Title: Biocatalysis alternatives dedicated to flavors and fragrances production

Madalina Tudorache

University of Bucharest, Romania


Madalina Tudorache has experience of more than 15 years in the research area, started with Immunochemistry and Analytical Chemistry in 2000 (PhD study at Lund University, Sweden). Now she is lecturer at the Department of Organic Chemistry, Biochemistry and Catalysis, Faculty of Chemistry, University of Bucharest, Romania. Her research interest is focused in the fields of Biocatalysis, Green Chemistry and Biomass Valorization. She is the author of more than 40 publications (38 ISI publications, h=12 and around 500 citations), 101 participations to the conferences (41 oral presentations and 60 posters) and 7 research projects.


We designed several biocatalytic system for the conversion of natural monoterpens into value-added products such as flavors and fragrances. An examples is the lipase-catalytic systems for α-pinene transformation to α-pinene oxide and further to campholenal, camphene, carveol, verbenol and verbenone. One of the models involved the lipase-based cross-linked aggregates design (cross-linked enzyme aggregates (CLEA) and cross-linked enzyme aggregates onto magnetic particles (CLEMPA)). Second model investigated the biotransformation α-pinene using a bifunctional biocatalysts designed as carbohydrate biopolymers entrapping lipase enzyme (lipase catalyzed the oxidation process followed by product izomerisation assisted by bio-polymer). In both cases, lipase catalysed the epoxidation of α-pinene using H2O2 as oxidation reagent and ethyl acetate as both acetate-supplier and solvent affording α-pinene oxide as the main product.
Second example of biocatalysis on this talk is the biphasic enzyme-based catalytic system for allylic oxidation of -pinene. The two phases consist : i) an organic solvent (e.g. pentane) hosting -pinene (substrate) and its derivatives (the reaction products), and ii) a buffer phase containing the dissolved peroxidase enzyme and a peroxi-based compound (e.g. H2O2). Thus, -pinene was oxidized at the allylic position by peroxide assisted of the peroxidase enzyme as biocatalyst. The biphasic enzyme-based system avoids the inconvenient of poor substrate/product solubility in aqueous phase. Also, faster kinetic and promising perspectives of process are provided due to one enzyme use instead of whole cell (multi-enzyme complex common for biotechnology).
Thirst example is a biocatalytic strategy for the synthesis of two important precursors in the pharmaceutical and perfumery industries: carvacrol and thymol. It involves the conversion of p-cymene by cytochrome P450BM3 monooxygenase, mimicking the in vivo synthesis in plants. The regioselective oxidation of p-cymene was performed in the presence of wild-type cytochrome P450 CYP102A1 monooxygenase from Bacillus megaterium.