期刊
ENZYME AND MICROBIAL TECHNOLOGY
卷 39, 期 6, 页码 1236-1241出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2006.03.006
关键词
lipase; enzymic acylation; flavonoid; polyphenolic; phenolic acid
Immobilised Candida antarctica lipase B (Novozym 435 (R)) was used to acylate flavonoid glycosides, both purified and in fruit extracts, using carboxylic acids as acyl donors, in the presence of 4 angstrom molecular sieves, using 2-methyl-2-propanol as solvent. Conversions ranged from similar to 25% to similar to 95% using palmitic, cinnamic and phenylpropionic (PPA) acids and hydroxylated derivatives of PPA as acyl donors. Both naringin (naringenin-7-rhamnoglucoside) and isoquercetin (quercetin-3-O-glucopyranoside) were readily acylated. Both compounds gave a major mono-acylated product, along with minor mono-acylated products, which were presumably positional isomers and also di-acylated products. When apple or blueberry extracts were the source of flavonoids, the enzyme showed strong selectivity for acylation of glycosides, with a primary aliphatic hydroxyl group on the sugar moiety, such as phloridzin (phloretin-2-glucoside) and anthocyanidin glucosides and galactosides. No acylation of compounds lacking a primary aliphatic hydroxyl group, such as flavonoid aglycones, chlorogenic acid (caffeoyl quinate) or anthocyanidin arabinosides was observed. Acylation, particularly with palmitic acid, greatly increased lipophilicity and solubility in the reaction solvent. (c) 2006 Elsevier Inc. All rights reserved.
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