Industrial Biotransformations

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Cyclodextrin glycosyltransferase Bacillus circulans ● The separation is established by selective adsorption of α- and β-cyclodextrins on chitosan beads with appropriate ligands. α-Cyclodextrins are selectively interacted with stearic acid and β-cyclodextrins with cyclohexanepropanamide-n-caproic acid. The adsorption selectivity is almost 100 %. In the case of the β-cyclodextrins a capacity of 240 g · L –1 gel bed is reached. ● The process data given here are related to the production of α-cyclodextrins. ● Before entering the adsorption column the temperature is lowered to 30 °C for effective adsorption. At this temperature almost no cyclodextrins are formed during circulation. Before re-entering the main reactor the temperature of the solution is again adjusted to 55 °C by using the energy of the reaction solution leaving the reactor. ● To prevent adsorption of the cyclodextrin glycosyltransferase in the α-cyclodextrin adsorbent 3 % w/v NaCl is added. CDs adsorbed on the resin through ionic bonds are easely removed by 4 % NaCl (Okabe et al., p. 115). 3) Flow scheme Fig. 2.4.1.19 – 2 4) Process parameters yield: 22.3 % (α-cyclodextrin); 10.8 % (β-cyclodextrin); 5.1 % (γ-cyclodextrin) chemical purity: 94.9 % reactor type: batch down stream processing: chromatography and crystallization enzyme supplier: Amano, Japan company: Mercian Co., Ltd., Japan 5) Product application EC 2.4.1.19 ● Cyclodextrins serve as molecular hosts and are used in the food industry for capturing and retaining flavors. They are also used in the formulation of pharmaceuticals. 265
Cyclodextrin glycosyltransferase Bacillus circulans 6) Literature EC 2.4.1.19 ● Okabe, M., Tsuchiyama, Y., Okamoto, R. (1993) Development of a cyclodextrin production process using specific adsorbents, in: <strong>Industrial</strong> Application of Immobilized Biocatalysts (Tanaka, A., Tosa, T., Kobayashi, T., eds.) pp. 109–129, Marcel Dekker Inc., New York ● Tsuchiyama, Y., Yamamoto, K.-I., Asou, T., Okabe, M., Yagi, Y., Okamoto, R. (1991) A novel process of cyclodextrin production by use of specific adsorbents. Part I. Screening of specific adsorbents, J. Ferment. Bioeng. 71, 407–412 ● Yang, C.-P., Su, C.-S. (1989) Study of cyclodextrin production using cyclodextrin glycosyltransferase immobilized on chitosan, J. Chem. Technol. Biotechnol. 46, 283–294 266
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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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Page 228 and 229: Catalase Microbial source 1) Reacti
Page 230 and 231: Oxygenase Arthrobacter sp. 1) React
Page 232 and 233: Naphthalene dioxygenase Pseudomonas
Page 234 and 235: Naphthalene dioxygenase Pseudomonas
Page 236 and 237: Benzoate dioxygenase Pseudomonas pu
Page 238 and 239: Cyclohexanone monooxygenase Acineto
Page 240 and 241: Cyclohexanone monooxygenase Acineto
Page 242 and 243: Oxygenase Escherichia coli OH OH 1
Page 244 and 245: Monooxygenases / Aryl alcohol dehyd
Page 246 and 247: Styrene monooxygenase Escherichia c
Page 248 and 249: Styrene monooxygenase Escherichia c
Page 250 and 251: Monooxygenase Pseudomonas putida H
Page 252 and 253: Monooxygenase Streptomyces sp. SC 1
Page 254 and 255: Oxygenase Nocardia autotropica 1) R
Page 256 and 257: Monooxygenase Nocardia corallina 1
Page 258 and 259: Monooxygenase Nocardia corallina
Page 260 and 261: Monooxygenase Nocardia corallina O
Page 262 and 263: Oxidase Pseudomonas oleovorans 1) R
Page 264 and 265: Reductase Baker’s yeast 1 = oxois
Page 266 and 267: Oxidase Rhodococcus erythropolis 2
Page 268 and 269: Desaturase Rhodococcus sp. 1) React
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 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
Page 318 and 319: Lipase Serratia marescens MeO R MeO
Page 320 and 321: Lipase Serratia marescens Fig. 3.1.
Page 322 and 323: Lipase Pseudomonas cepacia 1) React
Page 324 and 325: 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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