Institution: | aDepartamento de Biocatálisis, Instituto de Catálisis (CSIC), Campus UAM Cantoblanco, 28049 Madrid, Spain bDipartimento di Chimica Farmaceutica, Università di Pavia, via Taramelli 12, 27100 Pavia, Italy |
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. |