Directing Oat Groat Heat Treatment Conditions Towards Increased Protein Extractability

Overview

Journal Curr Res Food Sci

Date 2024 Dec 17

PMID 39687421

Authors

Ines Pynket

Frederik Janssen

Jarne Van Gils

Christophe M Courtin

Arno G B Wouters

Affiliations

Soon will be listed here.

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.

References

Clark P, Plaxco K, Sosnick T . Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different. J Mol Biol. 2020; 432(9):2882-2889. PMC: 8256682. DOI: 10.1016/j.jmb.2020.01.031. View

Klose C, Arendt E . Proteins in oats; their synthesis and changes during germination: a review. Crit Rev Food Sci Nutr. 2012; 52(7):629-39. DOI: 10.1080/10408398.2010.504902. View

Yang Z, Piironen V, Lampi A . Lipid-modifying enzymes in oat and faba bean. Food Res Int. 2017; 100(Pt 1):335-343. DOI: 10.1016/j.foodres.2017.07.005. View

Montemurro M, Pontonio E, Coda R, Rizzello C . Plant-Based Alternatives to Yogurt: State-of-the-Art and Perspectives of New Biotechnological Challenges. Foods. 2021; 10(2). PMC: 7913558. DOI: 10.3390/foods10020316. View

Aiking H, de Boer J . The next protein transition. Trends Food Sci Technol. 2024; 105:515-522. PMC: 7127173. DOI: 10.1016/j.tifs.2018.07.008. View

McClements D, Newman E, McClements I . Plant-based Milks: A Review of the Science Underpinning Their Design, Fabrication, and Performance. Compr Rev Food Sci Food Saf. 2020; 18(6):2047-2067. DOI: 10.1111/1541-4337.12505. View

HUTCHINSON J, MARTIN H, Moran T . Location and destruction of lipase in oats. Nature. 1951; 167(4254):758-9. DOI: 10.1038/167758a0. View

LOWRY O, ROSEBROUGH N, FARR A, RANDALL R . Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193(1):265-75. View

Dornez E, Cuyvers S, Holopainen U, Nordlund E, Poutanen K, Delcour J . Inactive fluorescently labeled xylanase as a novel probe for microscopic analysis of arabinoxylan containing cereal cell walls. J Agric Food Chem. 2011; 59(12):6369-75. DOI: 10.1021/jf200746g. View

10.

Decker E, Rose D, Stewart D . Processing of oats and the impact of processing operations on nutrition and health benefits. Br J Nutr. 2014; 112 Suppl 2:S58-64. DOI: 10.1017/S000711451400227X. View

11.

Sim S, Srv A, Chiang J, Henry C . Plant Proteins for Future Foods: A Roadmap. Foods. 2021; 10(8). PMC: 8391319. DOI: 10.3390/foods10081967. View

12.

Wei C, Hund A, Zhu D, Nystrom L . Exploring genetic dependence of lipase activity to improve the quality of whole-grain wheat. J Sci Food Agric. 2020; 100(7):3120-3125. DOI: 10.1002/jsfa.10346. View

13.

McClements D, Grossmann L . A brief review of the science behind the design of healthy and sustainable plant-based foods. NPJ Sci Food. 2021; 5(1):17. PMC: 8175702. DOI: 10.1038/s41538-021-00099-y. View

14.

Hermans W, Mutlu S, Michalski A, Langenaeken N, Courtin C . The Contribution of Sub-Aleurone Cells to Wheat Endosperm Protein Content and Gradient Is Dependent on Cultivar and N-Fertilization Level. J Agric Food Chem. 2021; 69(23):6444-6454. DOI: 10.1021/acs.jafc.1c01279. View

15.

Mariotti F, Tome D, Mirand P . Converting nitrogen into protein--beyond 6.25 and Jones' factors. Crit Rev Food Sci Nutr. 2008; 48(2):177-84. DOI: 10.1080/10408390701279749. View