Open Access Article
This Open Access Article is licensed under a
Creative Commons Attribution 3.0 Unported Licence

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

Katharina Schmölzer a, Melanie Weingarten b, Kai Baldenius b and Bernd Nidetzky *ac
aAustrian Centre of Industrial Biotechnology (acib), Petersgasse 14, 8010 Graz, Austria. E-mail: bernd.nidetzky@tugraz.at
bBASF SE, Carl-Bosch-Straße 38, 67056 Ludwigshafen, Germany
cInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, 8010 Graz, Austria

Received 21st May 2019 , Accepted 21st May 2019

First published on 4th June 2019


Abstract

Correction for ‘Lacto-N-tetraose synthesis by wild-type and glycosynthase variants of the β-N-hexosaminidase from Bifidobacterium bifidum’ by Katharina Schmölzer et al., Org. Biomol. Chem., 2019, DOI: 10.1039/c9ob00424f.


The authors regret that there was an error in some of the structures shown in Scheme 1. The correct graphic is shown below.
image file: c9ob90088h-s1.tif
Scheme 1 Strategy of lacto-N-tetraose (LNT) synthesis from lacto-N-biose 1,2-oxazoline (LNB-oxa) by LnbB from B. bifidum. (a) Hydrolysis of LNT by wild-type LnbB. (b) Proposed catalytic mechanism of LnbB. (c) LNB 1,2-oxazoline as possible donor substrate for synthesis of LNT via glycosylation of lactose.

The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.


This journal is © The Royal Society of Chemistry 2019
Click here to see how this site uses Cookies. View our privacy policy here.