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

^*Autor corresponent d’aquest treball

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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.

Idioma original	Anglès
Pàgines (de-a)	9324-9327
Nombre de pàgines	4
Revista	Chemical Communications
Volum	51
Número	45
DOIs	https://doi.org/10.1039/c5cc02450a
Estat de la publicació	Publicada - 7 de juny 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",

note = "Publisher Copyright: {\textcopyright} The Royal Society of Chemistry.",

year = "2015",

month = jun,

day = "7",

doi = "10.1039/c5cc02450a",

language = "English",

volume = "51",

pages = "9324--9327",

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TY - JOUR

T1 - Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity

AU - Filice, M.

AU - Romero, O.

AU - Gutiérrez-Fernández, J.

AU - De Las Rivas, B.

AU - Hermoso, J. A.

AU - Palomo, J.M.

N1 - Publisher Copyright: © The Royal Society of Chemistry.

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.

UR - https://www.scopus.com/pages/publications/84930654824

U2 - 10.1039/c5cc02450a

DO - 10.1039/c5cc02450a

M3 - Article

C2 - 25960359

AN - SCOPUS:84930654824

SN - 1359-7345

VL - 51

SP - 9324

EP - 9327

JO - Chemical Communications

JF - Chemical Communications

IS - 45

ER -

Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity

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