Tilapia (Oreochromis niloticus) bones are a fishery by-product whose use remains limited, despite containing proteins that can be processed into bioactive peptides with antioxidant activity. This study aims to evaluate the characteristics of protein hydrolysate and antioxidant activity from raw and cooked tilapia bones using the ABTS method. Enzymatic hydrolysis was performed using papain at concentrations of 4%, 6%, and 8% (b/v) at pH 7 and 55°C for 4 hours. The parameters analyzed included qualitative amino acid tests, dissolved protein levels determined by the Kjeldahl method, degree of hydrolysis based on dissolved proteins in 10% TCA, and antioxidant activity expressed as IC₅₀ values. The results showed that all samples tested positively for amino acids, including aromatic amino acids. The lowest IC₅₀ value was observed in the treatment of a ripe sample with an enzyme concentration of 8% (6.89 mg/mL), indicating the highest antioxidant activity among the treatments. This is in line with an increase in the degree of hydrolysis to 84.53% under the same conditions, as well as an increase in dissolved protein levels to up to 32.78%. These findings indicate that tilapia bone protein hydrolysate has the potential to serve as a natural source of antioxidants, particularly under optimal hydrolysis conditions.
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