Wang, M., Ettelaie, R. and Sarkar, A. orcid.org/0000-0001-8677-5234 (2025) Enzymatic hydrolysis of legume proteins: lessons on surface property outcomes. Current Opinion in Food Science, 62. 101259. ISSN 2214-7993
Abstract
There is burgeoning research interest in utilising legume proteins as eco-friendly and nutritionally-relevant plant-based alternatives to animal proteins. However, legume proteins exhibit techno-functional limitations that impede their widespread food applications. Herein, we review how enzymatic hydrolysis of legume proteins can be exploited to alter physical properties, improving their surface related functionalities based on current literature. The choice of enzyme, particularly the selectivity plays a significant role in obtaining different emulsifying and interfacial properties of legume protein hydrolysates. Several physicochemical characteristics synergistically affect the surface functional performance of legume proteins. Outlining future directions, this review highlights the transformative potential of enzymatic hydrolysis in legume proteins for enhancing the textural (lubrication) aspects. Additionally, precise measurements of structures of hydrolysates are a necessary undertaking in the future.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2024 The Author(s). This is an open access article under the terms of the Creative Commons Attribution License (CC-BY 4.0), which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Environment (Leeds) > School of Food Science and Nutrition (Leeds) > FSN Colloids and Food Processing (Leeds) |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/Z516119/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 11 Dec 2024 09:50 |
Last Modified: | 18 Feb 2025 13:36 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.cofs.2024.101259 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:220683 |