Industrial Biotransformations

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Lipase Serratia marescens MeO R MeO R Fig. 3.1.1.3 – 2 3) Flow scheme Fig. 3.1.1.3 – 3 Substrate HO O COOR O COOMe OH COOMe COOMe R CH3 C2H5 C3H7 C 4H 9 C 5H 11 CH 3 H OCH 3 CH 3 Specific activity (U*mg -1 ) a 570 320 510 640 650 640 560 350 a)/ b) for conditions of assays see lit. H. Matsumane and T. Shibatani H 0 0 0 Substrate R R COOMe CH2 O COR CH O COR CH2 O COR CH 3 C 3H 7 C 5H 11 C 7H 15 C9H19 C 11H 23 C 13H 27 C 15H 31 CH3 C 3H 7 C 5H 11 C 7H 15 C 9H 19 C 11H 23 C 13H 27 C 15H 31 EC 3.1.1.3 Specific activity (U*mg -1 ) b 61 450 91 620 570 380 210 91 270 3300 2500 3500 1500 140 120 56 307
Lipase Serratia marescens 4) Process parameters yield: 40–45 % ee: 99.9 % reactor type: batch, hollow fibre reactor (Sepracor Inc. Massachusetts, USA) capacity: 40 kg (–)-MPGM · m –2 ·a –1 down stream processing: crystallization enzyme activity: 1.6 · 105 U·m –2 enzyme stability: start-up date: t½ = 127 h 1993 production site: Tanabe Seiyaku Co., Japan company: Tanabe Seiyaku Co. Ltd., Japan 5) Product application ● The product is an intermediate in the synthesis of diltiazem. EC 3.1.1.3 ● Diltiazem hydrochloride is a coronary vasodilator and a calcium channel blocker (for anti-anginal and anti-hypertensive actions) and is produced worldwide in excess of 100 t · a –1 . ● In comparison to the chemical route only 5 steps (instead of 9 steps) are necessary. The kinetic resolution is carried out in an earlier step during the synthesis resulting in reduction of waste: 308
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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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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
Page 306 and 307: Lipase Candida cylindracea ● In c
Page 308 and 309: Lipase Candida antarctica 2 F 1) Re
Page 310 and 311: Lipase Candida antarctica ● It sh
Page 312 and 313: Lipase Candida antarctica ● The p
Page 314 and 315: Lipase Candida antarctica 3) Flow s
Page 316 and 317: Lipase Arthrobacter sp. ● For thi
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Page 322 and 323: Lipase Pseudomonas cepacia 1) React
Page 324 and 325: Lipase Candida antarctica 1) Reacti
Page 326 and 327: Lipase Candida antarctica 4) Proces
Page 328 and 329: -Galactosidase Saccharomyces lactis
Page 330 and 331: Lipase Pseudomonas cepacia ● The
Page 332 and 333: Lactonase Fusarium oxysporum 1 = pa
Page 334 and 335: Lactonase Fusarium oxysporum Fig. 3
Page 336 and 337: Lactonase Fusarium oxysporum 5) Pro
Page 338 and 339: Glutaryl amidase Escherichia coli F
Page 340 and 341: Glutaryl amidase Escherichia coli 6
Page 342 and 343: Glutaryl amidase Pseudomonas sp. 3)
Page 344 and 345: a-Amylase / Amyloglucosidase Bacill
Page 346 and 347: Nucleosidase / Phosphorylase Erwini
Page 348 and 349: Aminopeptidase Pseudomonas putida 1
Page 350 and 351: Aminopeptidase Pseudomonas putida
Page 352 and 353: Aminopeptidase Pseudomonas putida 3
Page 354 and 355: Aminopeptidase Pseudomonas putida
Page 356 and 357: Carboxypeptidase B Pig Pancreas 3)
Page 362 and 363: 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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