Industrial Biotransformations

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Alcohol dehydrogenase Rhodococcus erythropolis 5) Product application ● The trivial name for (S)-6-methyl-5-hepten-2-ol is (S)-(+)-sulcatol, a pheromone from the scolytid beetle Gnathotrichus sulcatus / Gnathotrichus retusus. ● (S)-1-Phenyl-2-propanol is used as an intermediate for the synthesis of amphetamines (sympathomimetics): NH 2 EC 1.1.1.1 ● (S)-4-Phenyl-2-butanol is used as a precursor for anti-hypertensive agents and spasmolytics or anti-epileptics: OH (S)-1-phenyl-2-propanol H3N + PO4 - HN CN amphetamine amphetamine phosphate amphetaminil Fig. 1.1.1.1 – 5 Fig. 1.1.1.1 – 6 HN OH labetalol antihypertensive agent OH CONH2 OH (S)-4-phenyl-2-butanol N + Br - emepronium bromide spasmolytic, antiepileptic HN OH bufeniode antihypertensive agent I OH I 159
Alcohol dehydrogenase Rhodococcus erythropolis 6) Literature EC 1.1.1.1 ● Bracher, F., Litz, T. (1994) Building blocks for the preparation of enantiomerically pure drugs containing a phenylalkylamine moiety, Arch. Pharm. 327, 591–593 ● Johnston, B., Slessor, K. (1979) Facile synthesis of the enantiomers of sulcatol, Can. J. Chem. 57, 233–235 ● Kragl, U., Kruse, W., Hummel, W., Wandrey, C. (1996) Enzyme engineering aspects of biocatalysis: Cofactor regeneration as example, Biotechnol. Bioeng. 52, 309–319 ● Kruse, W., Hummel, W., Kragl, U. (1996) Alcohol-dehydrogenase-catalyzed production of chiral hydrophobic alcohols. A new approach leading to a nearly waste-free process, Recl. Trav. Chim. Pays-Bas 115, 239–243 ● Kruse, W., Kragl, U., Wandrey, C. (1996) Verfahren zur kontinuierlichen enzymkatalysierten Gewinnung hydrophober Produkte, Forschungszentrum Jülich GmbH, DE 4436149 A1 ● Kruse, W., Kragl, U., Wandrey, C. (1998) Process for the continuous enzymatic extraction of hydrophobic products and device suitable therefor, Forschungszentrum Jülich GmbH, Germany, US 5,795,750 ● Liang, S.; Paquette, L.A. (1990) Biocatalytic-based synthesis of optically pure (C-6)-functionalized 1-(tert-butyldimethyl-silyloxy)-2-methyl-(E)-2-heptenes; Tetrahedron Asym. 1, 445– 452 ● Mori, K. (1975) Synthesis of optically active forms of sulcatol – The aggregation pheromone in the scolytid beetle, Gnathotrichus sulcatus, Tetrahedron 31, 3011–3012 160
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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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Page 122 and 123: Galleron, N., Ghim, S.Y., Glaser, P
Page 124 and 125: ment, Relaxation, and Reversal of t
Page 126 and 127: 81 Goddard, J.-P., Reymond, J.-L. 2
Page 128 and 129: 5 Basics of Bioreaction Engineering
Page 130 and 131: where r p = selectivity to componen
Page 132 and 133: 5.1 Definitions operoxidase (CPO) h
Page 134 and 135: 5.1 Definitions The residence time
Page 136 and 137: 5.1 Definitions In iso-electric pre
Page 138 and 139: 5.2 Biocatalyst Kinetics formation
Page 140 and 141: 5.2 Biocatalyst Kinetics K M values
Page 142 and 143: v ˆ V max ‰SŠ KM 1‡ ‰PŠ KI
Page 144 and 145: 5.3 Basic Reactor Types and their M
Page 146 and 147: dx concentration [S] 0 [S] 1 [S] e
Page 148 and 149: 5.4 Biocatalyst Recycling and Recov
Page 150 and 151: . better stability, especially towa
Page 152 and 153: 5.4.2 Cross-linking 5.4 Biocatalyst
Page 154 and 155: . immobilization methods . substrat
Page 156 and 157: References Owing to the need for st
Page 158 and 159: 40 Vuorilehto, K., Lütz, S., Wandr
Page 160 and 161: Common name of enzyme Name of strai
Page 162 and 163: Common name of enzyme Name of strai
Page 164 and 165: Alcohol dehydrogenase Neurospora cr
Page 166 and 167: Alcohol dehydrogenase Neurospora cr
Page 168 and 169: Alcohol dehydrogenase Rhodococcus e
Page 172 and 173: Alcohol dehydrogenase Acinetobacter
Page 174 and 175: Alcohol dehydrogenase Acinetobacter
Page 176 and 177: Dehydrogenase Zygosaccharomyces rou
Page 178 and 179: Alcohol dehydrogenase Lactobacillus
Page 184 and 185: Carbonyl reductase Escherichia coli
Page 186 and 187: Aldehyde reductase Escherichia coli
Page 188 and 189: Lactate dehydrogenase Staphylococcu
Page 190 and 191: d-Lactate dehydrogenase Leuconostoc
Page 192 and 193: d-Lactate dehydrogenase Leuconostoc
Page 194 and 195: d-Sorbitol dehydrogenase Gluconobac
Page 196 and 197: d-Sorbitol dehydrogenase Gluconobac
Page 198 and 199: Dehydrogenase Geotrichum candidum 1
Page 200 and 201: Ketoreductase 1 = ethyl-4-chloro-3-
Page 202 and 203: Dehydrogenase Candida sorbophila N
Page 204 and 205: 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
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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
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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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