88 3 Retrosynthetic Biocatalysis References 1 Faber, K. 2004, <strong>Biotransformations</strong> in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 205–212. 2 Ohta, H., Sugai, T. 2000, (Enzyme-mediated Decarboxylation Reactions in Organic Synthesis), Stereoselective Biocatalysis, ed. Patel, P.N., Marcel Dekker, New York, (pp.) 467–526. 3 Ohta, H., Sugai, T. 1998, (Enzymes in Organic Syntheses: A Novel Elimination Reaction in Andrographolide Triacetate), Nat. Prod. Lett. 12 (1), 1–4. 4 a) Faber, K. 2004, Biotransfromations in Organic Chemistry, Springer-Verlag, Berlin, pp. 52–63; b) Bornscheuer, U.T., Kazlauskas, R.J. 1999, (Survey of Enantioselective Protease- and Amidase-Catalyzed Reactions), in Hydrolases in Organic Synthesis, Wiley-VCH, Weinheim, (pp.) 179–193. 5 Rozzell, J.D., Bommarius, A.S. 2002, (Transamination), in Enzyme Catalysis on Organic Synthesis, eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 875–893. 6 Nakamura, K., Matsuda, T. 2002, (Reduction Reactions), in Enzyme Catalysis on Organic Synthesis, eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 1035–1036. 7 a) Choi, Y.K., Kim, M.J., Ahn, Y., Kim, M.J. 2001, (Lipase/Palladium-Catalyzed Asymmetric Transformations of Ketoximes to Optically Active Amines), Org. Lett. 3, 4099; b) Pàmies, O., Éll, A.H., Samec, J.S.M., Hermanns, N., Bäckvall, J.E. 2002, (An Efficient and Mild Ruthenium-catalyzed Racemization of Amines: Application to the Synthesis of Enantiomerically Pure Amines), Tetrahedron Lett. 43, 4699–4702. 8 Faber, K. 2004, <strong>Biotransformations</strong> in Organic Chemistry, Springer-Verlag, Berlin, (pp.) 63–134. 9 Bornscheuer, U.T., Kazlauskas, R.J. 1999, (Choosing Reaction Media: Water and Organic Solvents), in Hydrolases in Organic Synthesis, Wiley-VCH, Weinheim, (pp.) 39–63. 10 a) Nakamura, K., Matsuda, T. 2002, (Reduction Reactions), in Enzyme Catalysis on Organic Synthesis, (vol. 3), eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 991–1034; b) Klibanov, A.M. 2003, (Asymmetric Enzymic Oxidoreductions in Organic Solvents), Curr. Opin. Biotechnol. 14 (4), 427–431. 11 Flitsch, S., Grogan, G., Ashcroft, D. 2002, (Oxidation Reactions), in Enzyme Catalysis on Organic Synthesis, eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 1065–1099. 12 a) Allen, J.V., Williams, J.M.J. 1996, (Dynamic Kinetic Resolution with Enzyme and Palladium Combinations), Tetrahedron Lett. 37 (11), 1859–1862; b) Lee, D., Huh, E.A., Kim, M.-J., Jung, H.M., Koh, J.H. Park, J. 2000, (Dynamic Kinetic Resolution of Allylic Acohols Mediated by Rutheniumand Lipase-based Catalysts), Org. Lett.2, 2377–2379. 13 Pàmies, O., Bäckvall, J.-E. 2003, Chem. Rev. 103, 3247. 14 Kroutil, W., Mang, H., Edegger, K., Faber, K. 2004, (Biocatalytic Oxidation of Primary and Secondary Alcohols), Org. Bioorg. Chem. (346), 125–142 15 He, A., Li, T., Daniels, L., Fotheringham, I., Rosazza, J.P.N. 2004, (Nocardia sp. Carboxylic Acid Reductase: Cloning, Expression, and Characterization of a New Aldehyde Oxidoreductase Family), Appl. Environ. Microbiol. (70), 1874–1881. 16 Schmid, A., Hollmann, F., Bühler, B. 2002, (Oxidation of Aldehydes), in Enzyme Catalysis on Organic Synthesis, eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 1194–1201. 17 Hoh, C., Villela, M.F. 2000, (Enzyme Classification), in <strong>Industrial</strong> <strong>Biotransformations</strong>, eds. Liese, A., Seelbach, K., Wandrey, C., Wiley-VCH, Weinheim, (pp.) 48–49. 18 Mino, T., Matsuda, T., Hiramatsu, D., Yamashita, M. 2000, (Deprotection of Ketone Dimethylhydrazones Using Lipases), Tetrahedron Lett. 41, 1461–1463. 19 Flitsch, S., Grogan, G., Ashcroft, D. 2002, (Oxidation Reactions), in Enzyme Catalysis on Organic Synthesis, eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 1084–1099. 20 Faber, K., Orru, R.V.A. 2002, (Hydrolysis of Epoxides), in Enzyme Catalysis on Organic Synthesis, (vol. 2), eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 579–604.
21 Kim, M.-J., Choi, Y.K., Choi, M.Y., Kim, M.J., Park, J. 2001, (Lipase/Ruthenium-Catalyzed Dynamic Kinetic Resolution of Hydroxy Acids, Diols, and Hydroxy Aldehydes Protected with a Bulky Group), J. Org. Chem. 66, 4736–4738. 22 Faber, K. 2004, <strong>Biotransformations</strong> in Organic Chemistry, (vol. 5), Springer-Verlag, Berlin, (pp.) 63–122. 23 Hoh, C., Villela, M.F. 2000, (Enzyme Classification), in <strong>Industrial</strong> <strong>Biotransformations</strong>, eds. Liese, A., Seelbach, K., Wandrey, C., Wiley-VCH, Weinheim, (p.) 46. 24 Fülling, G., Sih, C.J. 1987, (Enzymatic Second-Order Asymmetric Hydrolysis of Ketorolac Esters: In Situ Racemization), J. Am. Chem. Soc. 109, 2845–2845. 25 a) Chang, C.-S., Tsai, S.-W., Kuo, J. 1999, Biotechnol. Bioeng. 64 (1), 121; b) Drueckhammer, D.G., Um, P.-J. 1998, (Dynamic Enzymatic Resolution of Thioesters), J. Am. Chem. Soc. 120, 5605–5610. 26 Williams, J.M.J., Dinh, P.M., Harris, W. 1999, (Selective Racemisation of Esters: Relevance to Enzymatic Hydrolysis Reactions), Tetrahedron Lett. 40, 749–752. 27 Pesti, J.A., Yin, J., Zhang, L.-h., Anzalone, L. 2001, (Reversible Michael Reaction-Enzymatic Hydrolysis: A New Variant of Dynamic Resolution), J. Am. Chem. Soc. 123, 11075–11076. 28 van den Heuvel, M., Cuiper, A.D., van der Deen, H., Kellogg, R.M., Feringa, B.L. 1997, Optically Active 6-Acetyloxy-2H-pyran-3(6H)-one Obtained by Lipase Catalyzed Transesterification and Esterification), Tetrahedron Lett. 38, 1655–1658. 29 Kato, D., Mitsuda, S., Ohta, H. 2002, (Microbial Deracemization of {alpha}-Substituted Carboxylic Acids), Org. Lett. 4, 371–373. 30 Um, P.-J., Drueckhammer, D.G. 1998, (Dynamic Enzymatic Resolution of Thioesters), J. Am. Chem. Soc. 120, 5605–5610. 31 Chai, W., Sakamaki, H., Kitanaka, S., Saito, M., Horiuchi, C.A. 2003, (Biotransformation of Cycloalkanediones by Caragana chamlagu), Bull. Chem. Soc. Jpn. 76 (1), 177–182. 32 Flitsch, S., Grogan, G., Ashcroft, D. 2002, (Oxidation Reactions), in Enzyme Catalysis on Organic Synthesis, (vol. 3), eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 1256–1260. References 89 33 Turner, N.J. 2004, (Enzyme Catalysed Deracemisation and Dynamic Kinetic Resolution Reactions), Curr. Opin. Chem. Biol. 8, 114–119. 34 Schulze, B. 2002, (Hydrolysis and Formation of C–N Bonds), in Enzyme Catalysis on Organic Synthesis, (vol. 2), eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 878–892. 35 a) Yamada, H., Shimizu, S., Yoneda, K. 1980, (Synthesis of d-Amino Acids Using Hydantoinase of Microorganism, Production of p-d-Hydroxyphenylglycine), Hakko to Kogyo 38 (10), 937–46; b) Pietzsch, M. Syldatk, C., 2002, (Hydrolysis and Formation of Hydantoins), in Enzyme Catalysis on Organic Synthesis, (vol. 2), eds. Drauz, K., Waldmann, H., Wiley-VCH, Weinheim, (pp.) 761–796; c) Martinkova, L., Kren, V., 2002, (Nitrile- and Amide-converting Microbial Enzymes: Stereo-, Regio- and Chemoselectivity), Biocatal. Biotransform. 20 (2), 73–93. 36 Chen, S.T., Huang, W.H., Wang, K.T.J. 1994, (Resolution of Amino Acids in a Mixture of 2-Methyl-2-propanol/Water (19:1) Catalyzed by Alcalase via In Situ Racemization of One Antipode Mediated by Pyridoxal 5-Phosphate), Org. Chem. 59, 7580–7581. 37 Crich, J.Z., Brieva, R., Marquart, P., Gu, R.L., Flemming, S., Sih, C.J. 1993, (Enzymic Asymmetric Synthesis of Alphaamino Acids. Enantioselective Cleavage of 4-Substituted Oxazolin-5-ones and Thiazolin-5-ones), J. Org. Chem. 58, 3252–3258. 38 a) Drauz, K., Kottenhahn, M., Makryaleas, K., Klenk, H., Bernd, M. 1991, (Chemoenzymatic Syntheses of {omega}-Ureido d-Amino Acids), Angew. Chem., Int. Ed. Engl. 30, 712–714; b) Sano, K., Mitsugi, K. 1978, (Enzymatic Production of l-Cysteine from d,l-2-Amino-D 2 -thiazoline-4-carboxylic Acid by Pseudomonas thiazolinophilum: Optimal Conditions for the Enzyme Formation and Enzymatic Reaction), Agric. Biol. Chem. 42, 2315–2321. 39 May, O., Verseck, S., Bommarius, S., Drauz, K. 2002, (Development of Dynamic Kinetic Resolution Processes for Biocatalytic Production of Natural and Nonnatural l-Amino Acids), Org. Proc. Res. Dev. 6, 452–457. 40 Carr, R., Alexeeva, M., Enright, A., Eve, T.S.C., Dawson, M.J., Turner, N.J. 2003,
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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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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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Alcohol dehydrogenase Lactobacillus
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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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Carboxypeptidase B Pig Pancreas 2)
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Carboxypeptidase B Pig Pancreas 3)
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Trypsin Pig Pancreas 2) Remarks ●
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Trypsin Pig Pancreas 2) Remarks ●
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Trypsin Pig Pancreas 2) Remarks ●
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Subtilisin Bacillus licheniformis 1
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Subtilisin Bacillus licheniformis 4
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Subtilisin Bacillus licheniformis
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Subtilisin Bacillus licheniformis 6
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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 Escherichia coli
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Penicillin amidase Bacillus megater
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Penicillin amidase Escherichia coli
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Penicillin amidase Escherichia coli
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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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Nitrile hydratase Rhodococcus rhodo
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Nitrile hydratase Rhodococcus rhodo
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Nitrile hydratase Rhodococcus rhodo
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Carnitine dehydratase Escherichia c
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Carnitine dehydratase Escherichia c
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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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518 7 Quantitative Analysis of Indu
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520 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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528 Index of strain strain enzyme n
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530 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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538 Index of starting material star
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540 Index of starting material star
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542 Index of starting material star
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544 Index of starting material star
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546 Index of product product enzyme
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548 Index of product product enzyme
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550 Index of product product enzyme
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552 Index of product product enzyme
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554 Index of product product enzyme
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556 Index of product product enzyme