Biotransformations in organic chemistry, advantages and limitations. Selectivity of the enzymes and models. Analysis of the various classes of enzymes and their use in laboratory and industrial organic syntheses. Hydrolases: esterases and lipases. Oxido-reductases: isolated enzymes and microorganisms. Lipoxygenases. Dioxygenases. Aldolases. Non conventional biotransformation: immobilized enzymes, modified enzymes, artificial cells and catalytic antibodies
Kurt Faber, Biotransformation in Organic Chemistry, A textbook. Springer ed. 2011, Sixth ed.
Learning Objectives
Students are provided with the tools and the necessary knowledge for the comprehension, use, and developments of enzymatic processes employed in the synthesis and chemical transformation of products of biological, pharmaceutical, and industrial interest
Prerequisites
none
Teaching Methods
frontal lessons
Further information
Short lab experiences at the end of the course about the use of enzymes in organic synthesis
Type of Assessment
Oral exams
Course program
Biotransformations: uses and limitations. Chiral synthons. Enzyme selectivity and models. Hydrolases: mechanism and applications fields. Esterases, meso tricks, lipases, kinetic resolution and dynamic kinetic resolutions. Lipases in non aqueous solvents. Oxido-reductases: use of isolated enzymes, regeneration of the co-factor, microorganisms (baker’s yeast). Lipoxygenases and hydro-peroxide liase. Dioxigenases, oxidation of aromatic compounds to diols and synthetic applications. Aldolases and formation of new C-C bonds. Non conventional biotransformation: immobilized enzymes, conformational engineering. Modified enzymes, artificial cells, monoclonal catalytic antibodies.