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

Food Chem. 2021 Oct 30:360:129951. doi: 10.1016/j.foodchem.2021.129951. Epub 2021 Apr 24.

Abstract

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 Cupi-Sayhua (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 ≥ 45%, p ≤ 0.05), 4 AMPs were purified by chromatography, glutelins KS 4 h (1:10) stood out with DH 40% and IP 52% and 70% of S. aureus and C. albicans, respectively (p ≤ 0.05), showed minimum inhibitory concentration (MIC) of 95% for E. coli (p ≤ 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.

Keywords: Antimicrobial activity in percent inhibition; Antimicrobial peptides; Chenopodium pallidicaule Aellen; Degree of hydrolysis; Hydrolyzed; Nutraceuticals; Protein fractions.

MeSH terms

  • Chenopodium / chemistry
  • Chenopodium / embryology*
  • Escherichia coli / metabolism
  • Hydrolysis
  • Microbial Sensitivity Tests
  • Pore Forming Cytotoxic Proteins / isolation & purification*
  • Protein Hydrolysates / chemistry
  • Seeds / chemistry*
  • Seeds / metabolism
  • Staphylococcus aureus / metabolism

Substances

  • Pore Forming Cytotoxic Proteins
  • Protein Hydrolysates