Anti- Activity and Peptidomic Profiling of Peptide Fractions Produced from Sturgeon Fish Skin Collagen () Using Commercial Enzymes

Overview

Journal Nutrients

Date 2021 Aug 27

PMID 34444819

Citations 4

Authors

Maryam Atef

Yasmina Ait Chait

Seyed Mahdi Ojagh

Ali Mohammad Latifi

Mina Esmaeili

Riadh Hammami

Chibuike C Udenigwe

Affiliations

Soon will be listed here.

Abstract

This study investigated peptide fractions from fish skin collagen for antibacterial activity against and strains. The collagen was hydrolyzed with six commercial proteases, including trypsin, Alcalase, Neutrase, Flavourzyme, pepsin and papain. Hydrolyzed samples obtained with trypsin and Alcalase had the largest number of small peptides (molecular weight <10 kDa), while the hydrolysate produced with papain showed the lowest degree of hydrolysis and highest number of large peptides. Four hydrolysates were found to inhibit the growth of the Gram-negative bacteria, with papain hydrolysate showing the best activity against , and Neutrase and papain hydrolysates showing the best activity against ; hydrolysates produced with trypsin and pepsin did not show detectable antibacterial activity. After acetone fractionation of the latter hydrolysates, the peptide fractions demonstrated enhanced dose-dependent inhibition of the growth (colony-forming units) of four strains, including (NCTC 6017), (ATCC 13311), (ATCC 14028) and (ATCC 10708). Shotgun peptidomics analysis of the acetone fractions of Neutrase and papain hydrolysates resulted in the identification of 71 and 103 peptides, respectively, with chain lengths of 6-22 and 6-24, respectively. This work provided an array of peptide sequences from fish skin collagen for pharmacophore identification, structure-activity relationship studies, and further investigation as food-based antibacterial agents against pathogenic microorganisms.

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