Abstract
The ever-increasing world population and environmental stress are leading to surging demand for nutrient-rich food products with cleaner labeling and improved sustainability. Plant proteins, accordingly, are gaining enormous popularity compared with counterpart animal proteins in the food industry. While conventional plant protein sources, such as wheat and soy, cause concerns about their allergenicity, peas, beans, chickpeas, lentils, and other pulses are becoming important staples owing to their agronomic and nutritional benefits. However, the utilization of pulse proteins is still limited due to unclear pulse protein characteristics and the challenges of characterizing them from extensively diverse varieties within pulse crops. To address these challenges, the origins and compositions of pulse crops were first introduced, while an overarching description of pulse protein physiochemical properties, e.g., interfacial properties, aggregation behavior, solubility, etc., are presented. For further enhanced functionalities, appropriate modifications (including chemical, physical, and enzymatic treatment) are necessary. Among them, non-covalent complexation and enzymatic strategies are especially preferable during the value-added processing of clean-label pulse proteins for specific focus. This comprehensive review aims to provide an in-depth understanding of the interrelationships between the composition, structure, functional characteristics, and advanced modification strategies of pulse proteins, which is a pillar of high-performance pulse protein in future food manufacturing.
Original language | English |
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Article number | 6 |
Journal | Foods |
Volume | 13 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2024 |
Funding
The authors acknowledge the support from the Center for Nanophase Materials Sciences (CNMS), which is a US Department of Energy, Office of Science User Facility at Oak Ridge National Laboratory and the support from the Laboratory Directed Research and Development Program of Oak Ridge National Laboratory, managed by UT-Battelle, for the U. S. Department of Energy. This work is supported by the Natural Science Foundation of China (Grant No. 32201953), the Shuguang Program of Wuhan Science and Technology Bureau (Grant No. 2022020801020262), Collaborative Grant-in-Aid of HBUT National “111” Center for Cellular Regulation and Molecular Pharmaceutics (Grant No. XBTK-2022017).
Keywords
- composition
- food application
- functional property
- non-covalent complexation
- physical modification
- pulse protein
- structure–property relationship