Abstract
The monodeacetylation of peracetylated-β-
d-galactose (
1) and peracetylated
N-acetyl-β-
d-glucosamine (
2) by different lipases is here described. Lipases from different sources in an immobilized form were evaluated to find those that offer the higher activity and regioselectivity in the reactions. In the hydrolysis of
1, the lipase from
Aspergillus niger was the most active one, although it hydrolyzed the anomeric position. Using the lipase from
Candida rugosa, 30% yield of the corresponding 6-OH isomer was achieved. On the other hand, in the hydrolysis of
2, the lipase from
A. niger was the most active and regioselective catalyst, producing more than 75% of the 6-OH derivative product.