Enhanced characterization and utilization of cowpea protein isolate: rheological and textural properties of heat-induced gels for plant-based egg omelet formulation

This study aimed to evaluate the potential of cowpea isolate (CPI) as an effective plant-based egg substitute by comparing its composition and physicochemical properties with those of commercial isolates, including mung bean, soy, and pea proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis identified a distinctive vicilin-like globulin in CPI that is critical for the unique functional properties of CPI. CPI has a smaller particle size, resulting in superior gelation capacity and water retention, which are essential for egg substitute applications. Thermal analysis revealed the high stability of CPI, which is advantageous for food processing. Notably, the unique heat-induced gelation behavior of CPI, characterized by a smooth transition from solid- to liquid-like states, provided a strength not observed in its commercial counterparts. Microstructural analysis showed that the CPI gel closely resembled the egg gel, underscoring the potential of CPI to mimic the texture of eggs, particularly in omelets.

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Publication Details

Journal
Food Chemistry X
Published
2024-11-03
DOI
https://doi.org/10.1016/j.fochx.2024.101956
Citations
5
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
1.74

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article

Enhanced characterization and utilization of cowpea protein isolate: rheological and textural properties of heat-induced gels for plant-based egg omelet formulation

Jungwoo Hahn, Hyun Woo Choi
5 citations
Food Chemistry X
Proteins in Food Systems
1.74
article

Enhanced characterization and utilization of cowpea protein isolate: rheological and textural properties of heat-induced gels for plant-based egg omelet formulation

Jungwoo Hahn, Hyun Woo Choi
article en
5 citations

Abstract

This study aimed to evaluate the potential of cowpea isolate (CPI) as an effective plant-based egg substitute by comparing its composition and physicochemical properties with those of commercial isolates, including mung bean, soy, and pea proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis identified a distinctive vicilin-like globulin in CPI that is critical for the unique functional properties of CPI. CPI has a smaller particle size, resulting in superior gelation capacity and water retention, which are essential for egg substitute applications. Thermal analysis revealed the high stability of CPI, which is advantageous for food processing. Notably, the unique heat-induced gelation behavior of CPI, characterized by a smooth transition from solid- to liquid-like states, provided a strength not observed in its commercial counterparts. Microstructural analysis showed that the CPI gel closely resembled the egg gel, underscoring the potential of CPI to mimic the texture of eggs, particularly in omelets.

Food Chemistry XVol. 24
Seoul National University (KR)
National Research Foundation, Ministry of Oceans and Fisheries, Ministry of Agriculture, Food and Rural Affairs, Korea Institute of Planning and Evaluation for Technology in Food, Agriculture, Forestry and Fisheries, National Research Foundation of Korea, Korea Institute of Marine Science and Technology promotion, Ministry of Science and ICT, South Korea, Korea Institute of Planning and Evaluation for Technology in Food, Agriculture and Forestry
Zero hunger
Openalex Percentile: Top 16%
Proteins in Food Systems
1.74
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