Industrial Biotransformations

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Thermolysin Bacillus thermoproteolyticus 3) Flow scheme Fig. 3.4.24.27 – 3 4) Process parameters selectivity: > 99.9 % ee: > 99.9 % reactor type: batch capacity: ~ 10,000 t a –1 worldwide; ~ 2,500 t a –1 by enzymatic coupling down stream processing: filtration start-up date: 1988 company: DSM, The Netherlands 5) Product application ● Aspartame is used as a low-calorie sweeteener in food, including soft drinks, table-top sweeteners, dairy products, instant mixes, dressings, jams, confectionery, toppings and in pharmaceuticals. ● Aspartame is a sweetener which is 200 times sweeter than sucrose. ● It was first approved in France in 1979. ● The first trademark was Nutrasweet TM (by Monsanto). EC 3.4.24.27 375
Thermolysin Bacillus thermoproteolyticus 6) Literature ● Harada, T., Irino, S., Kunisawa, Y., Oyama, K. (1996) Improved enzymatic coupling reaction of N-protected-l-aspartic acid and phenylalanine methyl ester, Holland Sweetener Company, The Netherlands, EP 0768384 A1 ● Kirchner, G., Salzbrenner, E., Werenka, C., Boesten, W. (1997) Verfahren zur Herstellung von Z-l-Asparaginsäure-Dinatriumsalz aus Fumarsäure, DSM Chemie Linz GmbH, Austria, Holland Sweetener Company, The Netherlands, EP 0832982 A2 ● Oyama, K. (1992) The industrial production of aspartame. In: Chirality in Industry (Collins, A.N., Sheldrake, G.N., Crosby, J., eds.), pp. 237–247, John Wiley & Sons Ltd., New York ● Sheldon, R.A. (1993) Chirotechnology, Marcel Dekker, New York, 235 ● Wiseman, A. (1995) Handbook of Enzyme Biotechnology, Ellis Horwood, London 376 EC 3.4.24.27
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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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Page 338 and 339: Glutaryl amidase Escherichia coli F
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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 ●
Page 368 and 369: Subtilisin Bacillus licheniformis 1
Page 372 and 373: Subtilisin Bacillus licheniformis
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Page 378 and 379: Subtilisin Bacillus sp. EtOOC (R/S)
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Page 384 and 385: Thermolysin Bacillus thermoproteoly
Page 388 and 389: Amidase Comamonas acidovorans 1) Re
Page 390 and 391: Amidase Klebsiella terrigena 2 H N
Page 392 and 393: Amidase Klebsiella terrigena 6) Lit
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Page 396 and 397: Urease Lactobacillus fermentum ●
Page 398 and 399: Penicillin amidase Escherichia coli
Page 402 and 403: Penicillin amidase Bacillus megater
Page 408 and 409: Penicillin acylase Escherichia coli
Page 414 and 415: Aminoacylase Aspergillus niger 2 N
Page 416 and 417: Aminoacylase Aspergillus niger 3) F
Page 418 and 419: Aminoacylase Aspergillus oryzae S C
Page 420 and 421: Aminoacylase Aspergillus oryzae 3)
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
Page 428 and 429: l-Hydantoinase Arthrobacter sp. DSM
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Page 432 and 433: -Lactamase Aureobacterium sp. 3) Fl
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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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