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The larvae of the Black Soldier Fly (Hermetia illucens L.) are rich in antimicrobial and antioxidant peptides. Recent studies have shown that protein extracts from these larvae (BSFL) possess cytotoxic activity against HeLa cervical cancer cells. However, the specific protein and peptide sizes responsible for this effect remain unclear. This study examines the cytotoxic and antioxidant properties of protein and peptide fractions from BSFL fed on palm kernel waste. The fractions were obtained using alkaline solubilization, acid precipitation, and ultrafiltration with 30 and 3 kDa molecular weight cut-offs, resulting in crude protein, >30 kDa protein, and 3-30 kDa protein-peptides. The superoxide radical scavenging activities were 32.23% (crude protein), 27.37% (>30 kDa protein), and 40.00% (3-30 kDa protein-peptides). While no cytotoxic effects were observed after 24 or 48 hours of incubation with HeLa cells, after 72 hours, the crude protein and >30 kDa protein exhibited cytotoxicity with IC₅₀ values of 27.08 ppm and 24.50 ppm, respectively. In contrast, the 3-30 kDa protein-peptides showed no significant cytotoxicity. These results suggest that while the crude and >30 kDa proteins exhibit strong cytotoxicity, which can be used for an anticancer, the 3-30 kDa peptides are potent antioxidants with no significant effect on cancer cells.