Industrial Biotransformations

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Carboxypeptidase B Pig Pancreas 3) Flow scheme Not published. 4) Process parameters conversion: >99.9 % yield: > 90 % selectivity: > 90 % reactor type: batch reactor volume: 7,500 L capacity: > 0.5 t · a –1 residence time: 4–6 h space-time-yield: 1.7 g · L –1 ·d –1 down stream processing: chromatography enzyme activity: 20 U · g –1 enzyme supplier: enzyme Calbiochem, USA start-up date: 1998 production site: Sanofi Aventis, Germany company: Sanofi Aventis, France 5) Product application ● In 1921 insulin could be isolated from dog pancreas. ● The sequence was identified by Sanger in 1955. ● Insulin regulates the blood sugar level. It is used for the treatment of diabetes mellitus. Up to 5 % of the population of the western world suffers from diabetes. ● A glucose level below 0.25 mM leads to problems in energy supply to the brain. Consequences can include coma, irreversible brain damage and death. ● Since insulin is decomposed by proteases it cannot be administered orally. A new application method is inhalation of modified insulin with faster effects due to exchange of single hydrophobic amino acid with several hydrophilic amino acids. The continuous application after measurement of the blood sugar level is the most comfortable and efficient way. 6) Literature EC 3.4.17.2 ● Frank, B.H., Chance, R.E. (1983) Two routes for producing human insulin utilizing recombinant DNA technology, Münch. Med. Wschr. 125, 14–20 ● Jørgensen, L.N., Rasmussen, E., Thomsen, B. (1989) HM(ge), Novo’s biosynthetic insulin; Med. View. III, No. 4, 1–7 ● Ladisch, M.R., Kohlmann, K.L. (1992) Recombinant human insulin, Biotechnol. Prog. 8, 469– 478 349
Trypsin Pig Pancreas SER GLY GLU LEU ALA LEU PRO GLN LEU SER GLY ALA GLY PRO GLY GLY GLY LEU GLU LEU VAL GLN GLN GLY LYS ARG S S GLY A-chain ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU GLN CYS THR LEU GLU ASN TYR ASN VAL GLN PRO COOH ASP NH2 GLU S ALA PHE VAL S S S GLU ASN ARG GLN ARG HIS THR LEUCYS GLY SER LYS HIS LEU VAL GLU ALA LEU TYR LEU VAL CYS GLY GLU ARG PRO GLY PHETYR THR B-chain H 2N 1) Reaction conditions pH: < 7.0 T: 6 °C medium: aqueous reaction type: carboxylic acid amide hydrolysis catalyst: solubilized enzyme enzyme: tryptase (trypsin) strain: pig pancreas CAS (enzyme): [9002-07–7] E S S GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU GLN CYS THR LEU GLU ASN TYR ASN COOH EC 3.4.21.4 H2N PHE VAL S S S S COOH ASN ARG GLN ARG HIS THR LEU CYS GLY SER HIS LYS LEU VAL GLU ALA LEU TYR LEU VAL CYS GLY GLU ARG PRO GLY PHETYR THR 1 = pro-arg-insulin 2 = mono/di-arg-insulin Fig. 3.4.21.4 – 1 350 1 2 - C-chain C-chain Eli Lilly <strong>Industrial</strong> <strong>Biotransformations</strong>. Andreas Liese, Karsten Seelbach, Christian Wandrey (Eds.) Copyright © 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 3-527-31001-0
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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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Page 316 and 317: Lipase Arthrobacter sp. ● For thi
Page 318 and 319: Lipase Serratia marescens MeO R MeO
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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
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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 358 and 359: Carboxypeptidase B Pig Pancreas 2)
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
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Page 388 and 389: Amidase Comamonas acidovorans 1) Re
Page 390 and 391: Amidase Klebsiella terrigena 2 H N
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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
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Penicillin acylase Escherichia coli
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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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