Industrial Biotransformations

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90 3 Retrosynthetic Biocatalysis (Directed Evolution of an Amine Oxidase Possessing both Broad Substrate Specificity and High Enantioselectivity), Angew. Chem., Int. Ed. Engl. 42, 4807–4810. 41 Roberts, St.M. 2001, (Preparative Biotransformations), J. Chem. Soc., Perkin Trans. 1 (13), 1475–1499. 42 Faber, K. 2004, Biotransformations in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 330–331. 43 Faber, K. 2004, Biotransformations in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 251–252. 44 Huerta, F.F., Laxmi, Y.R.S., Bäckvall, J.-E. 2000, (Dynamic Kinetic Resolution of {alpha}-Hydroxy Acid Esters), Org. Lett. 2 (4), 1037–1040. 45 Yamamoto, K., Oishi, K., Fujimatsu, I., Komatsu, I. 1991, Production of R-(–)-mandelic Acid from Mandelonitrile by Alcaligenes faecalis ATCC 8750), Appl. Environ. Microbiol. 57, 3028–3032. 46 Faber, K. 2004, Biotransformations in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 302–305. 47 a) Ward, O.P., Singh, A. 2000, (Enzymatic Asymmetric Synthesis by Decarboxylases), Curr. Opin. Biotechnol. 11 (6), 520–526; b) Seoane, G. 2000, (Enzymatic C–C Bondforming Reactions in Organic Synthesis), Curr. Org. Chem. 4 (3), 283–304. 48 Demir, A.S., Hamamci, H., Sesenoglu, O., Neslihanoglu, R., Asikoglu, B., Capanoglu, D. 2002, (Fungal Deracemization of Benzoin), Tetrahedron Lett. 43, 6447–6449. 49 Wong, C.-H. 2002, (Formation of C–C Bonds), in Enzyme Catalysis on Organic Synthesis, (vol. 2), eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 931–966. 50 a) Nakamura, K., Miyai, T., Nozaki, K., Ushio, K., Ohno, A. 1986, (Diastereo- and Enantio-selective Reduction of 2-Methyl-3oxobutanoate by Bakers’ Yeast), Tetrahedron Lett. 27, 3155–3156; for more examples see Ward, R. 1995, (Dynamic Kinetic Resolution), Tetrahedron Asymmetry 6, 1475–1490. 51 a) Kim, M.-J., Choi, Y.K., Choi, M.Y., Kim, M.J., Park, J., 2001, (Lipase/Ruthenium-Catalyzed Dynamic Kinetic Resolution of Hydroxy Acids, Diols, and Hydroxy Aldehydes Protected with a Bulky Group UND: Enantioselective Synthesis of {beta}- Hydroxy Acid Derivatives via a One-Pot Aldol Reaction-Dynamic Kinetic Resolution), J. Org. Chem. 66, 4736; b) Huerta, F.F., Bäckvall, J.-E. 2001, (Enantioselective Synthesis of ß-Hydroxy Acid Derivatives via a One-Pot Aldol Reaction-Dynamic Kinetic Resolution), Org. Lett. 3, 1209–1212. 52 Osprian, I., Fechter, M.H., Griengl, H. 2003, (Biocatalytic Hydrolysis of Cyanohydrins: An Efficient Approach to Enantiopure b-Hydroxy Carboxylic Acids), J. Mol. Catal. B: Enzymatic 24–25, 89–98. 53 a) Inagaki, M., Hiratake, J., Nishioka, T., Oda, J. 1992, (One-pot Synthesis of Optically Active Cyanohydrin Acetates from Aldehydes via Lipase-catalyzed Kinetic Resolution Coupled with In Situ Formation and Racemization of Cyanohydrins), J. Org. Chem. 57, 5643–5649; b) Brand, S., Jones, M.F., Rayner, C.M. 1995, (The First Examples of Dynamic Kinetic Resolution by Enantioselective Acetylation of Hemithioacetals: An Efficient Synthesis of Homochiral-Acetoxysulfides), Tetrahedron Lett. 36, 8493–8496. 54 Sharfuddin, M., Narumi, A., Iwai, Y., Keiko, M., Yamada, S., Kakuchi, T., Kaga, H. 2003, (Lipase-catalyzed Dynamic Kinetic Resolution of Hemiaminals), Tetrahedron Asymmetry 14, 1581–1585. 55 Faber, K. 2004, Biotransformations in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 240–242. 56 Faber, K. 2004, Biotransformations in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 322–327. 57 a) Faber, K. 2004, Biotransformations in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 253–256; b) Boll, M., Fuchs, G., Heider, J. 2002, (Anaerobic Oxidation of Aromatic Compounds and Hydrocarbons), Curr. Opin. Chem. Biol. 6 (5), 604–611. 58 Flitsch, S., Grogan, G., Ashcroft, D. 2002, (Oxidation Reactions), in Enzyme Catalysis on Organic Synthesis, eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 1213–1241. 59 Kohli, R.M., Walsh, C.T. 2003, (Enzymology of Acyl Chain Macrocyclization in Natural Product Biosynthesis), Chem. Commun. (3), 297–307. 60 Hoh, C., Villela, M.F. 2000, (Enzyme Classification), in Industrial Biotransformations,
eds. Liese, A., Seelbach, K., Wandrey, C., Wiley-VCH, Weinheim. (p.) 54. 61 Crout, D.H.G., Vic, G. 1998, (Glycosidases and Glycosyl Transferases in Glycoside and Oligosaccharide Synthesis), Curr. Opin. Chem. Biol. 2 (1), 98–111. References 91 62 Faber, K. 2004, Biotransformations in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 249–252. 63 Hoh, C., Villela, M.F. 2000, (Enzyme Classification), in Industrial Biotransformations, eds. Liese, A., Seelbach, K., Wandrey, C, Wiley-VCH., Weinheim, (pp.) 51–53.
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Industrial Biotransformations Edite
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Industrial Biotransformations Secon
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Contents Preface to the first editi
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5 Basics of Bioreaction Engineering
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X Preface to the first edition many
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XII Preface to the second edition E
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XIV List of Contributors Prof. Dr.
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2 1 History of Industrial Biotransf
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10 1 History of Industrial Biotrans
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R' 16 O H N 1 History of Industrial
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38 2 The Enzyme Classification Tab.
Page 54 and 55: 40 2 The Enzyme Classification trib
Page 56 and 57: 42 2 The Enzyme Classification EC 1
Page 68 and 69: 54 2 The Enzyme Classification 2.2.
Page 70 and 71: 56 2 The Enzyme Classification The
Page 74 and 75: 60 2 The Enzyme Classification in g
Page 76 and 77: 62 2 The Enzyme Classification Refe
Page 78 and 79: 64 3 Retrosynthetic Biocatalysis 3.
Page 80 and 81: 66 3 Retrosynthetic Biocatalysis R
Page 90 and 91: 76 3 Retrosynthetic Biocatalysis R
Page 92 and 93: 78 3 Retrosynthetic Biocatalysis Wh
Page 102 and 103: 88 3 Retrosynthetic Biocatalysis Re
Page 106 and 107: 4 Optimization of Industrial Enzyme
Page 108 and 109: 4.2 Learning from Nature Nature its
Page 110 and 111: 4.3 Enzyme Production Using Bacteri
Page 112 and 113: 4.4 Improvements to Enzymes by Mole
Page 114 and 115: 1 4.4 Improvements to Enzymes by Mo
Page 116 and 117: 4.4 Improvements to Enzymes by Mole
Page 118 and 119: 4.5 Identification of Improved Enzy
Page 120 and 121: 4.5 Identification of Improved Enzy
Page 122 and 123: Galleron, N., Ghim, S.Y., Glaser, P
Page 124 and 125: ment, Relaxation, and Reversal of t
Page 126 and 127: 81 Goddard, J.-P., Reymond, J.-L. 2
Page 128 and 129: 5 Basics of Bioreaction Engineering
Page 130 and 131: where r p = selectivity to componen
Page 132 and 133: 5.1 Definitions operoxidase (CPO) h
Page 134 and 135: 5.1 Definitions The residence time
Page 136 and 137: 5.1 Definitions In iso-electric pre
Page 138 and 139: 5.2 Biocatalyst Kinetics formation
Page 140 and 141: 5.2 Biocatalyst Kinetics K M values
Page 142 and 143: v ˆ V max ‰SŠ KM 1‡ ‰PŠ KI
Page 144 and 145: 5.3 Basic Reactor Types and their M
Page 146 and 147: dx concentration [S] 0 [S] 1 [S] e
Page 148 and 149: 5.4 Biocatalyst Recycling and Recov
Page 150 and 151: . better stability, especially towa
Page 152 and 153: 5.4.2 Cross-linking 5.4 Biocatalyst
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. immobilization methods . substrat
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References Owing to the need for st
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40 Vuorilehto, K., Lütz, S., Wandr
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Common name of enzyme Name of strai
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Common name of enzyme Name of strai
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Alcohol dehydrogenase Neurospora cr
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Alcohol dehydrogenase Neurospora cr
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Alcohol dehydrogenase Rhodococcus e
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Alcohol dehydrogenase Rhodococcus e
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Alcohol dehydrogenase Acinetobacter
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Alcohol dehydrogenase Acinetobacter
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Dehydrogenase Zygosaccharomyces rou
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Alcohol dehydrogenase Lactobacillus
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Carbonyl reductase Escherichia coli
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Aldehyde reductase Escherichia coli
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Lactate dehydrogenase Staphylococcu
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d-Lactate dehydrogenase Leuconostoc
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d-Lactate dehydrogenase Leuconostoc
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d-Sorbitol dehydrogenase Gluconobac
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d-Sorbitol dehydrogenase Gluconobac
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Dehydrogenase Geotrichum candidum 1
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Ketoreductase 1 = ethyl-4-chloro-3-
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Dehydrogenase Candida sorbophila N
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Dehydrogenase Candida sorbophila N
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Reductase Pichia methanolica 1 = Et
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Reductase Aureobasidium pullulans S
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Reductase Nocardia salmonicolor SC
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Glutamate dehydrogenase / Glucose 1
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Leucine dehydrogenase Bacillus spha
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Leucine dehydrogenase Bacillus spha
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Phenylalanine dehydrogenase / Forma
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d-Aminoacid oxidase Trijonopsis var
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d-Amino acid oxidase Trigonopsis va
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Nicotinic acid hydroxylase Achromob
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Nicotinic acid hydroxylase Achromob
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Catalase Microbial source 1) Reacti
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Oxygenase Arthrobacter sp. 1) React
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Naphthalene dioxygenase Pseudomonas
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Naphthalene dioxygenase Pseudomonas
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Benzoate dioxygenase Pseudomonas pu
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Cyclohexanone monooxygenase Acineto
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Cyclohexanone monooxygenase Acineto
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Oxygenase Escherichia coli OH OH 1
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Monooxygenases / Aryl alcohol dehyd
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Styrene monooxygenase Escherichia c
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Styrene monooxygenase Escherichia c
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Monooxygenase Pseudomonas putida H
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Monooxygenase Streptomyces sp. SC 1
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Oxygenase Nocardia autotropica 1) R
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Monooxygenase Nocardia corallina 1
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Monooxygenase Nocardia corallina
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Monooxygenase Nocardia corallina O
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Oxidase Pseudomonas oleovorans 1) R
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Reductase Baker’s yeast 1 = oxois
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Oxidase Rhodococcus erythropolis 2
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Desaturase Rhodococcus sp. 1) React
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Desaturase Rhodococcus sp. 3) Flow
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Oxidase Beauveria bassiana 1) React
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Oxidase Beauveria bassiana ● The
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Cyclodextrin glycosyltransferase Ba
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d-Amino acid transaminase Bacillus
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d-Amino acid transaminase Bacillus
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Transaminase Bacillus megaterium 1)
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Lipase Burkholderia plantarii 2 (R,
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Lipase Burkholderia plantarii 3) Fl
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Lipase Pseudomonas cepacia 1 = cis-
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Lipase Pseudomonas cepacia 5) Produ
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Lipase Pseudomonas cepacia 2 F 1 =
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Lipase Pseudomonas cepacia 6) Liter
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Lipase Mucor miehei Fig. 3.1.1.3 -
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Lipase Mucor miehei 6) Literature E
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Lipase Porcine pancreas 5) Product
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Lipase Pseudomonas fluorescens Fig.
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Lipase Pseudomonas fluorescens O O
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Lipase Candida cylindracea ● In c
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Lipase Candida antarctica 2 F 1) Re
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Lipase Candida antarctica ● It sh
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Lipase Candida antarctica ● The p
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Lipase Candida antarctica 3) Flow s
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Lipase Arthrobacter sp. ● For thi
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Lipase Serratia marescens MeO R MeO
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Lipase Serratia marescens Fig. 3.1.
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Lipase Pseudomonas cepacia 1) React
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Lipase Candida antarctica 1) Reacti
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Lipase Candida antarctica 4) Proces
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-Galactosidase Saccharomyces lactis
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Lipase Pseudomonas cepacia ● The
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Lactonase Fusarium oxysporum 1 = pa
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Lactonase Fusarium oxysporum Fig. 3
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Lactonase Fusarium oxysporum 5) Pro
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Glutaryl amidase Escherichia coli F
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Glutaryl amidase Escherichia coli 6
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Glutaryl amidase Pseudomonas sp. 3)
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a-Amylase / Amyloglucosidase Bacill
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Nucleosidase / Phosphorylase Erwini
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Aminopeptidase Pseudomonas putida 1
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Aminopeptidase Pseudomonas putida
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Aminopeptidase Pseudomonas putida 3
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Aminopeptidase Pseudomonas putida
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Carboxypeptidase B Pig Pancreas 3)
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Trypsin Pig Pancreas 2) Remarks ●
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Subtilisin Bacillus licheniformis 1
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Subtilisin Bacillus licheniformis
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Subtilisin Bacillus licheniformis
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Subtilisin Bacillus sp. EtOOC (R/S)
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Subtilisin Bacillus sp. drug discov
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Subtilisin Bacillus lentus 1 = (R,S
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Thermolysin Bacillus thermoproteoly
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Thermolysin Bacillus thermoproteoly
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Amidase Comamonas acidovorans 1) Re
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Amidase Klebsiella terrigena 2 H N
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Amidase Klebsiella terrigena 6) Lit
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Amidase Klebsiella oxytoca company:
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Urease Lactobacillus fermentum ●
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Penicillin amidase Escherichia coli
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Penicillin amidase Bacillus megater
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Penicillin acylase Escherichia coli
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Aminoacylase Aspergillus niger 2 N
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Aminoacylase Aspergillus niger 3) F
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Aminoacylase Aspergillus oryzae S C
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Aminoacylase Aspergillus oryzae 3)
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d-Hydantoinase Bacillus brevis Fig.
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d-Hydantoinase Bacillus brevis 3) F
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Hydantoinase / Carbamoylase Pseudom
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l-Hydantoinase Arthrobacter sp. DSM
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l-Hydantoinase Arthrobacter sp. DSM
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-Lactamase Aureobacterium sp. 3) Fl
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-Lactamase Pseudomonas solanacearum
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Lactamase / Racemase Cryptococcus l
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Nitrilase Acidovorax facilis 1 = 2-
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Nitrilase Escherichia coli 1) React
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Nitrilase / Hydroxylase Agrobacteri
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Nitrilase / Hydroxylase Alcaligenes
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Dehalogenase Pseudomonas putida 1)
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Dehalogenase Pseudomonas putida 5)
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Haloalkane dehalogenase Alcaligenes
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Haloalkane dehalogenase Alcaligenes
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Haloalkane dehalogenase Enterobacte
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Halohydrin dehalogenase 1 = ethyl-(
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Pyruvate decarboxylase Saccharomyce
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Acetolactate decarboxylase Bacillus
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Aspartate b-decarboxylase Pseudomon
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Aspartate b-decarboxylase Pseudomon
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Oxynitrilase Hevea brasiliensis 1 =
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N-Acetyl-d-neuraminic acid aldolase
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N-Acetyl-d-neuraminic acid aldolase
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Tyrosine phenol lyase Erwinia herbi
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Fumarase Corynebacterium glutamicum
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Fumarase Corynebacterium glutamicum
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Fumarase Brevibacterium flavum 4) P
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Enoyl-CoA hydratase Candida rugosa
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Enoyl-CoA hydratase Candida rugosa
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Tryptophan synthase Escherichia col
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Malease Pseudomonas pseudoalcaligen
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Malease Pseudomonas pseudoalcaligen
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Nitrile hydratase Pseudomonas chlor
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Nitrile hydratase Rhodococcus rhodo
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Carnitine dehydratase Escherichia c
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Aspartase Escherichia coli 3) Flow
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Aspartase Escherichia coli 5) Produ
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Aspartase Brevibacterium flavum 3)
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l-Aspartase Escherichia coli 3) Flo
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l-Phenylalanine ammonia-lyase Rhodo
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Amino acid racemase Amycolatopsis o
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GlcNAc 2-epimerase Escherichia coli
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Xylose isomerase Bacillus coagulans
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Xylose isomerase Bacillus coagulans
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a-Glucosyl transferase Protaminobac
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516 7 Quantitative Analysis of Indu
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522 Index of enzyme name enzyme nam
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524 Index of enzyme name enzyme nam
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526 Index of strain strain enzyme n
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532 Index of company company strain
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534 Index of company company strain
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536 Index of starting material star
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546 Index of product product enzyme
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