Roche Diagnostics Operations, Inc.

Basf Se Corporation

Technische Universitat Graz

Roche Diagnostics Gmbh

F. Hoffmann-la Roche Ag

Basf Beauty Care Solutions France S.a.s.

Universitat Wien

Forschungsholding Tu Graz Gmbh

Bernd Nidetzky

Christiane Luley

Michael Breuer

Kai-Uwe Baldenius

Rainer Mueller

Harald Sobek

Thomas Meier

Helmut Schwab

Alfred Engel

Bernhard Schaffar

Michael Greif

Bernhard Suppmann

Marco Thomann

Sebastian Malik

Vaidotas Navickas

Christine Jung

Mario Müller

Tibor Czabany

Doris Ribitsch

Patricia Wildberger

Katharina Schmoelzer

Sabine Zitzenbacher

Martin Pfeiffer

Stefan Leitgeb

Thomas Stoisser

Thornthan Sawangwan

Christiane Gödl

Rama Krishna Gudiminchi

Thomas Mag Rer Nat Stoisser

Michael Vogl

Lothar Brecker

Regina Kratzer

Alexandra Schwarz

The present invention relates to a method for producing 2-O-glyceryl-&#x3b1;-D-glucopyranoside (&#x3b1;GG; FIG.) from a glucosyl donor and a glucosyl acceptor comprising the steps: providing a sucrose phosphorylase (EC 2.4.1.7), incubating said sucrose phosphorylase with a mixture comprising a glucosyl donor and glycerol as glucosyl acceptor and isolating and/or purifying 2-O-glyceryl-&#x3b1;-D-glucopyranoside.

Method for producing 2-O-glyceryl-alpha-D-glucopyranoside

The present invention relates to methods of producing sugar phosphates by enzymatic transphosphorylation, wherein the phosphoryl transfer from phosphate donor substrates to sugar substrates is catalyzed by an enzyme having alpha-glucose-1-phosphatase activity. Furthermore, the present invention relates to a biocatalyst having sucrose phosphorylase as well as alpha-glucose-1-phosphatase activity and its use. The production of an enzyme having alpha-glucose-1-phosphatase activity and its use in the transphosphorylation of sugar substrates is also presented herein.

Enzymatic transphosphorylation of sugar substrates

The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human &#x3b2;-galactoside-&#x3b1;-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant &#x394;89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant &#x394;108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Quantitative control of sialylation and specific mono-sialylation

The present disclosure relates to a mutant lactate oxidase having increased stability, a nucleic acid encoding the mutant lactate oxidase, an expression vector comprising the nucleic acid, a host cell comprising the nucleic acid or the expression vector, a method of determining lactate in a sample, the use of the mutant lactate oxidase for determining lactate, a device for determining lactate in a sample using the mutant lactate oxidase and a kit for determining lactate comprising the mutant lactate oxidase.

Mutant lactate oxidase with increased stability and product, methods and uses involving the same

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Graz, Austria

Bernd Nidetzky