1 publication
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Synthesis of a Heterogeneous Artificial Metallolipase with Chimeric Catalytic Activity
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Chem. Commun. 2015, 51, 9324-9327, 10.1039/C5CC02450A
A solid-phase strategy using lipase as a biomolecular scaffold to produce a large amount of Cu2+-metalloenzyme is proposed here. The application of this protocol on different 3D cavities of the enzyme allows creating a heterogeneous artificial metallolipase showing chimeric catalytic activity. The artificial catalyst was assessed in Diels–Alder cycloaddition reactions and cascade reactions showing excellent catalytic properties.
Metal: CuLigand type: PhenanthrolineHost protein: Lipase from G. thermocatenulatus (GTL)Anchoring strategy: CovalentOptimization: GeneticNotes: ArM is immobilized on Sepabeads. Endo/exo = 93.5%
Metal: CuLigand type: PhenanthrolineHost protein: Lipase from G. thermocatenulatus (GTL)Anchoring strategy: CovalentOptimization: GeneticNotes: Cascade reaction: Ester hydrolysis (natural function of the host protein) followed by reduction (function of the designed ArM).