Baqiyatallah University of Medical Sciences Journal of Applied Biotechnology Reports 2322-1186 13 2 2026 06 30 Tyrosinase Inhibitory Activity of Black Soldier Fly (Hermetia illucens) Larval Hydrolysate 2035 2043 247493 10.30491/jabr.2025.531906.1888 EN Hegar Pramastya Department of Pharmaceutical Biology, School of Pharmacy, Institut Teknologi Bandung, Bandung, Indonesia 0000-0002-4585-219X Felix Saccio Teng Department of Pharmaceutical Biology, School of Pharmacy, Institut Teknologi Bandung, Bandung, Indonesia 0009-0007-1875-8409 Defri Rizaldy Department of Pharmaceutical Biology, School of Pharmacy, Institut Teknologi Bandung, Bandung, Indonesia 0000-0001-9745-3855 Journal Article 2025 07 02 <span class="fontstyle0"><strong>Introduction:</strong> </span><span class="fontstyle2">Black Soldier Fly (BSF) (</span><em><span class="fontstyle2">Hermetia illucens</span></em><span class="fontstyle2">) larvae contain protein in varying amounts depending on the age at harvest. Due to their high protein content, BSF larvae represent a promising alternative protein source with potential bioactivities, including tyrosinase inhibitory activity. This study aimed to evaluate the tyrosinase inhibitory activity of BSF larval protein hydrolysates as a function of larval age and the fractionation process.</span><br><span class="fontstyle0"><strong>Materials and Methods:</strong> </span><span class="fontstyle2">The larvae were dried and defatted using the Soxhlet extraction method. The defatted larvae were characterized by determining ash, moisture, and soluble protein contents. Enzymatic hydrolysis was carried out using Alcalase</span>^{<span class="fontstyle3">Ⓡ</span>}<span class="fontstyle2">. Soluble protein content in the hydrolysates was analyzed using the Bradford assay. The degree of hydrolysis (DH) of the hydrolysates was analyzed using the o-phthaldialdehyde (OPA) method. The hydrolysates were then freeze-dried and fractionated using C18 Solid Phase Extraction (SPE) before tyrosinase inhibition assays.</span><br><span class="fontstyle0"><strong>Results:</strong> </span><span class="fontstyle2">The highest tyrosinase inhibitory activity among the samples was observed in the 15-day-old (D15 larvae) hydrolysate at a concentration of 40,000 ppm, showing 88.98% inhibition. In comparison, inhibition at the same concentration was 75.77% for 5-day-old (D5 larvae), 82.07% for 10-day-old (D10 larvae), and 87.78% for 13-day-old (D13 larvae) hydrolysates.</span><br><span class="fontstyle0"><strong>Conclusions:</strong> </span><span class="fontstyle2">BSF larval protein hydrolysates exhibit varying levels of soluble protein depending on larval age. Moreover, the C18 SPE fractionation process yielded a higher percentage and more uniformity of tyrosinase inhibition than the unfractionated sample.</span> https://www.biotechrep.ir/article_247493_972a01ec512700c3c8d7e766937057cc.pdf