Bioactive Peptides Potential Derived from Enzymatic Hydrolysis of Bohadschia vitiensis Sea Cucumber

Abstract

Sea cucumber species Bohadschia vitiensis possesses high nutritional and bioactive potential, and its protein hydrolysates produced using crude and pure papain enzymes may serve as promising natural antioxidant and antibacterial agents for functional food and pharmaceutical applications. This study evaluates the chemical composition and bioactive properties of protein hydrolysates derived from the sea cucumber Bohadschia vitiensis, processed using both crude and pure papain enzymes. The proximate analysis and amino acid profile data are analyzed descriptively by calculating the mean and standard deviation. Yield values are tested using ANOVA. SDS-PAGE and antioxidant activity data are analyzed with linear regression, while antibacterial activity is assessed by calculating the average diameter of the inhibition zone. Proximate analysis showed high moisture content (85.74%), moderate protein (6.21%), and low fat (4.64%). Amino acid profiling revealed a dominance of glycine (18.70%), threonine (15.82%), and methionine (9.35%), indicating functional potential. Antioxidant activity analysis demonstrated superior radical scavenging ability in hydrolysates from pure papain (IC50: 341.37 µg/mL) compared to crude papain (IC50: 448.07 µg/mL). Antibacterial assays indicated effective inhibition zones against Salmonella sp. (26.7 mm), Staphylococcus aureus (20.4 mm), and Escherichia coli (20.6 mm), with hydrolysates from pure papain showing stronger effects. SDS-PAGE results confirmed the presence of low molecular weight peptides (13.86–17.79 kDa). The findings suggest B. vitiensis hydrolysates as promising candidates for functional food and nutraceutical applications.