Abstract
Mung bean (Vigna radiata L.) is a protein-rich pulse mainly cultivated in
Asia, where its consumption has been associated with positive health outcomes. Mung
bean protein is especially rich in leucine, lysine, phenylalanine, and tyrosine amino
acids and it contains the 8S α-globulin as the major seed storage protein. Protein derived products from pulses, such as protein concentrates, hydrolysates, and purified
peptide fractions are becoming popular functional foods. Mung bean peptides are
enzymatically generated using gastrointestinal and non-gastrointestinal proteases.
Protein hydrolysates generated by one or a combination of enzymes have been
demonstrated to exert different biological potentials, including antioxidant,
antihypertensive, anticancer, and hypocholesterolemic effects. These properties are
attributed to the amino acid sequences, the type of enzyme used for hydrolysis, and the
purification method. More robust experimental designs must be performed to
understand the role and mechanisms of these bioactive peptides with in vivo studies and
clinical trials. Furthermore, there is a lack of information related to the incorporation of
bioactive peptides into a food matrix while preserving their bioactivity. This chapter
provides an overview of the central aspects of mung bean physical structure and
chemical composition, protein characteristics, enzymatic production, and the biological
potential of mung bean protein hydrolysates and peptides. <br>
Publisher
BENTHAM SCIENCE PUBLISHERS