Scientists in Austria who have redesigned the active site of an enzyme to switch its regioselectivity may have latched onto a new way to make molecules that are important for infant formula. The engineered enzyme is almost identical to the original, it just catalyses a slightly different reaction to its twin.
Sialylated human milk oligosaccharides play an important role in infant health and development. They occur naturally in breast milk, but synthetic sialylated oligosaccharides are also in demand to enrich infant formula and other nutraceutical products.
Read the full article in Chemistry World»
Read the original journal article in ChemComm – it’s free to access until 27th April:
Complete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-D-galactoside sialyltransferase by active-site redesign
Katharina Schmölzer, Tibor Czabany, Christiane Luley-Goedl, Tea Pavkov-Keller, Doris Ribitsch, Helmut Schwab, Karl Gruber, Hansjörg Weber and Bernd Nidetzky
Chem. Commun., 2015,51, 3083-3086
DOI: 10.1039/C4CC09772F, Communication
