Abstract

β-Galactosidase activities from the recombinant thermophilic CLONEZYME™ glycosidase library were screened at 70 °C for catalysis of a transgalactosylation from o-nitrophenyl-β-galactopyranoside to N-acetylglucosamine. Three thermophilic glycosidases (Gly001-06, -07 and -09) were found to produce predominantly the β(1–4)-linked isomer, Gal β(1–4)GlcNAc with up to 61% yield and less than 10% of the hydrolysis side reaction product. Thus, commercial recombinant thermophilic enzyme libraries constitute a novel class of biocatalysts for preparative organic synthesis. © 1997 Elsevier Science Ltd.

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