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.
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