Alma D.

PY - 2024/10

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N2 - The high thermal stability of oat globulin, attributed to inter-subunit disulfide bonds and strong hydrophobic interactions, poses a challenge to its gelling capacity. This study investigated the heat-induced gelling properties of oat protein isolate (OPI), focusing on the synergistic effect of physical (high-intensity ultrasound, HIU) and chemical (cysteine-assisted disulfide bond disruption) treatments. Creep-recovery and viscoelasticity (Gʹ/Gʹʹ) tests revealed decreased deformability and enhanced rigidity of OPI intermolecular structure upon cysteine treatment (100–400 mg/g protein), especially for HIU-treated protein. The HIU + cysteine process substantially increased the gel hardness (from 0.005 to 0.69 N) over the individual treatments with a synergy up to 432%. Correspondingly, cooking loss was reduced by 28–98% due to the move of free water into a restricted state (protein-bound protons) within the gel matrix as detected by 1H NMR. These findings suggest new possibilities for utilizing oat protein in gel-based food products.

AB - The high thermal stability of oat globulin, attributed to inter-subunit disulfide bonds and strong hydrophobic interactions, poses a challenge to its gelling capacity. This study investigated the heat-induced gelling properties of oat protein isolate (OPI), focusing on the synergistic effect of physical (high-intensity ultrasound, HIU) and chemical (cysteine-assisted disulfide bond disruption) treatments. Creep-recovery and viscoelasticity (Gʹ/Gʹʹ) tests revealed decreased deformability and enhanced rigidity of OPI intermolecular structure upon cysteine treatment (100–400 mg/g protein), especially for HIU-treated protein. The HIU + cysteine process substantially increased the gel hardness (from 0.005 to 0.69 N) over the individual treatments with a synergy up to 432%. Correspondingly, cooking loss was reduced by 28–98% due to the move of free water into a restricted state (protein-bound protons) within the gel matrix as detected by 1H NMR. These findings suggest new possibilities for utilizing oat protein in gel-based food products.

KW - Cysteine (Cys)

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KW - High-intensity ultrasound (HIU)

KW - Nuclear magnetic resonance (NMR)

KW - Oat protein isolate (OPI)

KW - Rheological properties

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Unlocking the gelling potential of oat protein: Synergistic effects of sonication and disulfide cleavage

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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