81 Goddard, J.-P., Reymond, J.-L. 2004, (Enzyme Assays for High-throughput Screening), Curr. Opin. Biotechnol. 15, 314–322. 82 Reymond, J.L., Wahler, D., 2002, (Substrate Arrays as Enzyme Fingerprinting Tools), Chembiochem. 3, 701–708. 83 Wahler, D., Reymond, J.L. 2001, (Highthroughput Screening for Biocatalysts), Curr. Opin. Biotechnol. 12, 535–544. 84 Arnold, F.H., Georgiou, G. 2003, Directed Enzyme Evolution: Screening and Selection Methods, Humana Press, Totowa, New Jersey. 85 Eisenthal, R., Danson, M. 2002, Enzyme Assays: A Practical Approach, Oxford University Press, Oxford. 86 Reetz, M.T. 2003, (An Overview of Highthroughput Screening Systems for Enantioselective Enzymatic Transformations), in Directed Enzyme Evolution: Screening and Selection Methods, eds. Arnold, F.H., Georgiou, G., (vol. 230), Humana Press, Totowa, New Jersey, (pp.) 59–282. 87 Reetz, M.T. 2002, (New Methods for the High-throughput Screening of Enantioselective Catalysts and Biocatalysts), Angew. Chem., Int. Ed. Engl. 41, 1335–1338. 88 Svendsen, A. 2004, Enzyme Functionality: Design, Engineering, and Screening, Marcel Dekker, New York. 89 Arnold, F.H., Georgiou, G. 2003, Directed Evolution Library Creation: Methods and Protocols, Humana Press, Totowa, New Jersey. 90 Hughes, M.D., Nagel, D.A., Santos, A.F., Sutherland, A.J., Hine, A.V. 2003, (Removing the Redundancy from Randomised Gene Libraries), J. Mol. Biol. 331, 973–979. 91 Murakami, H., Hohsaka, T., Sisido, M. 2002, (Random Insertion and Deletion of Arbitrary Number of Bases for Codon-based Random Mutation of DNAs), Nat. Biotechnol. 20, 76–81. 92 Pikkemaat, M.G., Janssen, D.B. 2002, (Generating Segmental Mutations in Haloalkane Dehalogenase: A Novel Part in the Directed Evolution Toolbox), Nucleic Acids Res. 30, e35. 93 Zhao, H., Arnold, F.H. 1997, (Optimization of DNA Shuffling for High Fidelity Recombination), Nucleic Acids Res. 25, 1307–1308. 94 Crameri, A., Raillard, S.A., Bermudez, E., Stemmer, W.P.C. 1998, (DNA Shuffling of a Family of Genes from Diverse Species Accelerates Directed Evolution), Nature 391, 288–291. References 113 95 Shao, Z., Zhao, H., Giver, L., Arnold, F.H. 1998, (Random-priming In Vitro Recombination: an Effective Tool for Directed Evolution), Nucleic Acids Res. 26, 681–683. 96 Volkov, A.A., Shao, Z., Arnold, F.H. 1999, (Recombination and Chimeragenesis by In Vitro Heteroduplex Formation and In Vivo Repair), Nucleic Acids Res. 27, e18. 97 Kikuchi, M., Ohnishi, K., Harayama, S. 1999, (Novel Family Shuffling Methods for the In Vitro Evolution of Enzymes), Gene 236, 159–167. 98 Kikuchi, M., Ohnishi, K., Harayama, S. 2000, (An Effective Family Shuffling Method using Single-stranded DNA), Gene 243, 133–137. 99 Gibbs, M.D., Nevalainen, K.M., Bergquist, P.L. 2001, (Degenerate Oligonucleotide Gene Shuffling (DOGS): A Method for Enhancing the Frequency of Recombination with Family Shuffling), Gene 271, 13–20. 100 Coco, W.M., Levinson, W.E., Crist, M.J., Hektor, H.J., Darzins, A., Pienkos, P.T., Squires, C.H., Monticello, D.J. 2001, (DNA Shuffling Method for Generating Highly Recombined Genes and Evolved Enzymes), Nat. Biotechnol. 19, 354–359. 101 Song, J.K., Chung, B., Oh, Y.H., Rhee, J.S. 2002, (Construction of DNA-shuffled and Incrementally Truncated Libraries by a Mutagenic and Unidirectional Reassembly Method: Changing from a Substrate Specificity of Phospholipase to that of Lipase), Appl. Environ. Microbiol. 68, 6146–6151. 102 Ostermeier, M., Shim, J.H., Benkovic, S.J. 1999, (A Combinatorial Approach to Hybrid Enzymes Independent of DNA Homology), Nat. Biotechnol. 17, 1205–1209. 103 Sieber, V., Martinez, C.A., Arnold, F.H. 2001, (Libraries of Hybrid Proteins from Distantly Related Sequences), Nat. Biotechnol. 19, 456–460. 104 Kawarasaki, Y., Griswold, K.E., Stevenson, J.D., Selzer, T., Benkovic, S.J., Iverson, B.L., Georgiou, G. 2003, (Enhanced Crossover SCRATCHY: Construction and Highthroughput Screening of a Combinatorial Library Containing Multiple Non-homologous Crossovers), Nucleic Acids Res. 31, e126. 105 Reetz, M.T., Zonta, A., Schimossek, K., Liebeton, K., Jaeger, K.E. 1997, (Creation of Enantioselective Biocatalysts for Organic
114 4 Optimization of <strong>Industrial</strong> Enzymes by Molecular Engineering Chemistry by In Vitro Evolution), Angew. Chem., Int. Ed. Engl. 36, 2830–2832. 106 Farinas, E.T. 2003, (Colorimetric Screen for Aliphatic Hydroxylation by Cytochrome P450 using p-Nitrophenyl-substituted Alkanes), in Directed Enzyme Evolution: Screening and Selection Methods, (vol. 230), eds. Arnold, F.H., Georgiou, G., Humana Press, Totowa, New Jersey, (pp.) 149–155. 107 Badalassi, F., Wahler, D., Klein, G., Crotti, P., Reymond, J.L. 2000, (A Versatile Periodate-coupled Fluorogenic Assay for Hydrolytic Enzymes), Angew. Chem., Int. Ed. Engl. 39, 4067–4070. 108 Leroy, E., Bensel, N., Reymond, J.L. 2003, (Fluorogenic Cyanohydrin Esters as Chiral Probes for Esterase and Lipase Activity), Adv. Synth. Catal. 345, 859–865. 109 Sevestre, A., Helaine, V., Guyot, G., Martin, C., Hecquet, L. 2003, (A Fluorogenic Assay for Transketolase from Saccharomyces cerevisiae), Tetrahedron Lett. 44, 827–830. 110 Gonzalez-Garcia, E., Helaine, V., Klein, G., Schuermann, M., Sprenger, G.A., Fessner, W.D., Reymond, J.L. 2003, (Fluorogenic Stereochemical Probes for Transaldolases), Chem. Eur. J. 9, 893–899. 111 Zocher, F., Enzelberger, M.M., Bornscheuer, U.T., Hauer, B., Schmid, R.D. 1999, (A Colorimetric Assay Suitable for Screening Epoxide Hydrolase Activity), Anal. Chim. Acta 391, 345–351. 112 Beisson, F., Ferte, N., Nari, J., Noat, G., Arondel, V., Verger, R. 1999, (Use of Naturally Fluorescent Triacylglycerols from Parinari glaberrimum to Detect Low Lipase Activities from Arabidopsis thaliana Seedlings), J. Lipid Res. 40, 2313–2321. 113 Beisson, F., Tiss, A., Riviere, C., Verger, R. 2000, (Methods for Lipase Detection and Assay: A Critical Review), Eur. J. Lipid Sci. Technol. 102, 133–153. 114 Henke, E., Bornscheuer, U.T. 2003, (Fluorophoric Assay for the High-throughput Determination of Amidase Activity), Anal. Chem. 75, 255–260. 115 Konarzycka-Bessler, M., Bornscheuer, U.T. 2003, (A High-throughput-screening Method for Determining the Synthetic Activity of Hydrolases), Angew. Chem., Int. Ed. Engl. 42, 1418–1420. 116 Banerjee, A., Sharma, R., Banerjee, U.C. 2003, (A Rapid and Sensitive Fluorometric Assay Method for the Determination of Nitrilase Activity), Biotech. Appl. Biochem. 37, 289–293. 117 Li, Z., Bütikofer, L., Witholt, B. 2004, (Highthroughput Measurement of the Enantiomeric Excess of Chiral Alcohols by using Two Enzymes), Angew. Chem., Int. Ed. Engl. 43, 1698–1702. 118 Moris-Varas, F., Shah, A., Aikens, J., Nadkarni, N.P., Rozzell, J.D., Demirjian, D.C. 1999, (Visualization of Enzyme-catalyzed Reactions using pH Indicators: Rapid Screening of Hydrolase Libraries and Estimation of the Enantioselectivity), Bioorg. Med. Chem.7, 2183–2188. 119 Janes, L.E., Löwendahl, A.C., Kazlauskas, R.J. 1998, (Quantitative Screening of Hydrolase Libraries using pH Indicators: Identifying Active and Enantioselective Hydrolases), Chem. Eur. J. 4, 2324–2331. 120 Zhao. H. 2003, (A pH-indicator-based Screen for Hydrolytic Haloalkane Dehalogenase), in Directed Enzyme Evolution: Screening and Selection Methods, (vol. 230), eds. Arnold, F.H., Georgiou, G., Humana Press, Totowa, New Jersey, (pp.) 213–221. 121 Breuer, M., Pohl, M., Hauer, B., Lingen, B. 2002, (High-throughput Assay of (R)phenylacetylcarbinol Synthesized by Pyruvate Decarboxylase), Anal. Bioanal. Chem. 374, 1069–1073. 122 Lingen, B., Kolter-Jung, D., Dünkelmann, P., Feldmann, R., Grotzinger, J., Pohl, M., Müller, M. 2003, (Alteration of the Substrate Specificity of Benzoylformate Decarboxylase from Pseudomonas putida by Directed Evolution), Chembiochem. 4, 721–726. 123 Doderer, K., Lutz-Wahl, S., Hauer, B., Schmid, R.D. 2003, (Spectrophotometric Assay for Epoxide Hydrolase Activity Toward any Epoxide), Anal. Biochem. 321, 131–134. 124 Marchesi, J.R. 2003, (A Microplate Fluorimetric Assay for Measuring Dehalogenase Activity), J. Microbiol. Meth. 55, 325–329. 125 Wahler, D., Reymond, J.L. 2001, (Novel Methods for Biocatalyst Screening), Curr. Opin. Chem. Biol. 5, 152–158. 126 Eggert, T., Funke, S.A., Rao, O.M., Acharya, P., Krumm, H., Reetz, M.T., Jaeger, K.-E. 2005 (Multiplex-PCR-based recombination as a novel high fidelity method for directed evolution), Chembiochem 6, 1–6.
- 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:
4 1 History of Industrial Biotransf
- Page 20 and 21:
6 1 History of Industrial Biotransf
- Page 22 and 23:
8 1 History of Industrial Biotransf
- Page 24 and 25:
10 1 History of Industrial Biotrans
- Page 26 and 27:
12 1 History of Industrial Biotrans
- Page 28 and 29:
14 1 History of Industrial Biotrans
- Page 30 and 31:
R' 16 O H N 1 History of Industrial
- Page 32 and 33:
18 1 History of Industrial Biotrans
- Page 34 and 35:
20 1 History of Industrial Biotrans
- Page 36 and 37:
22 1 History of Industrial Biotrans
- Page 38 and 39:
24 1 History of Industrial Biotrans
- Page 40 and 41:
26 1 History of Industrial Biotrans
- Page 42 and 43:
28 1 History of Industrial Biotrans
- Page 44 and 45:
30 1 History of Industrial Biotrans
- Page 46 and 47:
32 1 History of Industrial Biotrans
- Page 48 and 49:
34 1 History of Industrial Biotrans
- Page 50 and 51:
36 1 History of Industrial Biotrans
- 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:
44 2 The Enzyme Classification EC 1
- Page 60 and 61:
46 2 The Enzyme Classification EC 1
- Page 62 and 63:
48 2 The Enzyme Classification EC 2
- Page 64 and 65:
50 2 The Enzyme Classification EC 3
- Page 66 and 67:
52 2 The Enzyme Classification EC 3
- 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:
58 2 The Enzyme Classification EC 5
- 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: 68 3 Retrosynthetic Biocatalysis 3.
- Page 84 and 85: 70 3 Retrosynthetic Biocatalysis 3.
- Page 86 and 87: 72 3 Retrosynthetic Biocatalysis 3.
- Page 88 and 89: 74 3 Retrosynthetic Biocatalysis 3.
- Page 90 and 91: 76 3 Retrosynthetic Biocatalysis R
- Page 92 and 93: 78 3 Retrosynthetic Biocatalysis Wh
- Page 94 and 95: 80 3 Retrosynthetic Biocatalysis 3.
- Page 96 and 97: 82 3 Retrosynthetic Biocatalysis 3.
- Page 98 and 99: 84 3 Retrosynthetic Biocatalysis 3.
- Page 100 and 101: 86 3 Retrosynthetic Biocatalysis 3.
- 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 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 180 and 181:
Alcohol dehydrogenase Lactobacillus
- Page 182 and 183:
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 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 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:
Carboxypeptidase B Pig Pancreas 2)
- Page 360 and 361:
Carboxypeptidase B Pig Pancreas 3)
- Page 362 and 363:
Trypsin Pig Pancreas 2) Remarks ●
- Page 364 and 365:
Trypsin Pig Pancreas 2) Remarks ●
- Page 366 and 367:
Trypsin Pig Pancreas 2) Remarks ●
- Page 368 and 369:
Subtilisin Bacillus licheniformis 1
- Page 370 and 371:
Subtilisin Bacillus licheniformis 4
- Page 372 and 373:
Subtilisin Bacillus licheniformis
- Page 374 and 375:
Subtilisin Bacillus licheniformis 6
- 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:
Penicillin amidase Escherichia coli
- Page 402 and 403:
Penicillin amidase Bacillus megater
- Page 404 and 405:
Penicillin amidase Escherichia coli
- Page 406 and 407:
Penicillin amidase Escherichia coli
- Page 408 and 409:
Penicillin acylase Escherichia coli
- Page 410 and 411:
Penicillin acylase Escherichia coli
- Page 412 and 413:
Penicillin acylase Escherichia coli
- 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:
Nitrile hydratase Rhodococcus rhodo
- Page 496 and 497:
Nitrile hydratase Rhodococcus rhodo
- Page 498 and 499:
Nitrile hydratase Rhodococcus rhodo
- Page 500 and 501:
Carnitine dehydratase Escherichia c
- Page 502 and 503:
Carnitine dehydratase Escherichia c
- Page 504 and 505:
Carnitine dehydratase Escherichia c
- 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:
518 7 Quantitative Analysis of Indu
- Page 530 and 531:
520 7 Quantitative Analysis of Indu
- 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:
528 Index of strain strain enzyme n
- Page 540 and 541:
530 Index of strain strain enzyme n
- 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:
538 Index of starting material star
- Page 550 and 551:
540 Index of starting material star
- Page 552 and 553:
542 Index of starting material star
- Page 554 and 555:
544 Index of starting material star
- Page 556 and 557:
546 Index of product product enzyme
- Page 558 and 559:
548 Index of product product enzyme
- Page 560 and 561:
550 Index of product product enzyme
- Page 562 and 563:
552 Index of product product enzyme
- Page 564 and 565:
554 Index of product product enzyme
- Page 566:
556 Index of product product enzyme