Human tyrosinase, a protein involved in the melanogenesis pathway, has various mutations in its corresponding gene (TYR) which have been linked to Oculocutaneous Albinism type 1 (OCA1), an autosomal recessive disease. Naturally, this inherited disorder leads to decreased melanocyte pigmentation accompanied by various\u00a0visual dysfunction. Recombinant human tyrosinase was individually overexpressed in whole Trichoplusia ni (T. ni) larvae. Purification of catalytically active protein was achieved through immobilized metal affinity chromatography (IMAC) and size-exclusion chromatography (SEC). Moreover, confirmation of protein identity was accomplished using human tyrosinase-specific antibodies and mass spectrometry. Lastly, the activity for both the intra-melanosomal domain (truncated, hTyrCtr) and full length (hTyr)\u00a0protein was displayed through L-DOPA and L-Tyrosine conversion into dopachrome (measured at 475 nm). This method of protein purification allows for higher yield recombinant hTyr and hTyrCtr protein from whole insect biomass to further elucidate characterization of both structure and role in human melanogenesis with the overall goal to use hTyr for enzyme replacement therapy.