Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity

M. Filice; O. Romero; J. Gutiérrez-Fernández; B. De Las Rivas; J. A. Hermoso; J.M. Palomo

doi:10.1039/c5cc02450a

Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity

M. Filice^*, O. Romero, J. Gutiérrez-Fernández, B. De Las Rivas, J. A. Hermoso, J.M. Palomo

^*Corresponding author for this work

Research output: Contribution to journal › Article › Research › peer-review

30 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	9324-9327
Number of pages	4
Journal	Chemical Communications
Volume	51
Issue number	45
DOIs	https://doi.org/10.1039/c5cc02450a
Publication status	Published - 7 Jun 2015

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title = "Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity",

abstract = "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.",

author = "M. Filice and O. Romero and J. Guti{\'e}rrez-Fern{\'a}ndez and {De Las Rivas}, B. and Hermoso, {J. A.} and J.M. Palomo",

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AU - Filice, M.

AU - Romero, O.

AU - Gutiérrez-Fernández, J.

AU - De Las Rivas, B.

AU - Hermoso, J. A.

AU - Palomo, J.M.

PY - 2015/6/7

Y1 - 2015/6/7

N2 - 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.

AB - 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.

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U2 - 10.1039/c5cc02450a

DO - 10.1039/c5cc02450a

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AN - SCOPUS:84930654824

VL - 51

SP - 9324

EP - 9327

IS - 45

ER -

Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity

Abstract

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