Natural heterogeneous catalysis with immobilised oxidase biocatalysts

Ashley P. Mattey; Jack J. Sangster; Jeremy I. Ramsden; Christopher Baldwin; William R. Birmingham; Rachel S. Heath; Antonio Angelastro; Nicholas J. Turner; Sebastian C. Cosgrove; Sabine L. Flitsch

doi:10.1039/D0RA03618H

Natural heterogeneous catalysis with immobilised oxidase biocatalysts

Ashley P. Mattey, Jack J. Sangster, Jeremy I. Ramsden, Christopher Baldwin, William R. Birmingham, Rachel S. Heath, Antonio Angelastro, Nicholas J. Turner, Sebastian C. Cosgrove, Sabine L. Flitsch

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

Abstract

The generation of immobilised oxidase biocatalysts allowing multifunctional oxidation of valuable chemicals using molecular oxygen is described. Engineered galactose oxidase (GOase) variants M1 and M3–5, an engineered choline oxidase (AcCO6) and monoamine oxidase (MAO-N D9) displayed long-term stability and reusability over several weeks when covalently attached on a solid support, outperforming their free counterparts in terms of stability (more than 20 fold), resistance to heat at 60 °C, and tolerance to neat organic solvents such as hexane and toluene. These robust heterogenous oxidation catalysts can be recovered after each reaction and be reused multiple times for the oxidation of different substrates

Original language	English
Pages (from-to)	19501-19505
Journal	RSC Advances
Volume	10
Issue number	33
Early online date	21 May 2020
DOIs	https://doi.org/10.1039/D0RA03618H
Publication status	E-pub ahead of print - 21 May 2020

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title = "Natural heterogeneous catalysis with immobilised oxidase biocatalysts",

abstract = "The generation of immobilised oxidase biocatalysts allowing multifunctional oxidation of valuable chemicals using molecular oxygen is described. Engineered galactose oxidase (GOase) variants M1 and M3–5, an engineered choline oxidase (AcCO6) and monoamine oxidase (MAO-N D9) displayed long-term stability and reusability over several weeks when covalently attached on a solid support, outperforming their free counterparts in terms of stability (more than 20 fold), resistance to heat at 60 °C, and tolerance to neat organic solvents such as hexane and toluene. These robust heterogenous oxidation catalysts can be recovered after each reaction and be reused multiple times for the oxidation of different substrates",

author = "Mattey, {Ashley P.} and Sangster, {Jack J.} and Ramsden, {Jeremy I.} and Christopher Baldwin and Birmingham, {William R.} and Heath, {Rachel S.} and Antonio Angelastro and Turner, {Nicholas J.} and Cosgrove, {Sebastian C.} and Flitsch, {Sabine L.}",

year = "2020",

month = may,

day = "21",

doi = "10.1039/D0RA03618H",

language = "English",

volume = "10",

pages = "19501--19505",

journal = "RSC Advances",

issn = "2046-2069",

publisher = "Royal Society of Chemistry",

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TY - JOUR

T1 - Natural heterogeneous catalysis with immobilised oxidase biocatalysts

AU - Mattey, Ashley P.

AU - Sangster, Jack J.

AU - Ramsden, Jeremy I.

AU - Baldwin, Christopher

AU - Birmingham, William R.

AU - Heath, Rachel S.

AU - Angelastro, Antonio

AU - Turner, Nicholas J.

AU - Cosgrove, Sebastian C.

AU - Flitsch, Sabine L.

PY - 2020/5/21

Y1 - 2020/5/21

N2 - The generation of immobilised oxidase biocatalysts allowing multifunctional oxidation of valuable chemicals using molecular oxygen is described. Engineered galactose oxidase (GOase) variants M1 and M3–5, an engineered choline oxidase (AcCO6) and monoamine oxidase (MAO-N D9) displayed long-term stability and reusability over several weeks when covalently attached on a solid support, outperforming their free counterparts in terms of stability (more than 20 fold), resistance to heat at 60 °C, and tolerance to neat organic solvents such as hexane and toluene. These robust heterogenous oxidation catalysts can be recovered after each reaction and be reused multiple times for the oxidation of different substrates

AB - The generation of immobilised oxidase biocatalysts allowing multifunctional oxidation of valuable chemicals using molecular oxygen is described. Engineered galactose oxidase (GOase) variants M1 and M3–5, an engineered choline oxidase (AcCO6) and monoamine oxidase (MAO-N D9) displayed long-term stability and reusability over several weeks when covalently attached on a solid support, outperforming their free counterparts in terms of stability (more than 20 fold), resistance to heat at 60 °C, and tolerance to neat organic solvents such as hexane and toluene. These robust heterogenous oxidation catalysts can be recovered after each reaction and be reused multiple times for the oxidation of different substrates

U2 - 10.1039/D0RA03618H

DO - 10.1039/D0RA03618H

M3 - Article

SN - 2046-2069

VL - 10

SP - 19501

EP - 19505

JO - RSC Advances

JF - RSC Advances

IS - 33

ER -

Natural heterogeneous catalysis with immobilised oxidase biocatalysts

Abstract

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