Issue 23, 2019

Lacto-N-tetraose synthesis by wild-type and glycosynthase variants of the β-N-hexosaminidase from Bifidobacterium bifidum

Abstract

Lacto-N-biose 1,2-oxazoline was prepared chemo-enzymatically and shown to be a donor substrate for β-1,3-glycosylation of lactose by the wild-type and glycosynthase variants (D320E, D320A, Y419F) of Bifidobacterium bifidum β-N-hexosaminidase. Lacto-N-tetraose, a core structure of human milk oligosaccharides, was formed in 20–60% yield of donor substrate (up to 8 mM product titre), depending on the degree of selectivity control by the enzyme used.

Graphical abstract: Lacto-N-tetraose synthesis by wild-type and glycosynthase variants of the β-N-hexosaminidase from Bifidobacterium bifidum

Associated articles

Supplementary files

Article information

Article type
Communication
Submitted
20 Feb 2019
Accepted
08 May 2019
First published
16 May 2019
This article is Open Access
Creative Commons BY-NC license

Org. Biomol. Chem., 2019,17, 5661-5665

Lacto-N-tetraose synthesis by wild-type and glycosynthase variants of the β-N-hexosaminidase from Bifidobacterium bifidum

K. Schmölzer, M. Weingarten, K. Baldenius and B. Nidetzky, Org. Biomol. Chem., 2019, 17, 5661 DOI: 10.1039/C9OB00424F

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