Protease-catalyzed monoacylation of 2-O-alpha-D-Glucopyranosyl-L-ascorbic acid in pyridine.
2-O-alpha-D-Glucopyranosyl-6-O-octanoyl-L-ascorbic acid was enzymatically synthesized from 2-O-alpha-D-glucopyranosyl-L-ascorbic acid (AA-2G) and vinyl octanoate with a protease from Bacillus subtilis in pyridine. Furthermore, with various linear saturated fatty acid vinylesters as acyl donors, AA-2G was also converted to their corresponding 6-O-acyl AA-2G in the same manner. The reactivities of transacylation decreased with increasing length of the acyl groups. Thus, short chain acyl groups were transferred to AA-2G by this protease more efficiently than were long chain acyl groups. This enzymatic method is recommended for the synthesis of 6-Acyl-AA-2G with short or medium length chain acyl groups.
Tai
A
A
Department of Immunochemistry, Faculty of Pharmaceutical Sciences, Okayama University, Japan.
Okazaki
S
S
Tsubosaka
N
N
Yamamoto
I
I
D000215:Acylation; D000217:Acyltransferases / Q000378:metabolism; D001205:Ascorbic Acid / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism*; D001412:Bacillus subtilis / Q000201:enzymology; D002384:Catalysis; D010450:Endopeptidases / Q000378:metabolism*; D011725:Pyridines / Q000378:metabolism*
D011725:Pyridines; C065378:ascorbic acid 2-O-glucoside; D000217:Acyltransferases; D010450:Endopeptidases; C023666:pyridine; D001205:Ascorbic Acid