Pearson Introduction to Biotechnology: International by William J. Thieman, Michael A. Palladino
By William J. Thieman, Michael A. Palladino
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Additional resources for Pearson Introduction to Biotechnology: International Edition, 2 E, Question Bank
Sample text
By hydrolysis of the nitrile group an -amino acid is produced. This synthesis is called the Strecker synthesis. , 1985). Another method is reductive animation by NH4 + of the carbonyl group of an -keto acid using for instance alcohol dehydrogenase. 5) using hydrolytic enzymes. All of the mentioned methods give predominantly the natural L-form of the amino acid. By using resolution both the L- and the D-forms are obtainable, however, since the L-form has higher economic interests, processes are designed to give only this enantiomer.
This interest in turn is mainly due to the need to synthesise enantiopure compounds as chiral building blocks for drugs and agrochemicals. Chiral building blocks can be provided by three basically different methods; i) by chemical transformation of enantiopure natural products ii) by asymmetric synthesis iii) by resolution of a racemic mixture. Enzymes as chiral catalysts play a role in all three methods. In nature enzymes catalyse all production of chiral compounds. In the laboratory enzymes can catalyse asymmetric synthesis, as well as resolve racemates.
Catalytic chiral epoxidations and dihydroxylations have been performed using (−) or (+)-diethyl tartrate and cinchona alkaloids as source of chirality, respectively (Sharpless). Chiral catalysts consisting of binaphthol chelated metals have been successfully employed for reductions of ketones (Noyori). Recently, using chiral binaphthol Mn (II) catalysts, racemic epoxides have been resolved by hydrolysis (Jacobsen). 2 Why are Enzymes of Interest to an Organic Chemist? Almost all chemical reactions need a catalyst to take place for instance by, acid, base, metals etc.