Sialyltransferase Initiates New Line of Sugar-Modifying Enzymes

The first in a line of recombinant enzymes for the in vitro sialylation of glycoproteins and other macromolecules is now available for biotech researchers.

The new product, alpha-2,6-sialyltransferase, was recently launched by Roche (Basel, Switzerland). Sialyltransferases are enzymes that transfer sialic acid to the terminal portions of sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins. Each sialyltransferase is specific for a particular sugar substrate. There are about twenty different sialyltransferases, which can be distinguished on the basis of the acceptor structure on which they act and on the type of sugar linkage they form.

The Roche alpha-2,6-sialyltransferase is based on a human genome sequence and expressed in mammalian expression systems. The enzyme was produced under animal-origin free conditions and offers a very high lot-to-lot consistency. Specifications call for the enzyme to deliver up to 95% bi-antennary sialylation of N-glycan chains within six to eight hours, a performance which is currently not offered by competitor products.

Over the coming months, Roche plans to complete the portfolio through launches of additional sialyl-and galactosyltransferase enzyme products.

“This launch is the first in a series to offer a complete glyco-engineering portfolio of key enzymes and activated sugars covering a broad spectrum of applications,” said Ruedi Stoffel, head of biochemical reagents and custom biotech at Roche. “The initial feedback from bio-manufacturing customers showed that our continuous scientific and technical support throughout the up-scaling and development process differentiates Roche as a strong partner.”

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