Pulse proteins are increasingly being investigated as nutritious and functional ingredients which could provide useful alternatives to animal proteins. However, pulse-protein ingredients do not always meet the functionality requirements necessary for various food applications. Enzymatic hydrolysis can be employed as a means of improving functional properties such as solubility and emulsifying, foaming, and gelling abilities. Enzymatic hydrolysis uses proteases to break down proteins into smaller peptides or amino acids. The resulting hydrolysates can have different functional properties compared to the original intact protein. This review examines the current literature regarding the modification of these properties using enzymatic hydrolysis.
Summary and key findings
- The effects of enzymatic hydrolysis on the functionality of pulse proteins varies considerably depending on the enzyme, substrate, and processing steps used (such as heat treatment, degree of hydrolysis, and pH).
- Differences in protease specificity and protein structures allow for a wide variety of peptide mixtures to be generated, with varying hydrophobic and electrostatic properties.
- Typically, the most significant techno-functional improvements are seen when the original protein ingredient has poor initial functionality. Solubility is usually improved in the mildly acidic range, which may also correspond with improved foaming and emulsifying properties.
- More work should be carried out on the potential of enzymatic hydrolysis to modify gelation properties of pulse proteins, as the literature is currently lacking in this area.
- The careful selection of proteases and control of hydrolysis is necessary to maximise the potential of enzymatic hydrolysis as a tool to improve pulse-protein functionality and to broaden the range of potential applications.
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