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

Gladys Moscoso-Mujica, Amparo I. Zavaleta, Ángel Mujica, Inés Arnao, Carlos Moscoso-Neira, Marco Santos, Johanna Sánchez

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23 Scopus citations


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.

Original languageEnglish
Article number129951
JournalFood Chemistry
StatePublished - 30 Oct 2021
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2021 Elsevier Ltd


  • Antimicrobial activity in percent inhibition
  • Antimicrobial peptides
  • Chenopodium pallidicaule Aellen
  • Degree of hydrolysis
  • Hydrolyzed
  • Nutraceuticals
  • Protein fractions


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