Encrypted antimicrobial and antitumoral peptides recovered from a protein-rich soybean (Glycine max) by-product

Twelve promising candidates for antimicrobial peptides encrypted in F7J075, Q948X9, Q94LX2, Q3V5S6, Q4LER6, AOAOROHYM3 and I1LMQ8 with molecular masses ranging from 718.42 to 4872.43 Da were identified in two fractions obtained from gel filtration chromatography of soybean meal aqueous extract, a defatted by-product generated by soybean oil refinery. Most peptides found in both fractions are encrypted in two regions of beta-conglycinin alpha or alpha-prime subunits, the major protein in soybean. The pool of peptides from both fractions inhibited the growth of Gram-positive and Gram-negative foodborne pathogens and exhibited no toxicity to mouse bone marrow or fibroblast cells, but inhibited human glioblastoma proliferation. Three-dimensional structure of beta-conglycinin domains containing the best AMP candidates, determined by molecular modeling, indicated an alpha-helix conformation. The production in large scale and use of multifunctional peptides encrypted in soybean meal proteins is an innovative application of the concept of circular bioeconomy.