Structure-function guided production of oat and chickpea protein isolates in comparison to pea protein isolate following mild extraction conditions

• Mild extraction was successfully scaled to produce oat and chickpea protein isolates • Results highlighted the functionality of the underutilized oat and chickpea proteins • Oat protein isolate (OPI) had good gel strength at pH 7 and solubility at pH 3.4 • Chickpea protein isolate (ChPI) had good solubility and emulsification capacity • OPI and ChPI can potentially replace traditional ingredients in food applications As the global plant protein consumption continues to rise, legumes remain the dominant protein source on the market. Additional plant protein sources with desirable functionality must be identified to meet the growing protein demand. To achieve desirable functionality of these rather challenging plant proteins, it is essential to preserve the structural integrity of the protein during the extraction process by employing mild conditions. Accordingly, a mild process involving alkaline extraction coupled with isoelectric precipitation (AE-IEP) to produce protein isolates from two legumes (chickpea and pea) and a cereal source (oat) was evaluated at a bench and pilot scale. Scaling the process was essential to demonstrate its potential commercial adaptation. Oat, chickpea, and pea protein isolates (OPI, ChPI, and PPI) were produced at benchtop and their production was scaled-up (SU) in the pilot plant to obtain SUOPI, SUChPI, and SUPPI. The adapted AE-IEP process effectively maintained structural integrity with limited denaturation and polymerization. Such structural integrity contributed to superior or comparable solubility of both SUPPI and SUChPI relative to commercial pea and soy protein isolates (cPPI and cSPI), and superior gel strength of SUOPI compared to SUChPI and SUPPI, and to cPPI. These functional performances were linked to unique surface properties, presence of soluble aggregates, and to the characteristics of the indigenous globulin proteins. These findings uniquely highlighted the potential of the underutilized oat and chickpea proteins, along with pea protein as functional contenders in the plant protein market, when produced following a mild yet scalable extraction process.

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Publication Details

Journal
Applied Food Research
Published
2025-10-21
DOI
https://doi.org/10.1016/j.afres.2025.101440
Citations
2
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
2.32
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article

Structure-function guided production of oat and chickpea protein isolates in comparison to pea protein isolate following mild extraction conditions

Abigail Krentz, Baraem Ismail, M. J. Creek, Sima Saeidy et al.
2 citations
Applied Food Research
Proteins in Food Systems
2.32
article

Structure-function guided production of oat and chickpea protein isolates in comparison to pea protein isolate following mild extraction conditions

Abigail Krentz, Baraem Ismail, M. J. Creek, Sima Saeidy, Brittany Kralik
article en
2 citations

Abstract

• Mild extraction was successfully scaled to produce oat and chickpea protein isolates • Results highlighted the functionality of the underutilized oat and chickpea proteins • Oat protein isolate (OPI) had good gel strength at pH 7 and solubility at pH 3.4 • Chickpea protein isolate (ChPI) had good solubility and emulsification capacity • OPI and ChPI can potentially replace traditional ingredients in food applications As the global plant protein consumption continues to rise, legumes remain the dominant protein source on the market. Additional plant protein sources with desirable functionality must be identified to meet the growing protein demand. To achieve desirable functionality of these rather challenging plant proteins, it is essential to preserve the structural integrity of the protein during the extraction process by employing mild conditions. Accordingly, a mild process involving alkaline extraction coupled with isoelectric precipitation (AE-IEP) to produce protein isolates from two legumes (chickpea and pea) and a cereal source (oat) was evaluated at a bench and pilot scale. Scaling the process was essential to demonstrate its potential commercial adaptation. Oat, chickpea, and pea protein isolates (OPI, ChPI, and PPI) were produced at benchtop and their production was scaled-up (SU) in the pilot plant to obtain SUOPI, SUChPI, and SUPPI. The adapted AE-IEP process effectively maintained structural integrity with limited denaturation and polymerization. Such structural integrity contributed to superior or comparable solubility of both SUPPI and SUChPI relative to commercial pea and soy protein isolates (cPPI and cSPI), and superior gel strength of SUOPI compared to SUChPI and SUPPI, and to cPPI. These functional performances were linked to unique surface properties, presence of soluble aggregates, and to the characteristics of the indigenous globulin proteins. These findings uniquely highlighted the potential of the underutilized oat and chickpea proteins, along with pea protein as functional contenders in the plant protein market, when produced following a mild yet scalable extraction process.

Applied Food ResearchVol. 5(2)
University of Minnesota (US)
Openalex Percentile: Top 11%
Proteins in Food Systems
2.32
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