Regioselective monoacylation of cyclomaltoheptaose at the C-2 secondary hydroxyl groups by the alkaline protease from Bacillus subtilis in nonaqueous media.
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.
Xiao
Yong-mei
YM
Department of Chemistry, Zhejiang University, Hangzhou 310027, People's Republic of China.
Wu
Qi
Q
Wang
Na
N
Lin
Xian-fu
XF
D000215:Acylation; D001412:Bacillus subtilis / Q000201:enzymology*; D015394:Molecular Structure; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D047392:beta-Cyclodextrins / Q000737:chemistry* / Q000378:metabolism
D047392:beta-Cyclodextrins; C494268:mono-(2-O-vinylbutanedioyl)-beta-cyclodextrin; C494270:mono-(2-O-vinyldecanedioyl)-beta-cyclodextrin; C494269:mono-(2-O-vinylhexanedioyl)-beta-cyclodextrin; D012697:Serine Endopeptidases; C032923:microbial serine proteinases; C031215:betadex