Industrial Biotransformations

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520 7 Quantitative Analysis of Industrial Biotransformations When the substrate or product is not a liquid but a solid with a low solubility, the high product titers required for industrial processes may also lead to suspension reactions. Product precipitation occurs in at least 15 industrial processes, usually in aqueous solvents. In about half of these cases, a suspension of a substrate is converted into a suspension of a product. The product titer has been found for a minority of the processes (see Figure 7.8), but this may be sufficient to draw some interesting conclusions. Only in rare cases is the product titer below 10 g L –1 . In most cases it is well above 100 g L –1 , with occasional values of about 500 g L –1 , irrespective of the product type. Thus, achievement of high product titers could be one of the strong points of biotransformation processes. product titer in g/L > 300 100 to 300 30 to 100 10 to 30 3to10 1to3
Index of enzyme name enzyme name EC number 521 strain company page Acetolactate decarboxylase 4.1.1.5 Bacillus brevis Novo Nordisk, Denmark 449 Alcohol dehydrogenase 1.1.1.1 Acinetobacter calcoaceticus Bristol-Myers Squibb, USA 162 Lactobacillus brevis Wacker Chemie, Germany 170 Lactobacillus kefiri Jülich Fine Chemicals GmbH 167 Neurospora crassa Zeneca Life Science Molecules, U.K. 153 Rhodococcus erythropolis Forschungszentrum Jülich GmbH, Germany 157 Aldehyde reductase 1.1.1.2 Lonza AG, Switzerland 174 Amidase 3.5.1.4 Comamonas acidovorans Lonza AG, Switzerland 377 Klebsiella oxytoca Lonza AG, Switzerland 382 Klebsiella terrigena Lonza AG, Switzerland 379 d-Amino acid oxidase 1.4.3.3 Trigonopsis variabilis ATCC 10679 Bristol-Myers Squibb, USA 211 Trijonopsis variabilis Sandoz AG, Switzerland 209 Amino acid racemase 5.1.1.10 Amycolatopsis orientalis subsp. lurida Degussa AG, Germany 504 d-Amino acid transaminase 2.6.1.21 Bacillus sp. NSC Technologies, USA 267 Aminoacylase 3.5.1.14 Aspergillus niger Celltech Group plc, U.K. 403 Aspergillus oryzae Degussa AG, Germany 407 Aminopeptidase 3.4.11.1 Pseudomonas putida DSM, The Netherlands 337 a-Amylase 3.2.1.1 Bacillus licheniformis Several companies 332 Amyloglucosidase 3.2.1.3 Aspergillus niger Several companies 332 Aryl alcohol dehydrogenase 1.1.1.90 Pseudomonas putida ATCC 33015 Pfizer Inc., USA 233 Aspartase 4.3.1.1 Brevibacterium flavum Mitsubishi Chemical Corporation, Japan 498 Escherichia coli BioCatalytics Inc., USA 494 Kyowa Hakko Kogyo Co., Ltd., Japan 496 l-Aspartase 4.3.1.1 Escherichia coli Tanabe Seiyaku Co., Ltd., Japan 500 Aspartate b-decarboxylase 4.1.1.12 Pseudomonas dacunhae Tanabe Seiyaku Co., Japan 451 Benzaldehyde dehydrogenase 1.2.1.28 Pseudomonas putida ATCC 33015 Pfizer Inc., USA 233 Benzoate dioxygenase 1.14.12.10 Pseudomonas putida ICI, U.K. 225 Carbamoylase 3.5.1.77 Pseudomonas sp. Dr. Vig Medicaments, India 415 Industrial Biotransformations. Andreas Liese, Karsten Seelbach, Christian Wandrey (Eds.) Copyright © 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 3-527-31001-0
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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.
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40 2 The Enzyme Classification trib
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42 2 The Enzyme Classification EC 1
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54 2 The Enzyme Classification 2.2.
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56 2 The Enzyme Classification The
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60 2 The Enzyme Classification in g
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62 2 The Enzyme Classification Refe
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64 3 Retrosynthetic Biocatalysis 3.
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66 3 Retrosynthetic Biocatalysis R
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76 3 Retrosynthetic Biocatalysis R
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78 3 Retrosynthetic Biocatalysis Wh
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88 3 Retrosynthetic Biocatalysis Re
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90 3 Retrosynthetic Biocatalysis (D
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4 Optimization of Industrial Enzyme
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4.2 Learning from Nature Nature its
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4.3 Enzyme Production Using Bacteri
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4.4 Improvements to Enzymes by Mole
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1 4.4 Improvements to Enzymes by Mo
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4.4 Improvements to Enzymes by Mole
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4.5 Identification of Improved Enzy
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4.5 Identification of Improved Enzy
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Galleron, N., Ghim, S.Y., Glaser, P
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ment, Relaxation, and Reversal of t
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81 Goddard, J.-P., Reymond, J.-L. 2
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5 Basics of Bioreaction Engineering
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where r p = selectivity to componen
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5.1 Definitions operoxidase (CPO) h
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5.1 Definitions The residence time
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5.1 Definitions In iso-electric pre
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5.2 Biocatalyst Kinetics formation
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5.2 Biocatalyst Kinetics K M values
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v ˆ V max ‰SŠ KM 1‡ ‰PŠ KI
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5.3 Basic Reactor Types and their M
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dx concentration [S] 0 [S] 1 [S] e
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5.4 Biocatalyst Recycling and Recov
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. better stability, especially towa
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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
Page 480 and 481: Enoyl-CoA hydratase Candida rugosa
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Page 484 and 485: Tryptophan synthase Escherichia col
Page 486 and 487: Malease Pseudomonas pseudoalcaligen
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Page 490 and 491: Nitrile hydratase Pseudomonas chlor
Page 492 and 493: Nitrile hydratase Rhodococcus rhodo
Page 500 and 501: Carnitine dehydratase Escherichia c
Page 506 and 507: Aspartase Escherichia coli 3) Flow
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Page 510 and 511: Aspartase Brevibacterium flavum 3)
Page 512 and 513: l-Aspartase Escherichia coli 3) Flo
Page 514 and 515: l-Phenylalanine ammonia-lyase Rhodo
Page 516 and 517: Amino acid racemase Amycolatopsis o
Page 518 and 519: GlcNAc 2-epimerase Escherichia coli
Page 520 and 521: Xylose isomerase Bacillus coagulans
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Page 524 and 525: a-Glucosyl transferase Protaminobac
Page 526 and 527: 516 7 Quantitative Analysis of Indu
Page 528 and 529: 518 7 Quantitative Analysis of Indu
Page 532 and 533: 522 Index of enzyme name enzyme nam
Page 534 and 535: 524 Index of enzyme name enzyme nam
Page 536 and 537: 526 Index of strain strain enzyme n
Page 542 and 543: 532 Index of company company strain
Page 544 and 545: 534 Index of company company strain
Page 546 and 547: 536 Index of starting material star
Page 556 and 557: 546 Index of product product enzyme
Page 566: 556 Index of product product enzyme
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Industrial Biotransformations

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