Industrial Biotransformations

More documents

Recommendations

Info

Catalase Microbial source 1) Reaction conditions pH: 6.0–9.0 medium: 3-phase-system: organic, solid, aqueous reaction type: redox reaction catalyst: solubilized enzyme: hydrogen-peroxide: hydrogen peroxide oxidoreductase (catalase) strain: microbial source CAS (enzyme): [9001-05–2] 2) Remarks O2 + 2 1 Me NO 2 EC 1.11.1.6 ● During oxidative coupling to dinitrodibenzyl (DNDB) hydrogen peroxide is produced as a byproduct. It is not possible to decompose H 2O 2 by the addition of heavy-metal catalysts because only incomplete conversion is reached. Additionally, subsequent process steps with DNDB are problematic due to contamination with heavy-metal catalyst. ● The reaction solution consists of three phases: 1) water, 2) organic phase and 3) solid phase consisting of DNDB. ● The catalase derived from microbial source has advantages compared to beef catalase since the activity remains constant over a broad pH range from 6.0 to 9.0; temperatures up to 50 °C are tolerated and salt concentrations up to 25 % do not affect the enzyme stability. ● The reaction is carried out in a cascade of CSTRs. After the chemical reaction in the first vessel, the pH is adjusted with acetic acid. Decomposition of H 2O 2 is induced by catalase solution added to the second reactor at a constant rate. Oxygen is removed by dilution with nitrogen in the third reactor. O 2N NO2 2 H2O2 H2O + 1/2 O2 1 = nitrotoluene 2 = dinitrodibenzyl (DNDB) Novartis Fig. 1.11.1.6 – 1 (t-BuOK) + E 217
Catalase Microbial source 3) Flow scheme Fig. 1.11.1.6 – 2 4) Process parameters conversion: > 98 % yield: > 98 % selectivity: 99.9 % reactor type: cascade of CSTR‘s residence time: > 1 h down stream processing: degassing with nitrogen company: Novartis, Switzerland 5) Product application ● The process is only relevant to remove the undesired side product H 2O 2. The dinitrodibenzyl is used as a pharmaceutical intermediate. 6) Literature EC 1.11.1.6 ● Onken, U., Schmidt, E., Weissenrieder, T. (1996) Enzymatic H 2O 2 decomposition in a threephase suspension, Ciba-Geigy; International conference on biotechnology for industrial production of fine chemicals, 93rd event of the EFB; Zermatt, Switzerland, 29.09.1996 218
Page 2 and 3:
Industrial Biotransformations Edite
Page 4 and 5:
Industrial Biotransformations Secon
Page 6 and 7:
Contents Preface to the first editi
Page 8 and 9:
5 Basics of Bioreaction Engineering
Page 10 and 11:
X Preface to the first edition many
Page 12 and 13:
XII Preface to the second edition E
Page 14 and 15:
XIV List of Contributors Prof. Dr.
Page 16 and 17:
2 1 History of Industrial Biotransf
Page 18 and 19:
Page 20 and 21:
Page 22 and 23:
Page 24 and 25:
10 1 History of Industrial Biotrans
Page 26 and 27:
Page 28 and 29:
Page 30 and 31:
R' 16 O H N 1 History of Industrial
Page 32 and 33:
Page 34 and 35:
Page 36 and 37:
Page 38 and 39:
Page 40 and 41:
Page 42 and 43:
Page 44 and 45:
Page 46 and 47:
Page 48 and 49:
Page 50 and 51:
Page 52 and 53:
38 2 The Enzyme Classification Tab.
Page 54 and 55:
40 2 The Enzyme Classification trib
Page 56 and 57:
42 2 The Enzyme Classification EC 1
Page 58 and 59:
Page 60 and 61:
Page 62 and 63:
Page 64 and 65:
Page 66 and 67:
Page 68 and 69:
54 2 The Enzyme Classification 2.2.
Page 70 and 71:
56 2 The Enzyme Classification The
Page 72 and 73:
Page 74 and 75:
60 2 The Enzyme Classification in g
Page 76 and 77:
62 2 The Enzyme Classification Refe
Page 78 and 79:
64 3 Retrosynthetic Biocatalysis 3.
Page 80 and 81:
66 3 Retrosynthetic Biocatalysis R
Page 82 and 83:
Page 84 and 85:
Page 86 and 87:
Page 88 and 89:
Page 90 and 91:
76 3 Retrosynthetic Biocatalysis R
Page 92 and 93:
78 3 Retrosynthetic Biocatalysis Wh
Page 94 and 95:
Page 96 and 97:
Page 98 and 99:
Page 100 and 101:
Page 102 and 103:
88 3 Retrosynthetic Biocatalysis Re
Page 104 and 105:
90 3 Retrosynthetic Biocatalysis (D
Page 106 and 107:
4 Optimization of Industrial Enzyme
Page 108 and 109:
4.2 Learning from Nature Nature its
Page 110 and 111:
4.3 Enzyme Production Using Bacteri
Page 112 and 113:
4.4 Improvements to Enzymes by Mole
Page 114 and 115:
1 4.4 Improvements to Enzymes by Mo
Page 116 and 117:
4.4 Improvements to Enzymes by Mole
Page 118 and 119:
4.5 Identification of Improved Enzy
Page 120 and 121:
4.5 Identification of Improved Enzy
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 170 and 171:
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
Page 220 and 221: d-Aminoacid oxidase Trijonopsis var
Page 222 and 223: d-Amino acid oxidase Trigonopsis va
Page 224 and 225: Nicotinic acid hydroxylase Achromob
Page 226 and 227: Nicotinic acid hydroxylase Achromob
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 276 and 277: Cyclodextrin glycosyltransferase Ba
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
Page 326 and 327:
Lipase Candida antarctica 4) Proces
Page 328 and 329:
-Galactosidase Saccharomyces lactis
Page 330 and 331:
Lipase Pseudomonas cepacia ● The
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:
Page 360 and 361:
Page 362 and 363:
Trypsin Pig Pancreas 2) Remarks ●
Page 364 and 365:
Page 366 and 367:
Page 368 and 369:
Subtilisin Bacillus licheniformis 1
Page 370 and 371:
Page 372 and 373:
Subtilisin Bacillus licheniformis
Page 374 and 375:
Page 376 and 377:
Subtilisin Bacillus licheniformis
Page 378 and 379:
Subtilisin Bacillus sp. EtOOC (R/S)
Page 380 and 381:
Subtilisin Bacillus sp. drug discov
Page 382 and 383:
Subtilisin Bacillus lentus 1 = (R,S
Page 384 and 385:
Thermolysin Bacillus thermoproteoly
Page 386 and 387:
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
Page 394 and 395:
Amidase Klebsiella oxytoca company:
Page 396 and 397:
Urease Lactobacillus fermentum ●
Page 398 and 399:
Penicillin amidase Escherichia coli
Page 400 and 401:
Page 402 and 403:
Penicillin amidase Bacillus megater
Page 404 and 405:
Page 406 and 407:
Page 408 and 409:
Penicillin acylase Escherichia coli
Page 410 and 411:
Page 412 and 413:
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
Page 430 and 431:
l-Hydantoinase Arthrobacter sp. DSM
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
Page 452 and 453:
Haloalkane dehalogenase Alcaligenes
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
Page 464 and 465:
Aspartate b-decarboxylase Pseudomon
Page 466 and 467:
Oxynitrilase Hevea brasiliensis 1 =
Page 468 and 469:
N-Acetyl-d-neuraminic acid aldolase
Page 470 and 471:
N-Acetyl-d-neuraminic acid aldolase
Page 472 and 473:
Tyrosine phenol lyase Erwinia herbi
Page 474 and 475:
Fumarase Corynebacterium glutamicum
Page 476 and 477:
Fumarase Corynebacterium glutamicum
Page 478 and 479:
Fumarase Brevibacterium flavum 4) P
Page 480 and 481:
Enoyl-CoA hydratase Candida rugosa
Page 482 and 483:
Enoyl-CoA hydratase Candida rugosa
Page 484 and 485:
Tryptophan synthase Escherichia col
Page 486 and 487:
Malease Pseudomonas pseudoalcaligen
Page 488 and 489:
Malease Pseudomonas pseudoalcaligen
Page 490 and 491:
Nitrile hydratase Pseudomonas chlor
Page 492 and 493:
Nitrile hydratase Rhodococcus rhodo
Page 494 and 495:
Page 496 and 497:
Page 498 and 499:
Page 500 and 501:
Carnitine dehydratase Escherichia c
Page 502 and 503:
Page 504 and 505:
Page 506 and 507:
Aspartase Escherichia coli 3) Flow
Page 508 and 509:
Aspartase Escherichia coli 5) Produ
Page 510 and 511:
Aspartase Brevibacterium flavum 3)
Page 512 and 513:
l-Aspartase Escherichia coli 3) Flo
Page 514 and 515:
l-Phenylalanine ammonia-lyase Rhodo
Page 516 and 517:
Amino acid racemase Amycolatopsis o
Page 518 and 519:
GlcNAc 2-epimerase Escherichia coli
Page 520 and 521:
Xylose isomerase Bacillus coagulans
Page 522 and 523:
Xylose isomerase Bacillus coagulans
Page 524 and 525:
a-Glucosyl transferase Protaminobac
Page 526 and 527:
516 7 Quantitative Analysis of Indu
Page 528 and 529:
Page 530 and 531:
Page 532 and 533:
522 Index of enzyme name enzyme nam
Page 534 and 535:
524 Index of enzyme name enzyme nam
Page 536 and 537:
526 Index of strain strain enzyme n
Page 538 and 539:
Page 540 and 541:
Page 542 and 543:
532 Index of company company strain
Page 544 and 545:
534 Index of company company strain
Page 546 and 547:
536 Index of starting material star
Page 548 and 549:
Page 550 and 551:
Page 552 and 553:
Page 554 and 555:
Page 556 and 557:
546 Index of product product enzyme
Page 558 and 559:
Page 560 and 561:
Page 562 and 563:
Page 564 and 565:
Page 566:
show all

Industrial Biotransformations

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?