Issue 2, 2017

Highly efficient and selective biocatalytic production of glucosamine from chitin

Abstract

N-Acetyl glucosamine (GlcNAc) is one of the most abundant biomolecules on Earth and is cheaply available from chitin, a major component of crustaceans. The key step in the conversion of GlcNAc to high-value products is the de-N-acetylation to glucosamine, in itself a valuable dietary supplement that is produced at over 29 000 tons scale per annum by chemical hydrolysis, a process that requires harsh reaction conditions and leads to side products requiring separation. Here, we report for the first time the isolation and characterisation of an enzyme, a deacetylase from Cyclobacterium marinum that is able to catalyse the highly selective quantitative hydrolysis of GlcNAc to glucosamine under mild reaction conditions. This enzyme is small (38 kDa), is easily obtainable by heterologous expression in E. coli, has high turnover rates (kcat = 61 s−1), tolerates high substrate concentrations (over 100 g L−1) and can be repeatedly re-used as an immobilised catalyst. When coupled with chitinase, the high selectivity of the enzyme for GlcNAc over other biomolecules allowed one-pot extraction of glucosamine from crude solid mushroom fractions containing chitin, thus allowing for alternative production of glucosamine from non-animal sources, of benefit to consumers with crustacean allergies and vegan diets. We suggest that the deacetylase fills an important gap in the sustainable exploitation of GlcNAc and chitin.

Graphical abstract: Highly efficient and selective biocatalytic production of glucosamine from chitin

Supplementary files

Article information

Article type
Paper
Submitted
21 Okt. 2016
Accepted
10 Nov. 2016
First published
02 Dec. 2016

Green Chem., 2017,19, 527-535

Highly efficient and selective biocatalytic production of glucosamine from chitin

Y. M. Lv, P. Laborda, K. Huang, Z. P. Cai, M. Wang, A. M. Lu, C. Doherty, L. Liu, S. L. Flitsch and J. Voglmeir, Green Chem., 2017, 19, 527 DOI: 10.1039/C6GC02910H

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements