Abstract
Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread,\r\nfrom 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\r\ncatalyzes 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\r\nproduct concentrations. Here, we show that the enzyme’s performance can be greatly improved by\r\nimmobilization on solid supports. The best results are achieved using amino-functionalized magnetic\r\nmicroparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h\r\nat 75 ◦C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction\r\ncycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production\r\nranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of\r\nthe aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural\r\nbenzylisoquinoline alkaloid.
| Lingua originale | Inglese |
|---|---|
| pagine (da-a) | 6529-6542 |
| Numero di pagine | 14 |
| Rivista | International Journal of Molecular Sciences |
| Volume | 23 |
| Numero di pubblicazione | 12 |
| DOI | |
| Stato di pubblicazione | Pubblicato - 2022 |
All Science Journal Classification (ASJC) codes
- Catalisi
- Biologia Molecolare
- Spettroscopia
- Informatica Applicata
- Chimica Fisica e Teorica
- Chimica Organica
- Chimica Inorganica
Keywords
- : enzyme immobilization
- aldehydes
- amine oxidase
- biocatalysis
- magnetic particles
- oxidative deamination
- primary amines
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