Daria Kowalczykiewicz
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Daria Kowalczykiewicz has a total of 13 co-authors. Here are the top co-authors by number of shared publications:
- Andrzej Bolesław JarzęBski
Department of Chemical Engineering, Silesian University of Technology, M. Strzody 7, 44-100 Gliwice, Poland
1 shared publication - André Pollender
Environmental Microbiology, Institute of Biosciences, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany
1 shared publication - Antje Kumpf
Environmental Microbiology, Institute of Biosciences, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany
1 shared publication - Arkadiusz Chruściel
MEXEO Wiesław Hreczuch, ul. Energetyków 9, 47-225 Kędzierzyn-Koźle, Poland
1 shared publication - Dirk Tischler
Microbial Biotechnology, Faculty of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany
1 shared publication - Isabel Bento
EMBL Hamburg Notkestrasse 85 22607 Hamburg Germany
1 shared publication
Latest Publications
- Open Access
- 23 October 2019
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 20 (21) , 5263
Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach
Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.
- 23 October 2019
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 20 (21) , 5263
Open AccessLeloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach
Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.