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Review
. 2024 Jun 5;72(22):12319-12339.
doi: 10.1021/acs.jafc.4c00380. Epub 2024 May 23.

Decoding the Duality of Antinutrients: Assessing the Impact of Protein Extraction Methods on Plant-Based Protein Sources

Maria Lilibeth Manzanilla-Valdez  1 , Zidan Ma  1 , Martin Mondor  2   3 , Alan Javier Hernández-Álvarez  1
Affiliations
Review

Decoding the Duality of Antinutrients: Assessing the Impact of Protein Extraction Methods on Plant-Based Protein Sources

Maria Lilibeth Manzanilla-Valdez et al. J Agric Food Chem. .

Abstract

This review aims to provide an updated overview of the effects of protein extraction/recovery on antinutritional factors (ANFs) in plant protein ingredients, such as protein-rich fractions, protein concentrates, and isolates. ANFs mainly include lectins, trypsin inhibitors, phytic acid, phenolic compounds, oxalates, saponins, tannins, and cyanogenic glycosides. The current technologies used to recover proteins (e.g., wet extraction, dry fractionation) and novel technologies (e.g., membrane processing) are included in this review. The mechanisms involved during protein extraction/recovery that may enhance or decrease the ANF content in plant protein ingredients are discussed. However, studies on the effects of protein extraction/recovery on specific ANFs are still scarce, especially for novel technologies such as ultrasound- and microwave-assisted extraction and membrane processing. Although the negative effects of ANFs on protein digestibility and the overall absorption of plant proteins and other nutrients are a health concern, it is also important to highlight the potential positive effects of ANFs. This is particularly relevant given the rise of novel protein ingredients in the market and the potential presence or absence of these factors and their effects on consumers' health.

Keywords: antinutritional factors; dry fractionation; plant proteins; protein digestibility; protein extraction; wet extraction.

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Conflict of interest statement

The authors declare no competing financial interest.

Figures

Figure 1
Figure 1
Classification of common ANFs and their corresponding heat stability.
Figure 2
Figure 2
Bowman-Birk trypsin inhibitor and Kunitz trypsin inhibitor, and their corresponding reactive sites.,
Figure 3
Figure 3
Phytate structure and its’ six binding sites
Figure 4
Figure 4
Lectin binding with host carbohydrate complexes from glycoproteins
Figure 5
Figure 5
Mechanisms of phenolic compounds with biomolecules after digestion.
Figure 6
Figure 6
Mechanisms of phenolic compounds with proteins; noncovalent and covalent interactions.
Figure 7
Figure 7
Mechanisms of oxalates binding to different compounds
Figure 8
Figure 8
Mechanisms of saponin binding to different compounds
Figure 9
Figure 9
Mechanisms of tannins binding to proteins and carbohydrates
See this image and copyright information in PMC

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