<span class="fontstyle۰">Tyrosinase Inhibitory Activity of Black Soldier Fly (<span class="fontstyle۰">Hermetia illucens<span class="fontstyle۰">) Larval Hydrolysate

Introduction: Black Soldier Fly (BSF) (Hermetia illucens) 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.Materials and Methods: 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Ⓡ. 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 C۱۸ Solid Phase Extraction (SPE) before tyrosinase inhibition assays.Results: The highest tyrosinase inhibitory activity among the samples was observed in the ۱۵-day-old (D۱۵ larvae) hydrolysate at a concentration of ۴۰,۰۰۰ ppm, showing ۸۸.۹۸% inhibition. In comparison, inhibition at the same concentration was ۷۵.۷۷% for ۵-day-old (D۵ larvae), ۸۲.۰۷% for ۱۰-day-old (D۱۰ larvae), and ۸۷.۷۸% for ۱۳-day-old (D۱۳ larvae) hydrolysates.Conclusions: BSF larval protein hydrolysates exhibit varying levels of soluble protein depending on larval age. Moreover, the C۱۸ SPE fractionation process yielded a higher percentage and more uniformity of tyrosinase inhibition than the unfractionated sample.

کلیدواژه ها:

Hermetia Illucens ، Tyrosinase Inhibition ، Enzymatic hydrolysis ، Solid-phase extraction ، Larval Hydrolysate ، Alcalase