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Updated: Apr 12, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity
M Filice1, O Romero, J Gutiérrez-Fernández
1Departamento de Biocatálisis, Instituto de Catálisis, CSIC, Marie Curie 2, Campus UAM, 28049, Madrid, Spain. marco.filice1@gmail.com.
Abstract:
A solid-phase strategy using lipase as a biomolecular scaffold to produce a large amount of Cu(2+)-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.
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