Abstract
A simple method for immobilizing extracellular enzyme without prepurification of the enzyme was developed. Extracellular His-tagged Thermomyces lanuginosus lipase (His-TLL) was immobilized via affinity by direct treatment of core–shell structured iron oxide magnetic nanoparticles containing long-armed nickel-nitrilotriacetic acid surface groups (Ni-NTA-MNPs) with the cell culture supernatant of Pichia pastoris (h-TLL), giving high enzyme loading efficiency, specific enzyme loading, and specific enzyme activity. The nanobiocatalyst His-TLL-MNPs (80 nm) (5 wt % loading) catalyzed the one-pot conversion of waste grease (24 wt % FFA) to biodiesel with 94% yield and showed excellent recyclability. Ni-NTA-MNPs were easily regenerated from the recycled biocatalyst and reusable for enzyme immobilization. The immobilization method was proven to be general by the immobilization of extracellular His-tagged Candida antarctica lipase B (His-CALB) from the cell culture supernatant of P. pastoris (h-CALB).
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