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Asymmetric Biocatalytic Cannizzaro Reaction: Control of the Redox Equilibrium

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Asymmetric Biocatalytic Cannizzaro Reaction: Control of the Redox Equilibrium Asymmetric biocatalytic Cannizzaro reaction: control of the redox equilibrium Diplomarbeit Zur Erlangung des akademischen Grades „Magister rerum naturalium“ an der Naturwissenschaftlichen Fakultät der Karl-Franzens Universität Graz vorgelegt von Horst Lechner Diese Arbeit wurde im Zeitraum von März 2010 bis März 2011 am Institut für Chemie an der Karl-Franzens Universität Graz unter der Betreuung von Prof. Kurt Faber durchgeführt. The scientist is not a person, who gives the right answers, he is one who asks the right questions. Claude Lévi-Strauss, Le Cru et le cuit, 1964 1 Acknowledgments At this page all the people who contributed to the successful completion of this diploma thesis should be mentioned. At first there are my parents for their support in every way. Additionally I have to mention my family and my friends for giving me the kind of atmosphere and environment I needed to become how I am. Then I want to thank Kurt Faber, my supervisor, for his scientific support and the possibility to work in his group. Silvia Glück was a big support at the beginning and at the end of my thesis, introducing me into to the work and the scientific writing. I would also like to thank the whole Fab-Crew, especially Wolfgang Kroutil, who was always there with some good ideas if problems occurred, Michi Fuchs – without him I would be a little bit lost in the fields of organic synthesis and Christiane Wünsch – she build the basis for this work with her thesis. And of course, all the other groups members working in the labs during my time there are to acknowledge: Babsi, Markus, Kathi D., Jörg, Hansi, Kathi T., Francesco, Christoph, Elina, Verena, Christine, Aashrita, Michi T, Dorina, Frau Schwarzl and Barbara. I had a great time! Furthermore I got some help from the Strubi-group, especially Monika Oberer concerning expression problems. 2 Abstract The Cannizzaro reaction is a disproportion reaction whereat two aldehydes are reduced to an alcohol and oxidized to an acid. In nature some alcohol dehydrogenases (ADHs) are able to catalyse this reaction, recycling the cofactor NAD(H)/NADP(H) during the reaction. From previous work done in our group it is already known that several ADHs have this property. During this work two more purified ADHs are added to this list (Candida magnolia ADH3 and horse liver ADH). Since no balanced ratio of the formed alcohol and acid was to observe with the available ADHs a second enzyme was incorporated into the system. Since the reductive half reaction was always favoured an aldehyde dehydrogenase (ALDH) was introduced for supporting oxidation. With the standard substrates benzaldehyde, 2-phenylacetaldehyde and rac-2-phenylpropanal two crude enzyme preparations, benzaldehyde dehydrogenase from Acetinobacter sp. and a commercially available ALDH from baker’s yeast were tested to obtain an equalized product ratio. This aim could be accomplished for benzaldehyde and 2-phenylacetaldehyde. Several other ALDHs were tested especially concerning activity and enantioselectivity with rac-2- phenylpropanal. The second part of this thesis covers the extension of the racemic substrate spectrum for further enantioselective dismutation. In the previous work it was shown that the enantioselective reduction and oxidation of rac-2-phenylpropanal is catalyzed with moderate enantiomeric excess. Now one of the new purified ADHs, namely horse liver ADH, showed very good results for reduction and moderate results for oxidation of this substrate. To get more insight into the enantioselectivity of these enzymes some more tests have to be done. As a consequence rac-2-phenylbutanal and rac-2-(4-isobutyl)-phenylpropanal were synthesized and tested. With the latter substrate, although just 3 out of 9 enzymes were able using it as substrate for dismutation, quite good results were achieved with Candida magnolia ADH3. A time-conversion curve was generated to get estimated initial rates for the oxidation of alcohols (2-octanol, 1-phenylethanol) and the reduction of aldehydes (2-octanone, acetophenone) for all ADHs. During this study the influence of magnesium(II) ions on enzyme activity were evaluated. 3 Zusammenfassung Die Cannizzaro Reaktion ist eine Disproportionierungsreaktion in der zwei Aldehyde zu einem Alkohol reduziert, beziehungsweise zu einer Säure oxidiert werden. In der Natur wird diese Reaktion von Alkoholdehydrogenasen (ADHs) katalysiert, wobei der Cofaktor NAD(H)/NADP(H) recycelt wird. Durch die vorangegangen Experimente, welche in unserer Arbeitgruppe durchgeführt wurden, war schon bekannt, dass mehrere ADHs diese Funktion haben. Während dieser Diplomarbeit konnten zwei weitere ADHs dieser Liste hinzugefügt werden (Candida magnolia ADH3 und horse liver (Pferdeleber) ADH). Aufgrund des unausgewogenen Verhältnisses der Produkte, Alkohol und Säure, mit allen vorhandenen ADHs, wurde ein zweites Enzym eingeführt. Da die Reduktion im Gegensatz zur Oxidation bevorzugt war, wurde eine Aldehyddehydrogenase (ALDH) verwendet um die benachteiligte Oxidation zu unterstützen. Mit den Standardsubstraten Benzaldehyd, 2-Phenylacetaldehyd und rac-2-Phenylpropanal wurden zwei unaufgereinigte Enzympräperationen getestet und zwar Benzaldehyde Dehydrogenase von Acetinobacter sp. und gekaufte Bäckerhefe ALDH um ein ausgewogenes Produktverhältnis zu erreichen. Dieses Ziel konnte für Benzaldehyd und 2-Phenylacetaldehyd erreicht werden. Mehrere andere ALDHs wurden bezüglich ihrer Aktivität und Enantioselektivität besonders bezüglich rac-2-Phenylpropanal getestet. Der zweite Teil dieser Diplomarbeit behandelt die Erweiterung des Substratspektrums um weitere razemische Substrate für die enantioselektive Dismutation. In einer vorangegangen Arbeit wurde bereits gezeigt, dass die enantioselektive Reduktion und Oxidation von rac-2-Phenylpropanal mit moderaten Ergebnissen katalysiert wird. Mit einer der zwei neuen ADHs, nämlich der horse liver ADH, konnten sehr gute Ergebnisse für die Reduktion und moderate Ergebnisse für die Oxidation dieses Substrates erreicht werden. Um mehr über die Enantioselektivität der Enzyme zu erfahren wurden weitere Experimente durchgeführt. Somit wurden rac-2-Phenylbutanal and rac-2-(4-Isobutyl)-Phenylpropanal synthetisiert und getestet. Das zweite Substrat konnte nur 3 der 9 ADHs disproportionieren, wobei mit Candida magnolia ADH3 relativ gute Ergebnisse erzielt wurden. Eine Zeit-Umsatz Kurve würde erstellt um geschätzte Anfangsgeschwindigkeiten für die Oxidation von Alkoholen (2-Octanol, 1-Phenylethanol) und die Reduktionen von Aldehyden (2- Octanon, Acetophenon) für alle Enzyme zu bekommen. Während dieser Experimente wurde auch der Einfluss vom Magnesium(II) Ionen auf die Enzymaktivität beobachtet. 4 Contents 1 Introduction.........................................................................................................................................6 1.1 Short-chain alcohol dehydrogenases (SDR)...........................................................................7 1.2 The medium-chain dehydrogenase/reductase family (MDR)...........................................10 1.3 Other enzymes with dismutase activity.................................................................................13 1.4 Aldehyde dehydrogenases.......................................................................................................15 1.5 Aim of this thesis .....................................................................................................................17 2 Results and discussion......................................................................................................................21 2.1 Balanced oxidation – reduction product equilibrium………………………………...21 2.1.1 Crude aldehyde dehydrogenases........................................................................................21 2.1.2 Purified aldehyde dehydrogenases ....................................................................................25 2.2 New aldehyde dehydrogenases...............................................................................................26 2.3 Balancing the ratio with cofactors .........................................................................................27 2.4 Formaldehyde dismutase – a “real” dismutase ....................................................................28 2.5 Asymmetric Cannizzaro reaction...........................................................................................29 2.5.1 Determination of the absolute stereo configuration ......................................................31 2.6 Expression and purification of ADH-3, -4, -T, BALDH and BYALDH4 .....................32 2.7 Change of enzymatic rates due the influence of Magnesium (II) .....................................34 2.8 Conclusion ................................................................................................................................38 2.9 Outlook......................................................................................................................................38 3 Experimental part..............................................................................................................................41 3.1 Materials.....................................................................................................................................41 3.2 Microbiological work...............................................................................................................42 3.3 Protein expression....................................................................................................................46
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