Chitin is one of the most abundant and cheaply available biopolymers in Nature. Chitin has become a valuable starting material for many biotechnological products through manipulation of its N-acetyl functionality, which can be cleaved under mild conditions using the enzyme family of de-N-acetylases. However, the chemoselective enzymatic re-acylation of glucosamine derivatives, which can introduce new stable functionalities into chitin derivatives, is much less explored. Herein we describe an acylase (CmCDA from Cyclobacterium marinum) that catalyzes the N-acylation of glycosamine with a range of carboxylic acids under physiological reaction conditions. This biocatalyst closes an important gap in allowing the conversion of chitin into complex glycosides, such as C5-modified sialosides, through the use of highly selective enzyme cascades.
An Enzymatic N-Acylation Step Enables the Biocatalytic Synthesis of Unnatural Sialosides
Parmeggiani F.;
2020-01-01
Abstract
Chitin is one of the most abundant and cheaply available biopolymers in Nature. Chitin has become a valuable starting material for many biotechnological products through manipulation of its N-acetyl functionality, which can be cleaved under mild conditions using the enzyme family of de-N-acetylases. However, the chemoselective enzymatic re-acylation of glucosamine derivatives, which can introduce new stable functionalities into chitin derivatives, is much less explored. Herein we describe an acylase (CmCDA from Cyclobacterium marinum) that catalyzes the N-acylation of glycosamine with a range of carboxylic acids under physiological reaction conditions. This biocatalyst closes an important gap in allowing the conversion of chitin into complex glycosides, such as C5-modified sialosides, through the use of highly selective enzyme cascades.File | Dimensione | Formato | |
---|---|---|---|
Transacetylation - REVISED MANUSCRIPT FINAL.pdf
accesso aperto
:
Post-Print (DRAFT o Author’s Accepted Manuscript-AAM)
Dimensione
580.92 kB
Formato
Adobe PDF
|
580.92 kB | Adobe PDF | Visualizza/Apri |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.