ArticleFood chemistry. Molecular sciences2025
Identifying microbial proteins and changes in proteome in spontaneously fermented pulse protein isolates.
Article in Food chemistry. Molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Solid-State Fermentation of Legumes: Multi-Scale Structural Modifications to Unlock Techno-Functional Properties.Comprehensive reviews in food science and food safety · 2026Review
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Authors and funding
9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Pulses are a sustainable source of plant-based proteins, but they often fall short in terms of sensory attributes and functionality. Fermentation has been investigated as a natural food processing method to address these limitations. Spontaneous fermentation, where native microflora grow without the addition of specific microbes, has been traditionally used in food processing by various cultures around the world. However, there is a knowledge gap regarding the changes that occur in protein composition during spontaneous fermentation. This study used capillary gel electrophoresis and liquid chromatography coupled to tandem mass spectrometry to examine the changes in protein size distribution, identify microbial proteins and understand proteome-level changes that occurred during the spontaneous fermentation of three protein isolate substrates: chickpea, faba bean, and lentil. The findings revealed that proteins from a variety of bacterial and fungal species were identified in all substrates, and the number and quantity of these microbial proteins increased during spontaneous fermentation. This rise in microbial protein content was associated with the hydrolysis of proteins from the pulse substrates, which could potentially alter the functionality of the protein ingredient.
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