Industrial Biotransformations

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Monooxygenase Nocardia corallina 1 = alkene 2 = epoxide Fig. 1.14.14.1 – 1 E R R 1 2 EC 1.14.14.1 1) Reaction conditions T: 30 °C medium: two phase : aqueous / organic reaction type: epoxidation catalyst: suspended whole cells enzyme: substrate, reduced-flavoprotein : oxygen oxidoreductase (unspecific monooxygenase) strain: Nocardia corallina B 276 CAS (enzyme): [62213–32–5] O Nippon Mining Holdings, Inc. 245
Monooxygenase Nocardia corallina 2) Remarks ● The alkene monooxygenase catalyzes the epoxidation of terminal and sub-terminal alkenes: Fig. 1.14.14.1 – 2 H H O O O n (n >_ 0) n (n >_ 0) n (n = 4, 5...) ● The stereospecific epoxidation yields predominantly the (R)-enantiomer. ● The epoxidation activity is formed constitutively since the conversion takes place independent of the type of carbon source used (alkene or glucose). ● The biotransformation is carried out in a conventional fermentation system. O O n (n >_ 4) (n = 1, 2...) EC 1.14.14.1 ● The substrates have to be divided in three main classes: short-chain gaseous (C 3-C 5), short chain – liquid (C 6-C 12), long-chain (C >12) olefins. 246 Cl F F F Me OMe Me O Cl O O n F F F F O F
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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
Page 206 and 207: Reductase Pichia methanolica 1 = Et
Page 208 and 209: Reductase Aureobasidium pullulans S
Page 210 and 211: Reductase Nocardia salmonicolor SC
Page 212 and 213: Glutamate dehydrogenase / Glucose 1
Page 214 and 215: Leucine dehydrogenase Bacillus spha
Page 216 and 217: Leucine dehydrogenase Bacillus spha
Page 218 and 219: Phenylalanine dehydrogenase / Forma
Page 220 and 221: d-Aminoacid oxidase Trijonopsis var
Page 222 and 223: d-Amino acid oxidase Trigonopsis va
Page 224 and 225: Nicotinic acid hydroxylase Achromob
Page 226 and 227: Nicotinic acid hydroxylase Achromob
Page 228 and 229: Catalase Microbial source 1) Reacti
Page 230 and 231: Oxygenase Arthrobacter sp. 1) React
Page 232 and 233: Naphthalene dioxygenase Pseudomonas
Page 234 and 235: Naphthalene dioxygenase Pseudomonas
Page 236 and 237: Benzoate dioxygenase Pseudomonas pu
Page 238 and 239: Cyclohexanone monooxygenase Acineto
Page 240 and 241: Cyclohexanone monooxygenase Acineto
Page 242 and 243: Oxygenase Escherichia coli OH OH 1
Page 244 and 245: Monooxygenases / Aryl alcohol dehyd
Page 246 and 247: Styrene monooxygenase Escherichia c
Page 248 and 249: Styrene monooxygenase Escherichia c
Page 250 and 251: Monooxygenase Pseudomonas putida H
Page 252 and 253: Monooxygenase Streptomyces sp. SC 1
Page 254 and 255: Oxygenase Nocardia autotropica 1) R
Page 258 and 259: Monooxygenase Nocardia corallina
Page 260 and 261: Monooxygenase Nocardia corallina O
Page 262 and 263: Oxidase Pseudomonas oleovorans 1) R
Page 264 and 265: Reductase Baker’s yeast 1 = oxois
Page 266 and 267: Oxidase Rhodococcus erythropolis 2
Page 268 and 269: Desaturase Rhodococcus sp. 1) React
Page 270 and 271: Desaturase Rhodococcus sp. 3) Flow
Page 272 and 273: Oxidase Beauveria bassiana 1) React
Page 274 and 275: Oxidase Beauveria bassiana ● The
Page 276 and 277: Cyclodextrin glycosyltransferase Ba
Page 278 and 279: d-Amino acid transaminase Bacillus
Page 280 and 281: d-Amino acid transaminase Bacillus
Page 282 and 283: Transaminase Bacillus megaterium 1)
Page 284 and 285: Lipase Burkholderia plantarii 2 (R,
Page 286 and 287: Lipase Burkholderia plantarii 3) Fl
Page 288 and 289: Lipase Pseudomonas cepacia 1 = cis-
Page 290 and 291: Lipase Pseudomonas cepacia 5) Produ
Page 292 and 293: Lipase Pseudomonas cepacia 2 F 1 =
Page 294 and 295: Lipase Pseudomonas cepacia 6) Liter
Page 296 and 297: Lipase Mucor miehei Fig. 3.1.1.3 -
Page 298 and 299: Lipase Mucor miehei 6) Literature E
Page 300 and 301: Lipase Porcine pancreas 5) Product
Page 302 and 303: Lipase Pseudomonas fluorescens Fig.
Page 304 and 305: 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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Industrial Biotransformations

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