title: Lipase-catalyzed modification of phenolic antioxidants.
abstract: The chemical acylation of natural antioxidants may improve their oxidative and thermal stability, as well as modify their hydrophile-lipophile balance (HLB). These processes are generally carried out under harsh conditions using strongly corrosive acids. In contrast, lipase-catalyzed acylation is characterized by mild reaction conditions, low energy requirements, and a minimization of side reactions. We report the one-step enzymatic acylation of a phenolic antioxidant (α-tocopherol) and a polyphenol (resveratrol) by lipase-catalyzed transesterification. In particular, the regioselectivity of resveratrol acylation can be controlled by an adequate selection of the biocatalyst.
authors.affiliation: Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica, CSIC, Madrid, Spain.
authors.forename: Pamela
authors.initials: P
authors.lastname: Torres
authors.forename: Dolores
authors.initials: D
authors.lastname: Reyes-Duarte
authors.forename: Antonio
authors.initials: A
authors.lastname: Ballesteros
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Plou
mesh_terms: D000215:Acylation; D000421:Alcaligenes / Q000737:chemistry / Q000201:enzymology; D000975:Antioxidants / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D055162:Biocatalysis; D002175:Candida / Q000737:chemistry / Q000201:enzymology; D004951:Esterification; D005656:Fungal Proteins / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008049:Lipase / Q000737:chemistry*; D010084:Oxidation-Reduction; D000077185:Resveratrol; D013237:Stereoisomerism; D013267:Stilbenes / Q000737:chemistry*; D013379:Substrate Specificity; D024502:alpha-Tocopherol / Q000737:chemistry*
chemical_list: D000975:Antioxidants; D001426:Bacterial Proteins; D005656:Fungal Proteins; D013267:Stilbenes; D008049:Lipase; D024502:alpha-Tocopherol; D000077185:Resveratrol