Mung bean proteins and peptides: nutritional, functional and bioactive properties

Abstract

To date, no extensive literature review exists regarding potential uses of mung bean proteins and peptides. As mung bean has long been widely used as a food source, early studies evaluated mung bean nutritional value against the Food and Agriculture Organization of the United Nations (FAO)/the World Health Organization (WHO) amino acids dietary recommendations. The comparison demonstrated mung bean to be a good protein source, except for deficiencies in sulphur-containing amino acids, methionine and cysteine. Methionine and cysteine residues have been introduced into the 8S globulin through protein engineering technology. Subsequently, purified mung bean proteins and peptides have facilitated the study of their structural and functional properties. Two main types of extraction methods have been reported for isolation of proteins and peptides from mung bean flours, permitting sequencing of major proteins present in mung bean, including albumins and globulins (notably 8S globulin). However, the sequence for albumin deposited in the UniProt database differs from other sequences reported in the literature. Meanwhile, a limited number of reports have revealed other useful bioactivities for proteins and hydrolysed peptides, including angiotensin-converting enzyme inhibitory activity, anti-fungal activity and trypsin inhibitory activity. Consequently, several mung bean hydrolysed peptides have served as effective food additives to prevent proteolysis during storage. Ultimately, further research will reveal other nutritional, functional and bioactive properties of mung bean for uses in diverse applications.

Functional properties and dynamic rheology of protein isolates extracted from male and female common carp (Cyprinus carpio) muscle subjected to pH‐shifting method

“…Foam formation is governed by some mechanisms such as how proteins molecules penetrate, transport, and reorganize themselves at air–water interface (Özyurt et al, ). High levels of hydrophobic residue after homogenization may result in lower FC, whereas formation of a cohesive continuous network with high elasticity by MBPI having optimum intermolecular network formation creates stable foams at air–liquid interface (Yi‐Shen, Shuai, & Fitzgerald, ).…”

Comparative assessment of physicochemical and antioxidative properties of mung bean protein hydrolysates

“…2 shows the molecular weight distribution of mung bean protein (control) with very intense broad bands in the range of 37 to 75 kDa, which probably corresponds to the 8S vicilin. 24,25 32 and 25 kDa peptide might be 8S vicilin subunit, and the distinct bands of approximately 20 kDa most likely corresponded to 11S fractions or basic 7S subunit of seed storage protein. 26 However, large molecular weight bands of mung bean proteins decreased gradually with the increasing hydrolysis time of cin treatment.…”

Integrated Transcriptomic and Metabolic Framework for Carbon Metabolism and Plant Hormones Regulation in Vigna radiata during Post-Germination Seedling Growth

“…Mung bean is a potential source of most essential amino acids with the exception of sulphur-containing amino acids including methionine and cysteine 28 . The profiles of most amino acids during mung bean germination were similar to the results reported previously 11 , although there were some variations among the reported values of the amino acid contents, which might be explained by the differences in mung bean varieties and analytical methods 29 .…”