Antimicrobial peptides purified from hydrolysates of kanihua (Chenopodium pallidicaule Aellen) seed protein fractions

The kanihua (Chenopodium pallidicaule Aellen) Andean grain from the Peruvian Altiplano presents proteins of 15% to 19%. The objective was to obtain purified bioactive antimicrobial peptides (AMPs), hydrolyzed with Alcalase and Pepsin-pancreatin sequential system of protein fractions of kanihua varieties Ramis (KR) and CupiSayhua (KS), and hydrolysates with different degrees of hydrolysis (DH) and percentage inhibition (IP) of the growth of E. coli, S. aureus, and C. albicans. To obtain AMPs, nutraceuticals, bio-preservatives, and novel ingredients in food design. The results showed 216 hydrolysates (1%, w/v), only 28 presented significant difference compared to controls (IP 0.05), and presented an anionic charge. In conclusion, the simulated digestion in vitro showed higher DH (7%-67%) than Alcalase (13%-54%); the majority were extensive; of 28 hydrolysates with IP 45% 4 AMPs with important IPs were obtained, and one was anionic.

Automated summary

The study aimed to obtain purified bioactive antimicrobial peptides from two varieties of kanihua and investigate their inhibition effects on E. coli, S. aureus, and C. albicans growth. Experimental results showed that 4 AMPs with significant inhibition rates were obtained from the hydrolysates.