Industrial Biotransformations

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Pyruvate decarboxylase Saccharomyces cerevisiae molasses 1) Reaction conditions [1]: 0.022 M, 3.3 g · L –1 [150.17 g · mol –1 ] medium: aqueous reaction type: carboligation catalyst: whole cells enzyme: 2-oxo-acid carboxy-lyase (α-ketoacid carboxylase, pyruvate decarboxylase) strain: Saccharomyces cerevisiae CAS (enzyme): [9001-04-01] 2) Remarks ● Phenylacetylcarbinol production from benzaldehyde by yeast is also operated on a large scale by Knoll (BASF, Germany) and Malladi Drugs (India). ● Phenylacetylcarbinol is chemically converted in a two-step process to d-pseudoephedrine: 3) Flow scheme Not published. O O H HO yeast E 1 + 2 O (1R)-3 EC 4.1.1.1 1 = acetaldehyde 2 = benzaldehyde 3 = phenylacetylcarbinol = PAC Krebs Biochemicals & Industries Ltd. Fig. 4.1.1.1 – 1 Fig. 4.1.1.1 – 2 O HO HO + CH3NH2 + H2 / Pt (1R)-phenylacetylcarbinol HN + Ac2O (1R, 2S)-ephedrine (1R, 2R)-pseudoephedrine (isoephedrine, (+)-threo-2methylamino-1-phenyl-1-propanyl) <strong>Industrial</strong> <strong>Biotransformations</strong>. Andreas Liese, Karsten Seelbach, Christian Wandrey (Eds.) Copyright © 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 3-527-31001-0 HO HN 447
Pyruvate decarboxylase Saccharomyces cerevisiae 4) Process parameters reactor type: batch reactor volume: 30,000 L capacity: 120 t · a –1 enzyme consumption: production site: 6 gyeast ·kgPAC Hyderabad, India company: Krebs Biochemicals & Industries Ltd., India 5) Product application ● Ephedrine and pseudoephedrine are used for the treatment of asthma, hay fever and as a bronchodilating agent and decongestant. 6) Literature ● Dr. Ravi, R.T., Krebs Biochemicals Ltd., personal communication EC 4.1.1.1 ● Cheetham, P.S.J. (1994) Case studies in applied biocatalysis – from ideas to products, in: Applied Biocatalysis (Cabral, J.M.S., Best, D., Boross, L., Tramper, J., eds.), pp. 87–89, Harwood Academic Publishers, USA 448
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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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Page 408 and 409: Penicillin acylase Escherichia coli
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Page 418 and 419: Aminoacylase Aspergillus oryzae S C
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Page 422 and 423: d-Hydantoinase Bacillus brevis Fig.
Page 424 and 425: d-Hydantoinase Bacillus brevis 3) F
Page 426 and 427: Hydantoinase / Carbamoylase Pseudom
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Page 432 and 433: -Lactamase Aureobacterium sp. 3) Fl
Page 434 and 435: -Lactamase Pseudomonas solanacearum
Page 436 and 437: Lactamase / Racemase Cryptococcus l
Page 438 and 439: Nitrilase Acidovorax facilis 1 = 2-
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Page 442 and 443: Nitrilase / Hydroxylase Agrobacteri
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Page 446 and 447: Dehalogenase Pseudomonas putida 1)
Page 448 and 449: Dehalogenase Pseudomonas putida 5)
Page 450 and 451: Haloalkane dehalogenase Alcaligenes
Page 452 and 453: Haloalkane dehalogenase Alcaligenes
Page 454 and 455: Haloalkane dehalogenase Enterobacte
Page 456 and 457: Halohydrin dehalogenase 1 = ethyl-(
Page 460 and 461: Acetolactate decarboxylase Bacillus
Page 462 and 463: Aspartate b-decarboxylase Pseudomon
Page 464 and 465: Aspartate b-decarboxylase Pseudomon
Page 466 and 467: Oxynitrilase Hevea brasiliensis 1 =
Page 468 and 469: N-Acetyl-d-neuraminic acid aldolase
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Page 472 and 473: Tyrosine phenol lyase Erwinia herbi
Page 474 and 475: Fumarase Corynebacterium glutamicum
Page 476 and 477: Fumarase Corynebacterium glutamicum
Page 478 and 479: Fumarase Brevibacterium flavum 4) P
Page 480 and 481: Enoyl-CoA hydratase Candida rugosa
Page 482 and 483: Enoyl-CoA hydratase Candida rugosa
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
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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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