Abstract
During the past 15 years, the development of strategies to apply the catalytic potential of redox coenzyme-requiring enzymes has been a subject of intensive study. The main purpose of which has been to cut the cost of coenzyme to an economically acceptable level. One approach has been the utilization of isolated coenzyme-dependent enzyme systems with simultaneous enzymatic coenzyme regeneration (recycling). This has been used in conjugation with ultrafiltration reactor technology (enzyme membrane reactor), with coenzyme concentration being kept at a catalytic level. The concept implies confinement (immobilization) and practically 100% retention of both enzymes and coenzymes being dissolved in homogeneous solution within the reactor space that is closed off by an ultrafiltration membrane through which low-molecular-weight reactants (substrates and products) can freely pass. Since the problem of retaining nearly 100% native coenzymes of relatively low molecular weight by ultrafiltration membranes has not been satisfactorily solved, active macromolecular coenzyme derivatives are required. In this review, the syntheses, properties and merits of water-soluble macromolecular derivatives of NAD(H), NADP(H) and FAD are considered with respect to their biotechnological application.
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Klibanov AM (1983) Technology Review 86: 50
Godtfredsen SE, Ingvorsen K, Yde B, Andresen O (1985) The scope of biocatalysts in organic chemical processing, in: Studies in organic chemistry 22, Biocatalysts in organic syntheses; Tramper J, van der Plas HC, Linko P (eds) Amsterdam, Elsevier, p 3
Sugiura Y, Kuwahara J, Nagasawa T, Yamada H (1987) J. Am. Chem. Soc. 109: 5848
Linko YY, Linko P (1985) Immobilized biocatalysts in organic synthesis and chemical production, in: see Ref. 2, p 159
Laane C, Tramper J, Lilly MD (eds) (1987) Studies in organic chemistry 29, Biocatalysis in organic media, Amsterdam, Elsevier
Chenault HK, Whitesides GM (1987) Appl. Biochem. Biotech. 14: 147
Whitesides GM, Wong CH (1985) Angew. Chem. 97: 617
Matos JR, Smith MB, Wong CH (1985) Bioorg. Chem 13: 121
Jones JB (1986) Tetrahedron 42: 3351
Keinan E, Hafeli EK, Seth KK, Lamed R (1986) J. Am. Chem. Soc. 108: 162
Lee LG, Whitesides GM (1986) J. Org. Chem. 51: 25
Simon H, Bader J, Günther H, Neumann S, Thanos J (1985) Angew. Chem. 97: 541
Wichmann R, Wandrey C, Bückmann AF, Kula MR (1981) Biotech. Bioeng. 23: 2789
Wandrey C, Bossow B (1985) Continuous Cofactor Regeneration, in: Proc. 3rd Int. Conf. Chemistry and Biotechnology of Biologically Active Natural Products, Sept. 16–21, 1985, Sofia (Bulgaria) Bulgarian Acad. Sci. 1: 195
Ohshima T, Wandrey C, Kula MR, Soda K (1985) Biotech. Bioeng. 27: 1616
Hummel W, Schütte H, Schmidt E, Wandrey C, Kula MR (1987) Appl. Microbiol. Biotechnol. 26:409
Asano Y, Nakazawa A (1987) Agric. Biol. Chem. 51: 2035
Asano Y, Endo K, Nakazawa A, Hibino Y, Okazaki N, Ohmori M, Numao N, Kondo K (1987) Agric. Biol. Chem. 51: 2621
Hummel W, Schütte H, Kula MR (1984) Enzyme Engineering 7; Ann. N. Y. Acad. Sci. 434: 87
Riva S, Bovara R, Pasta P, Carrea G (1986) J. Org. Chem. 51: 2902
Crans DC, Kazlauskas RJ, Hirschbein BL, Wong CH, Abril O, Whitesides GM (1987) Methods in Enzymology, 136: 263
May SW, Padgette SR (1983) Bio/Technology, 5: 677
Alberti BN, Klibanov AM (1982) Enzyme Microb. Technol. 4: 47
Szwajcer E, Brodelius P, Mosbach K (1982) Enzyme. Microb. Technol. 4: 409
Aretz W, Sauber K (1984) L-Amino Acid Oxidase, in: Proc. 3rd Europ. Conf. Biotechnology, September 10–14, 1984, München (FRG), Vol. I, Rehm HJ, Behrens D (eds) Weinheim, Verlag Chemie, p 445
Tu SC, Edelstein SJ, McCormick DB (1973) Arch. Biochem. Biophys. 159: 880
Murata K, Tani K, Kato J, Chibata I (1979) J. Appl. Biochem. 1: 282
Dennda G, Kula MR (1986) Biotechnol. 4: 143
Wang SS, King CK (1979) Adv. Biochem. Eng. 12: 119
Lee LG, Whitesides GM (1985) J. Am. Chem. Soc. 107: 6999
Knowles C (1983) Patent Application PCT/GB83/00175
Ilan E, Chang TMS (1986) Appl. Biochem. Biotech. 13: 221
Kitpreechavanich V, Nishio N, Hayashi M, Nagai S (1985) Biotech. Lett. 7: 657
Kulbe KD, Chmiel H (1988) Enzyme Engineering 9; Ann. N.Y. Acad. Sci. 542: 444
Mosbach K (1978) Adv Enzymology, 46: 205
Katayama N, Hayakawa K, Urabe I, Okada H (1984) Enzyme Microb. Technol. 6: 538
Everse J, Zoll EL, Kahan L, Kaplan NO (1971) Bioorg. Chem. 1: 207
Chambers RP, Walle EM, Baricos WH, Cohen W (1978) Enzyme Engineering, 3: 363
Schütte H, Hummel W, Kula MR (1982) Biochem. Biophys. Acta 716: 298
Wong CH, Whitesides GM (1981) J. Am. Chem. Soc. 103: 4890
Wong CH, Drueckhammer DG, Sweers HM (1985) J. Am. Chem. Soc. 107: 4028
Bückmann AF (1987) Progress Report 1987, Biotechnology Action Programme of the EEC, 2:255
Kazlauskas RJ, Whitesides GM (1985) J. Org. Chem. 50: 1069
Wong CH, McCurry SD, Whitesides GM (1980) J. Am. Chem. Soc. 102: 7983
Wandrey C, Wichmann R, Leuchtenberger W, Kula MR, Bückmann AF (1982) US Patent 4.304.858
Wandrey C, Wichmann R, Leuchtenberger W, Kula MR, Bückmann AF (1982) US Patent 4.326.031
Kroner KH, Schütte H, Stach W, Kula MR (1982) J. Chem. Tech. Biotechnol. 32: 130
Cordes A, Kula MR (1986) J. Chromatogr. 376: 375
Yamamoto I, Saiki T, Liu SM, Ljungdahl LG (1983) J. Biol. Chem. 258: 1826
Rella R, Raia CA, Pisani FM, Trincone A, Vaccaro C, Nucci R, Gambacorta A, De Rosa M, Rossi M (1987) Specifity and Stability in Organic Solvents of a Novel Archaebacterial NAD-Dependent Alcohol Dehydrogenase, in: Proc. 4th Europ Congr on Biotechn, June 14–19, 1987, Amsterdam (NL), Vol. 2, Neijssel OM, van der Meer RR, Luyben KChAM (eds) Amsterdam, Elsevier, p 336
Rossmann MG, Moras D, Olsen KW (1974) Nature 250: 194
Wierenga RK, Drenth J, Schulz GE (1983) J. Mol. Biol. 167: 725
Mansson MO, Mosbach K (1987) in: Coenzymes and Cofactors, Dolphin D, Paulson R, Avramovic O (eds) 2B: 217, Wiley, New York
Okada H, Urabe I (1987) Methods in Enzymology 136: 34
Sogin DC (1976) J. Neurochem. 27: 1333
Jones JB, Taylor KE (1976) Can. J. Chem. 54: 2969
Lindberg M, Larsson PO, Mosbach K (1973) Eur. J. Biochem. 40: 187
Lowe CR, Mosbach K (1974) Eur. J. Biochem. 49: 511
Muramatsu M, Urabe I, Yamada Y, Okuda H (1977) Eur. J. Biochem. 80: 111
Okuda K, Urabe I, Okada H (1985) Eur. J. Biochem. 151: 33
Zappelli P, Rossodivita A, Re L (1975) Eur. J. Biochem. 54: 475
Zappelli P, Pappa R, Rossodivita A, Re L (1977) Eur. J. Biochem. 72: 309
Zappelli P, Pappa R, Rossodivita A, Re L (1978) Eur. J. Biochem. 89: 491
Schmidt HL, Grenner G (1976) Eur. J. Biochem. 67: 295
Weibel MK, Fuller CW, Stadel JM, Bückmann, AF, Doyle T, Bright HJ (1974) Enzyme Engineering 2: 203
Bückmann AF (1979) German Patent DP 28.41.414
Sakamoto H, Nukamura A, Urabe I, Yamada Y, Okada H (1986) J. Ferment. Technol. 64: 511
Bückmann AF (1988) Heterocycles 27: 1623
Imahori K, Tomita K (1980) German Patent DP 2945129.4
Wykes JR, Dunnill P, Lilly MD (1972) Biochim. Biophys. Acta 286: 260
Lee CY, Kaplan NO (1975) Arch. Biochem. Biophys. 168: 665
Zappelli P, Rossodivita A, Prosperi G, Pappa R, Re L (1976) Eur. J. Biochem. 62: 211
Zappelli P, Pappa R, Rossodivita A, Re L (1977) Eur. J. Biochem. 72: 309
Okuda K, Urabe I, Okada H (1985) Eur. J. Biochem. 147: 249
Riva S, Carrea G, Veronese FM, Bückmann AF (1986) Enzyme Microb. Technol. 9: 556
Bückmann AF (1987) Europ Patent Appl 0 247 537.A2
Bückmann AF, Wray V, van der Plas HC (1987) Two Unexpected Transformations of N(1)-(2-Aminoethyl)-Adenine Derivatives of NAD, NADP and FAD under Mild Aqueous Conditions, in: Proc. 11th Intl. Conf. Heterocyclic Chemistry, August 16–21, 1987, Heidelberg (FRG) Neidlein R (ed) Frankfurt, GDCh, p 398
Davies P, Mosbach K (1974) Biochim. Biophys. Acta 370: 329
Malinauskas AA, Kulys JJ (1978) Biotech. Bioeng. 20: 769
Sakaguchi Y, Murachi T (1980) J. Appl. Biochem. 2: 117
Bückmann AF, Kula MR, Wichmann R, Wandrey C (1981) J. Appl. Biochem. 3: 301
Katayama N, Urabe I, Okada H (1983) Eur. J. Biochem. 132: 403
Hayakawa K, Urabe I, Okada H (1985) J. Ferment. Technol. 63: 245
Yamazaki Y, Maeda H, Suzuki H (1976) Biotech. Bioeng. 18: 1761
Yoshikawa M, Goto M, Ikura K, Sasaki R, Chiba H (1983) Agric. Biol. Chem. 46: 207
Bückmann AF, Morr M, Johansson G (1981) Makromol. Chem. 82: 1379
Yamazaki Y, Maeda H (1981) Agric. Biol. Chem. 45: 2277
Le Goffic F, Sicsic S, Vincent C (1980) Eur. J. Biochem. 108: 143
Fuller CW, Rubin JR, Bright HJ (1980) Eur. J. Biochem. 103: 421
Bückmann AF, Morr M, Kula MR (1987) Biotechnol. Appl. Biochem. 9: 258
Albertsson PA (1985) Partition of cell particles and macromolecules, 3rd ed., Wiley Interscience, New York
Mansson MO, Larsson PO, Mosbach K (1987) Eur. J. Biochem. 86: 455
Mansson MO, Larsson PO, Mosbach K (1979) FEBS Lett. 98: 309
Gacesa P, Venn RF (1979) Biochem. J. 177: 369
Kovar J, Simek K, Kucera I, Matyska L (1984) Eur. J. Biochem. 139: 585
SchÄfer HG, Jacobi T, Eichhorn H, Woenckhaus C (1986) Biol. Chem. Hoppe-Seyler 367: 969
Eguchi, T, Iizuka T, Kagotani T, Lee JH, Urabe I, Okada H (1986) Eur. J. Biochem. 155: 415
Nakamura A, Urabe I, Okada H (1986) J. Biol. Chem. 261: 16792
Kato N, Yamagami T, Shimao M, Sakazawa C (1987) Appl, Microb. Biotechnol. 25: 415
Goulas P (1987) Eur. J. Biochem. 168: 469
Woenckhaus C, Koob R, Burkhard A, SchÄfer HG (1983) Bioorg. Chem. 12: 45
Jacobi T, Woenckhaus C (1987) Binary enzyme reactors with modified dehydrogenase, in: Proc. 4th Europ Congr Biotechn, Vol. 1 Neijssel OM, van der Meer RR, Luyben KChAM (eds) Elsevier, Amsterdam, p 72
Wandrey C, Wichmann R (1985) Coenzyme regeneration in membrane reactors, in: Application of isolated enzymes and immobilized cells to biotechnology Laskin A (ed) Addison Wesley, p 177
Adachi S, Ogata M, Tobita H, Hashimoto K (1984) Enzyme Microbiol. Technol. 6: 259
Grenner G, Schmidt HL, Völkl W (1976) Hoppe-Seyler’s Z. Physiol. Chem. 357: 887
BrÄnden CJ, Jornvall H, Eklund H, Furugren B (1975) Alcohol dehydrogenase, in: The Enzymes, Vol. 11, Boyer PD (ed) New York, Academic Press p 103
Holbrook JJ, Liljas A, Steindl SJ, Rossmann, MG (1975) Lactate dehydrogenase, in: The Enzymes, Vol. 11, Boyer PD (ed), New York, Academic Press p 191
Yamazaki Y, Maeda H, Satoh A, Hiromi K (1984) J. Biochem. 95: 109
Schmidt HL, Dolabdjian B (1980) Methods in Enzymology 66: 176
Furukawa D, Urabe I, Okada H (1981) Eur. J. Biochem. 114: 101
Furukawa S, Katayama N, Iizuka T, Urabe I, Okada H (1980) FEBS Lett. 121: 239
Hummel W, Schütte H, Kula MR (1984) Enzyme Engineering 7; Ann. N. Y. Acad. Sci. 434: 194
Jones JB (1985) An illustrative example of a synthetically useful enzyme: Horse liver alcohol dehydrogenase, in: Enzymes in organic synthesis, Ciba Foundation Symposium 111, Porter R, Clark S (eds) London, Pitman, p 3
Whitesides GM (1985) Applications of cell-Free enzymes in organic synthesis, in: Enzymes in organic synthesis, Ciba Foundation Symposium 111, Porter R, Clark S (eds) London, Pitman, p 76
Carrea G, Bovara R, Longhi R, Riva S (1985) Enzyme Microb. Technol. 7: 597
Kajiwara S, Maeda H (1985) Biotech. Bioeng. 18: 1794
Yamazaki Y, Maeda H (1982) Agric. Biol. Chem. 46: 1571
Chang TMS (1987) Methods in Enzymology 16: 67
Flaschel E, Wandrey C, Kula MR (1983) Adv. Biochem. Eng/Biotechnol. 26: 73
Fiolitakis E, Wandrey C (1982) Reaction technology of the enzymatically catalysed production of l-alanine, in: Proc. 3rd Rotenburg Fermentation Symposium, Lafferty RM (ed) p 273
Leuchtenberger W, Wandrey C, Kula MR (1986) German Patent, 33.07.094.6
Tichy S, Vasic-Racki D, Schütte H, Talsky G, Wandrey C (1987) Chem. Biochem. Eng. 1: 25
Schmidt E, Vasic-Racki D, Wandrey C (1987) Appl. Microbiol. Biotechnol. 26: 42
Marconi W, Prosperi G, Giovenco S, Morisi F (1975) J. Mol. Catal. 1: 111
Grunwald J, Chang TMS (1979) J. Appl. Biochem. 1: 104
Grunwald J, Chang TMS (1981) J. Mol. Catal. 11: 83
Sakaguchi Y, Sukahara M, Endo J, Murachi T (1981) J. Appl. Biochem. 3: 32
Schütte H, Hummel W, Kula M-R (1984) Appl. Microbiol. Biotechnol. 19: 167
Hummel W, Schütte H, Kula MR (1985) Appl. Microbiol. Biotechnol. 21: 7
Hummel W, Schütte H, Kula MR, Leuchtenberger W (1985) German Pat Appl P 35.36.662.1
Schütte H, Hummel W, Tsai H, Kula MR (1985) Appl. Microbiol. Biotechnol. 22: 306
Campagna R, Bückmann AF (1987) Appl. Microbiol. Biotechnol. 26: 417
Schütte H, Hummel W, Kula MR, Leuchtenberger W (1985) German Patent P 32.34.022.2
Schmidt E, Wichmann R, Kula MR, Wandrey C (1987) Production of l-amino acids from their corresponding α-ketoacids, in: Proc. of the Sectorial Meeting of Contractors, CEC Biotechnology Action Programme (BAP), Enzyme Engineering: Protein design and application in biocatalysis, Capri (Italy) Rossi M (ed) Brussels, CEC, p 131
Furukawa S, Sugimoto Y, Urabe I, Okada H (1980) Biochimie 62: 629
Kula MR, Kroner KH, Hustedt H (1982) Adv. Biochem. Eng. 24: 73
Bückmann AF (1987) Biocatalysis 1: 173
Info 87-9 (1987) Merck-Schuchardt, Germany (FRG)
Lotter H, Drauz KH, Kleemann A, Leuchtenberger W, Wandrey C, Kula MR (1987) Herstellung und Anwendung von l-tert-Leucin, Poster presented at the 21th GDCh Hauptversammlung, 13–18 Sept, 1987, Berlin
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Bückmann, A.F., Carrea, G. (1989). Synthesis and application of water-soluble macromolecular derivatives of the redox coenzymes NAD(H), NADP(H) and FAD. In: Vertebrate Cell Culture II and Enzyme Technology. Advances in Biochemical Engineering/Biotechnology, vol 39/1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0051953
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