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.
Lingua originale | English |
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pagine (da-a) | 6529-6542 |
Numero di pagine | 14 |
Rivista | International Journal of Molecular Sciences |
Volume | 23 |
DOI | |
Stato di pubblicazione | Pubblicato - 2022 |
Keywords
- : enzyme immobilization
- aldehydes
- amine oxidase
- biocatalysis
- magnetic particles
- oxidative deamination
- primary amines