Industrial Biotransformations

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Aminoacylase Aspergillus niger 2 N S 1) Reaction conditions pH: 7.0 medium: aqueous reaction type: carboxylic acid amide hydrolysis catalyst: immobilized enzyme enzyme: N-acetyl-l-amino-acid amidohydrolase (aminoacylase) strain: Aspergillus niger CAS (enzyme): [9012–37–7] 2) Remarks CO 2H NHAc D,L-1 L-2 N S EC 3.5.1.14 1 = N-acetyl-D,L-3-(4-thiazolyl)alanine 2 = 3-(4-thiazolyl)alanine 3 = N-acetyl-D-3-(4-thiazolyl)alanine Celltech Group plc Fig. 3.5.1.14 – 1 CO 2H ● The whole process consisting of the following reaction steps is performed in one vessel: Fig. 3.5.1.14 – 2 E + H2O NH2 + O + OH N S D-1 CO 2H NHAc 403
Aminoacylase Aspergillus niger ● The hydrolysis is performed by slow addition of hydroxide solution, maintaining the mixture at pH 9–10; at this pH the initial product undergoes decarboxylation; this causes a reduction in pH and, by careful control of the base addition, the resulting mixture can be kept approximately neutral. ● The neutral solution can be directly used for the biotransformation. ● The product is extracted directly from the aqueous reaction mixture with methyl-tert-butyl ether (MTBE) and is of high enantiomeric purity. ● The d-isomer can be recycled via an oxazolinone that tautomerizes to the enol: N 1 = N-acetyl-3-(4-thiazolyl)alanine 2 = oxazolinone (azlactone) 3 = enol Fig. 3.5.1.14 – 3 ● Since the enzyme is immobilized and employed in a packed bed reactor it can be used several times resulting in a protein-free solution after down-stream processing. ● The process can be applied to other unnatural alanine derivatives, e.g.: Fig. 3.5.1.14 – 4 404 S D-1 CO 2H NHAc 1 = 2-naphthylalanine 2 = 4-cyanophenylalanine 3 = 2-pyridylalanine 4 = allylglycine Ac 2O, OH - N N S S 2 N N 3 O OH O O Me Me L-1 L-2 N NH2 L-3 NH2 CO2H CO2H NC NH 2 L-4 NH2 N CO2H S D,L-1 CO2H EC 3.5.1.14 CO 2H NHAc
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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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Page 384 and 385: Thermolysin Bacillus thermoproteoly
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Page 388 and 389: Amidase Comamonas acidovorans 1) Re
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Page 396 and 397: Urease Lactobacillus fermentum ●
Page 398 and 399: Penicillin amidase Escherichia coli
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Page 408 and 409: Penicillin acylase Escherichia coli
Page 416 and 417: Aminoacylase Aspergillus niger 3) F
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-
Page 440 and 441: Nitrilase Escherichia coli 1) React
Page 442 and 443: Nitrilase / Hydroxylase Agrobacteri
Page 444 and 445: Nitrilase / Hydroxylase Alcaligenes
Page 446 and 447: Dehalogenase Pseudomonas putida 1)
Page 448 and 449: Dehalogenase Pseudomonas putida 5)
Page 450 and 451: Haloalkane dehalogenase Alcaligenes
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Page 454 and 455: Haloalkane dehalogenase Enterobacte
Page 456 and 457: Halohydrin dehalogenase 1 = ethyl-(
Page 458 and 459: Pyruvate decarboxylase Saccharomyce
Page 460 and 461: Acetolactate decarboxylase Bacillus
Page 462 and 463: 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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