Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme’s performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid

Immobilization of Lathyrus cicera amine oxidase on magnetic microparticles for biocatalytic applications / DI FABIO, Elisa; Iazzetti, Antonia; Incocciati, Alessio; Caseli, Valentina; Fabrizi, Giancarlo; Boffi, Alberto; Bonamore, Alessandra; Macone, Alberto. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1422-0067. - 23:12(2022), p. 6529. [10.3390/ijms23126529]

Immobilization of Lathyrus cicera amine oxidase on magnetic microparticles for biocatalytic applications

Elisa Di Fabio
Primo
;
Antonia Iazzetti
Secondo
;
Alessio Incocciati;Valentina Caseli;Giancarlo Fabrizi;Alberto Boffi;Alessandra Bonamore
;
Alberto Macone
Ultimo
2022

Abstract

Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from Lathyrus cicera has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme’s performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid
enzyme immobilization; amine oxidase; magnetic particles; aldehydes; biocatalysis; oxidative deamination; primary amines
01 Pubblicazione su rivista::01a Articolo in rivista
Immobilization of Lathyrus cicera amine oxidase on magnetic microparticles for biocatalytic applications / DI FABIO, Elisa; Iazzetti, Antonia; Incocciati, Alessio; Caseli, Valentina; Fabrizi, Giancarlo; Boffi, Alberto; Bonamore, Alessandra; Macone, Alberto. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1422-0067. - 23:12(2022), p. 6529. [10.3390/ijms23126529]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1648657
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