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Bernd Nidetzky

Martin Pfeiffer: Enzymes of natural product glycosylation
Annika Borg: EpiSwitch: the specificity of carbohydrate epimerases

Closed projects
Christiane Goedl: The glycogen phosphorylase from Sulfolobus solfataricus
Sigrid Egger: From the enzymatic mechanism to biocatalytic applications: dehydrogenases / reductases of AKR and LDR superfamily types
Alexander Gutmann: Insight into the distinctive mechanism of C-glycosyltransferases
Thomas Eixelsberger: Complex oxidoreductive transformations in glycobiology

Further Information
Curriculum Vitae (45 kB)
Publication List (external Link)
Collaborators (48 kB)
Grants (51 kB)


Bernd Nidetzky
Institute of Biotechnology and Biochemical Engineering
Technische Universität Graz
Petersgasse 12/1
8010 Graz

e-Mail: bernd.nidetzky@tugraz.at
phone: +43 316 873 8400
fax: +43 316 873 8434
web: http://www.cis.tu-graz.ac.at/biote

Carbohydrate-active enzymes and natural products bio-synthesis: mechanisms and applications

The group of B. Nidetzky carries out basic research on enzyme catalysis and is involved in bioprocess development using enzymes as the biocatalysts. The concept is to build on the understanding of fundamental kinetic and chemical mechanisms of the enzymatic reaction and then move towards the real application by analyzing interactions between biochemical and physical factors that occur on the process scale. Of interest are enzymes that can make glycosidic bonds between sugar units and catalyze oxidoreductive biotransformations. The aim is to utilize renewable carbohydrate-based resources for the production of functional “sugars” to be used in medicine or for food and feed applications; to explore novel enzymes from nature, analyze their structure and function, and design improved processes by targeted modifications of enzyme properties and innovative reaction engineering.

Laboratory know-how and infrastructure

The methodical expertise covers all steps of enzymatic process development, from the identification and production of enzymes to the optimization of the enzyme-catalyzed conversion in different bioreactors including the downstream processing. The group has strong know-how in the elucidation of relationships between enzyme structure, function and stability using a combination of advanced kinetic studies, site-directed mutagenesis, and in collaboration with external partners, X-ray crystallography and structural modeling. The laboratory is well equipped for studies of molecular enzymology (rapid-mixing stopped flow instrument with multiple wavelengths absorbance and fluorescence detection). High-resolution analytical devices for the study of proteins and carbohydrates are also available.

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