Aldehydes are a class of carbonyl compounds widely used as intermediates in the pharmaceutical, cosmetic and food industries. To date, there are few fully enzymatic methods for synthesizing these highly reactive chemicals. In the present work, we explore the biocatalytic potential of an amino oxidase extracted from the etiolated shoots of Lathyrus cicera for the synthesis of value‐added aldehydes, starting from the corresponding primary amines. In this frame, we have developed a completely chromatography‐free purification protocol based on crossflow ultrafiltration, which makes the production of this enzyme easily scalable. Furthermore, we determined the kinetic parameters of the amine oxidase toward 20 differently substituted aliphatic and aromatic primary amines, and we developed a biocatalytic process for their conversion into the corresponding aldehydes. The reaction occurs in aqueous media at neutral pH in the presence of catalase, which removes the hydrogen peroxide produced during the reaction itself, contributing to the recycling of oxygen. A high conversion (>95%) was achieved within 3 h for all the tested compounds.
Biocatalytic production of aldehydes: exploring the potential of lathyrus cicera amine oxidase / Di Fabio, E.; Incocciati, A.; Boffi, A.; Bonamore, A.; Macone, A.. - In: BIOMOLECULES. - ISSN 2218-273X. - 11:10(2021), p. 1540. [10.3390/biom11101540]
Biocatalytic production of aldehydes: exploring the potential of lathyrus cicera amine oxidase
Di Fabio E.;Incocciati A.;Boffi A.;Bonamore A.
;Macone A.
2021
Abstract
Aldehydes are a class of carbonyl compounds widely used as intermediates in the pharmaceutical, cosmetic and food industries. To date, there are few fully enzymatic methods for synthesizing these highly reactive chemicals. In the present work, we explore the biocatalytic potential of an amino oxidase extracted from the etiolated shoots of Lathyrus cicera for the synthesis of value‐added aldehydes, starting from the corresponding primary amines. In this frame, we have developed a completely chromatography‐free purification protocol based on crossflow ultrafiltration, which makes the production of this enzyme easily scalable. Furthermore, we determined the kinetic parameters of the amine oxidase toward 20 differently substituted aliphatic and aromatic primary amines, and we developed a biocatalytic process for their conversion into the corresponding aldehydes. The reaction occurs in aqueous media at neutral pH in the presence of catalase, which removes the hydrogen peroxide produced during the reaction itself, contributing to the recycling of oxygen. A high conversion (>95%) was achieved within 3 h for all the tested compounds.File | Dimensione | Formato | |
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