Comparative antimicrobial and antioxidant activity from collagen peptides from fish scales from Seriola rivoliana, using shrimp and commercial enzymes
DOI:
https://doi.org/10.18633/biotecnia.v27.2734Keywords:
collagen, peptides, antimicrobial, antioxidantAbstract
The fish processing industry faces dual challenges: environmental impact and low-profit applications for by-products, emphasizing the need to valorize this waste. In this study, collagen was isolated from Seriola rivoliana fish scales. SDS-PAGE results indicated that the purified collagen consisted of two distinct chains (α1- and α2-), consistent with the composition of type I collagen. Fish scale collagen is composed of Gly, Ala y Pro amino acids, with high proportion of Pro (20%), and exhibits an absorption peak at 230 nm in the UV-Vis spectrum. Collagen was hydrolyzed with 60 and 120 mU of activity of Wobenzym (WE) and digestive gland extract from shrimp waste (SE). The resulting collagen-derived peptides from WE showed DPPH scavenging activity, while shrimp-derived peptides did not. Both WE and SE-derived peptides inhibited the growth of marine pathogens (Vibrio diabolicus, Vibrio parahaemolyticus, and Photobacterium) and human pathogens (Escherichia coli, Pseudomonas spp., and Salmonella spp.). However, SE-derived peptides demonstrated stronger inhibitory effects against human pathogens, while WE-derived peptides were more effective against marine pathogens. These results suggest that waste materials, such as scales from the marine fish S. rivoliana, have potential as a source of collagen for generating peptides with antioxidant and antimicrobial properties.
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