Queen bee larvae (Apis mellifera) as a novel bioactive matrix: tyrosinase inhibition, compositional analysis, and...

Queen bee larvae (QBL), a by-product of Apis mellifera royal jelly production, represent an underexplored protein-rich biological matrix with enzyme-modulatory bioactivity. This study provides the first systematic characterisation of lyophilised QBL through compositional profiling, tyrosinase inhibitory activity, cytocompatibility assessment, and topical carrier stability evaluation. Compositional analysis (AOAC/ISO-accredited methods) revealed a protein-dominant matrix (55.19 g/100 g) rich in essential amino acids, B-group vitamins, vitamins C, D3 and E, and minerals (Mg 1566 mg/kg; Ca 676.6 mg/kg), with total antioxidant capacity of 312.1 µM Trolox equivalents. QBL demonstrated concentration-dependent human tyrosinase inhibition, reaching 75.7 ± 2.5% at 1000 µg/mL. HaCaT keratinocyte viability exceeded 80% across all concentrations at 24 h and 48 h. A QBL-incorporated model gel maintained physicochemical integrity and microbiological stability over three months. These findings establish QBL as a biocompatible, protein-dominant natural matrix with tyrosinase-modulatory and antioxidant properties, warranting further investigation as a bioactive natural product.