Identification and comparison of proteomic and peptide profiles of mung bean seeds and sprouts

The objectives of this study were to analyze and compare the proteomic and peptide profiles of mung bean (Vigna radiata) seeds and sprouts. Label-free proteomics and peptidomics technologies allowed the identification and relative quantification of proteins and peptides. There were 1918 and 1955 proteins identified in mung bean seeds and sprouts, respectively. The most common biological process of proteins in these two samples was the metabolic process, followed by cellular process and single-organism process. Their dominant molecular functions were catalytic activity, binding, and structural molecule activity, and the majority of them were the cell, cell part, and organelle proteins. These proteins were primarily involved in metabolic pathways, biosynthesis of secondary metabolites, and ribosome. PCA and HCA results indicated the proteomic profile varied significantly during mung bean germination. A total of 260 differential proteins between mung bean seeds and sprouts were selected based on their relative abundance, which were associated with the specific metabolism during seed germination. There were 2364 peptides identified and 76 potential bioactive peptides screened based on the in silico analysis. Both the types and concentration of the peptides in mung bean sprouts were higher than those in seeds, and the content of bioactive peptides in mung bean sprouts was deduced to be higher.