Lipase catalyzed esterification of oleuropein with fatty acids
2013
Abd Elgwad, A. I. M.
This work underlines the biocatalytic preparation of novel bioactive analogs of oleuropein in organic media. Oleuropein (1) was enzymatically acylated with different aliphatic acids as acyl donors (butyric acid (2) and oleic acid (4)) by an immobilized lipase Candida antarctica (Novozyme 435(copyright) and commercial Asperillus nigor (Sigma) to synthesize lipophilic antioxidants, regarding a green organic synthesis. Immobilized lipase Novozyme 435(copyright) has shown regioselectivity with short chain fatty acid (2) and long chain fatty acid (4). The biocatalytic reaction did not occur in the presence of commercial Asperillus nigor (Sigma) as the catalyst. The antioxidant properties of oleuropein6''-O-oleate (5) were assessed by employing the peroxyoxalate chemiluminescence test, and compared with oleuropein (1), which was used as a reference antioxidant potential towards scavenging of H2O2 in a non-polar medium. A significant increase of antioxidant potential towards scavenging of H2O2 in a non-polar medium was observed for oleuropein6''-O-oleate (5) rather than oleuropein (1). This research work succeeded to modify the hydrophilic properties of oleuropein (1) to obtain new lipophilic products with multifunctional properties combining, for instance, antioxidant and miscibility properties in a non-polar medium.
اظهر المزيد [+] اقل [-]الكلمات المفتاحية الخاصة بالمكنز الزراعي (أجروفوك)
المعلومات البيبليوغرافية
تم تزويد هذا السجل من قبل Mediterranean Agronomic Institute of Chania