ArticleCurrent research in food science2024
Directing oat groat heat treatment conditions towards increased protein extractability.
Article in Current research in food science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Unravelling the Role of Oat β-Glucan on the Surface Behavior of an Oat Protein-Rich Coextract: An Enzymatic Approach.Biomacromolecules · 2026Article
- Understanding the impact of oat groat heat treatment on its protein extractability.Food chemistry: X · 2026Article
- Improving protein extractability from oats using malted cereal extracts under acidic fermentation-like conditions.Current research in food science · 2026Article
- Colloidal state and emulsifying properties of protein isolates from kilned and non-kilned oats.Current research in food science · 2026Article
- Enzyme activity and constituent extractability of kilned and non-kilned oats at pH values relevant for acidic food fermentations.Food chemistry: X · 2025Article
- Integrative lipidomics and proteomics reveal the aging mechanisms of heat-treated oat flour during long-term storage.Food chemistry: X · 2025Article
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5 authors.
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Abstract
Oat-based liquid and semi-solid dairy alternatives require extractable proteins for nutritional and technological purposes. However, oats are industrially heat treated ('kilned') to inactivate endogenous lipases thereby avoiding rancidity development. Such heat treatment results in a protein extractability decrease. We here investigated the possibility of directing oat groat heat treatment conditions [oat groat moisture content (13.0-20.0%), heating temperature (80-100 °C) and heating time (15-45 min)] on a lab-scale to achieve complete enzyme inactivation, with peroxidase activity as a marker, while maintaining high protein extractability. Non-heat-treated and industrially heat-treated oats were included as reference samples. The peroxidase activity and protein extractability of lab-scale heat-treated oats decreased with an increase in moisture content, heating temperature and time. Several lab-scale heat-treated oats for which complete peroxidase inactivation was observed, had significantly higher protein extractabilities (31-59%) than industrially kilned oats (21%). The activity of endogenous lipases was determined for a selected sample set. Lipases required milder heat treatment conditions for complete inactivation than peroxidases. Such milder heat treatment led to samples with protein extractabilities between 31 and 65%. A notable observation was that heat treating oats (≥90 °C) caused clumping of the intracellular material of the aleurone cells, likely due to protein aggregation. The main conclusion of this study is that oat heat treatment conditions can be altered successfully to achieve complete enzyme inactivation while maintaining high protein extractability. The obtained insights could lead to the development of oat-based products with higher protein content and desired shelf stability.
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