Regioselective monoacylation of cyclomaltoheptaose at the C-2 secondary hydroxyl groups by the alkaline protease from Bacillus subtilis in nonaqueous media
Xiao, Y.-m.; Wu, Q.; Wang, N.; Lin, X.-f.
Carbohydrate Research 339(7): 1279-1283
Transesterification of cyclomaltoheptaose (beta-CD) with divinyl butanedioate, divinyl hexanedioate, and divinyl decanedioate, catalyzed by the alkaline protease from Bacillus subtilis in anhydrous DMF for 5 days, furnished the corresponding vinyl-beta-CD derivatives. The products were characterized by ESI-MS, (1)H NMR, (13)C NMR, IR, and DSC. The results indicated the products to be monosubstituted esters, with monoacylation occurring at the C-2 secondary hydroxyl groups of beta-CD. The regioselectivity of the monoacylation as catalyzed by alkaline protease was not affected by the chain length of the acyl donor.