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Volumn 57, Issue 5, 2014, Pages 385-391

Hydrophobic formic acid esters for cofactor regeneration in aqueous/organic two-liquid phase systems

Author keywords

Biocatalysis; Cofactor regeneration; Monooxygenase; Oxyfunctionalisation; Two liquid phase system

Indexed keywords

BIOCATALYSIS; COFACTOR REGENERATION; MONOOXYGENASES; OXYFUNCTIONALISATION; TWO-LIQUID-PHASE SYSTEMS;

EID: 84894362312     PISSN: 10225528     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11244-013-0195-y     Document Type: Article
Times cited : (13)

References (34)
  • 2
    • 0042933788 scopus 로고    scopus 로고
    • Recent developments in pyridine nucleotide regeneration
    • 10.1016/S0958-1669(03)00094-6
    • van der Donk WA, Zhao H (2003) Recent developments in pyridine nucleotide regeneration. Curr Opin Biotechnol 14(4):421-426
    • (2003) Curr Opin Biotechnol , vol.14 , Issue.4 , pp. 421-426
    • Van Der Donk, W.A.1    Zhao, H.2
  • 3
    • 80052323316 scopus 로고    scopus 로고
    • Enzymatic reductions for the chemist
    • 1:CAS:528:DC%2BC3MXhtV2hsr3E 10.1039/c1gc15424a
    • Hollmann F, Arends IWCE, Holtmann D (2011) Enzymatic reductions for the chemist. Green Chem 13(9):2285-2313
    • (2011) Green Chem , vol.13 , Issue.9 , pp. 2285-2313
    • Hollmann, F.1    Arends, I.2    Holtmann, D.3
  • 4
    • 79751478451 scopus 로고    scopus 로고
    • Enzyme-mediated oxidations for the chemist
    • 1:CAS:528:DC%2BC3MXhs1GjtL8%3D 10.1039/c0gc00595a
    • Hollmann F, Arends IWCE, Buehler K, Schallmey A, Buhler B (2011) Enzyme-mediated oxidations for the chemist. Green Chem 13:226-265
    • (2011) Green Chem , vol.13 , pp. 226-265
    • Hollmann, F.1    Arends, I.2    Buehler, K.3    Schallmey, A.4    Buhler, B.5
  • 5
    • 79751520578 scopus 로고    scopus 로고
    • Biocatalytic redox reactions for organic synthesis: Nonconventional regeneration methods
    • 1:CAS:528:DC%2BC3cXovVCgur8%3D 10.1002/cctc.201000069
    • Hollmann F, Arends Isabel WCE, Buehler K (2010) Biocatalytic redox reactions for organic synthesis: nonconventional regeneration methods. ChemCatChem 2(7):762-782
    • (2010) ChemCatChem , vol.2 , Issue.7 , pp. 762-782
    • Hollmann, F.1    Arends Isabel, W.C.E.2    Buehler, K.3
  • 6
    • 84872506468 scopus 로고    scopus 로고
    • Recent advances in cofactor regeneration systems applied to biocatalyzed oxidative processes
    • 10.2174/138527212804004643 1:CAS:528:DC%2BC38XhvFSns7fK 10.2174/138527212804004643
    • Rodriguez C, Lavandera I, Gotor V (2012) Recent advances in cofactor regeneration systems applied to biocatalyzed oxidative processes. Curr Org Chem 16(21):2525-2541. doi: 10.2174/138527212804004643
    • (2012) Curr Org Chem , vol.16 , Issue.21 , pp. 2525-2541
    • Rodriguez, C.1    Lavandera, I.2    Gotor, V.3
  • 7
    • 33847087242 scopus 로고
    • Enzyme-catalyzed organic synthesis - NADH regeneration by using formate dehydrogenase
    • 10.1021/ja00543a038 1:CAS:528:DyaL3cXmtlCnsLs%3D 10.1021/ja00543a038
    • Shaked Z, Whitesides GM (1980) Enzyme-catalyzed organic synthesis - NADH regeneration by using formate dehydrogenase. J Am Chem Soc 102(23):7104-7105. doi: 10.1021/ja00543a038
    • (1980) J Am Chem Soc , vol.102 , Issue.23 , pp. 7104-7105
    • Shaked, Z.1    Whitesides, G.M.2
  • 8
    • 84255169447 scopus 로고    scopus 로고
    • 2+ complex catalysts and enzymatic reduction using oxidoreductases with cofactor regeneration
    • 10.1002/asia.201100584 1:CAS:528:DC%2BC3MXhs1elurrN 10.1002/asia. 201100584
    • 2+ complex catalysts and enzymatic reduction using oxidoreductases with cofactor regeneration. Chem-Asian J 7(1):64-74. doi: 10.1002/asia.201100584
    • (2012) Chem-Asian J , vol.7 , Issue.1 , pp. 64-74
    • Sonoike, S.1    Itakura, T.2    Kitamura, M.3    Aoki, S.4
  • 10
    • 34547149690 scopus 로고    scopus 로고
    • Hydroxylation of dodecanoic acid and (2R,4R,6R,8R)-tetramethyldecanol on a preparative scale using an NADH-dependent CYP102A1 mutant
    • 10.1002/adsc.200700054 1:CAS:528:DC%2BD2sXntVSjurc%3D 10.1002/adsc.200700054
    • Kuehnel K, Maurer SC, Galeyeva Y, Frey W, Laschat S, Urlacher VB (2007) Hydroxylation of dodecanoic acid and (2R,4R,6R,8R)-tetramethyldecanol on a preparative scale using an NADH-dependent CYP102A1 mutant. Adv Synth Catal 349(8-9):1451-1461. doi: 10.1002/adsc.200700054
    • (2007) Adv Synth Catal , vol.349 , Issue.8-9 , pp. 1451-1461
    • Kuehnel, K.1    Maurer, S.C.2    Galeyeva, Y.3    Frey, W.4    Laschat, S.5    Urlacher, V.B.6
  • 11
    • 0242439281 scopus 로고    scopus 로고
    • + cofactor recycling system: Towards a technical application of heme-containing monooxygenases in fine chemical synthesis
    • 1:CAS:528:DC%2BD3sXkvF2qt70%3D 10.1002/adsc.200303021
    • + cofactor recycling system: towards a technical application of heme-containing monooxygenases in fine chemical synthesis. Adv Synth Catal 345(6-7):802-810
    • (2003) Adv Synth Catal , vol.345 , Issue.6-7 , pp. 802-810
    • Maurer, S.C.1    Schulze, H.2    Schmid, R.D.3    Urlacher, V.B.4
  • 12
    • 4544324488 scopus 로고    scopus 로고
    • Coupling of biocatalytic asymmetric epoxidation with nadh regeneration in organic-aqueous emulsions
    • 1:CAS:528:DC%2BD2cXjsFWhtr4%3D 10.1002/anie.200353338
    • Hofstetter K, Lutz J, Lang I, Witholt B, Schmid A (2004) Coupling of biocatalytic asymmetric epoxidation with nadh regeneration in organic-aqueous emulsions. Angew Chem Int Ed 43(16):2163-2166
    • (2004) Angew Chem Int Ed , vol.43 , Issue.16 , pp. 2163-2166
    • Hofstetter, K.1    Lutz, J.2    Lang, I.3    Witholt, B.4    Schmid, A.5
  • 13
    • 0037010696 scopus 로고    scopus 로고
    • Preparative application of 2-hydroxybiphenyl 3-monooxygenase with enzymatic cofactor regeneration in organic-aqueous reaction media
    • 10.1016/S1381-1177(02)00165-0
    • Lutz J, Mozhaev VV, Khmelnitsky YL, Witholt B, Schmid A (2002) Preparative application of 2-hydroxybiphenyl 3-monooxygenase with enzymatic cofactor regeneration in organic-aqueous reaction media. J Mol Catal B Enzym 19-20:177-187
    • (2002) J Mol Catal B Enzym , vol.19-20 , pp. 177-187
    • Lutz, J.1    Mozhaev, V.V.2    Khmelnitsky, Y.L.3    Witholt, B.4    Schmid, A.5
  • 14
    • 0035931416 scopus 로고    scopus 로고
    • Preparative regio- and chemoselective functionalization of hydrocarbons catalyzed by cell free preparations of 2-hydroxybiphenyl 3-monooxygenase
    • 1:CAS:528:DC%2BD3MXptlSruw%3D%3D 10.1016/S1381-1177(00)00180-6
    • Schmid A, Vereyken I, Held M, Witholt B (2001) Preparative regio- and chemoselective functionalization of hydrocarbons catalyzed by cell free preparations of 2-hydroxybiphenyl 3-monooxygenase. J Mol Catal B Enzym 11(4-6):455-462
    • (2001) J Mol Catal B Enzym , vol.11 , Issue.4-6 , pp. 455-462
    • Schmid, A.1    Vereyken, I.2    Held, M.3    Witholt, B.4
  • 15
    • 2442646281 scopus 로고    scopus 로고
    • Use of an ionic liquid in a two-phase system to improve an alcohol dehydrogenase catalysed reduction
    • 10.1039/b401065e 10.1039/b401065e
    • Eckstein M, Villela M, Liese A, Kragl U (2004) Use of an ionic liquid in a two-phase system to improve an alcohol dehydrogenase catalysed reduction. Chem Commun 9:1084-1085. doi: 10.1039/b401065e
    • (2004) Chem Commun , vol.9 , pp. 1084-1085
    • Eckstein, M.1    Villela, M.2    Liese, A.3    Kragl, U.4
  • 17
    • 84873182641 scopus 로고    scopus 로고
    • Increasing the productivity of peroxidase-catalyzed oxyfunctionalization: A case study on the potential of two-liquid-phase systems
    • 10.1002/cctc.201200490 1:CAS:528:DC%2BC38Xhs1agsrrK 10.1002/cctc. 201200490
    • Churakova E, Arends IWCE, Hollmann F (2013) Increasing the productivity of peroxidase-catalyzed oxyfunctionalization: a case study on the potential of two-liquid-phase systems. ChemCatChem 5:565-568. doi: 10.1002/cctc.201200490
    • (2013) ChemCatChem , vol.5 , pp. 565-568
    • Churakova, E.1    Arends, I.2    Hollmann, F.3
  • 18
    • 80054993701 scopus 로고    scopus 로고
    • Formate dehydrogenase - A biocatalyst with novel applications in organic chemistry
    • 10.1039/c1ob06064c
    • Frohlich P, Albert K, Bertau M (2011) Formate dehydrogenase - a biocatalyst with novel applications in organic chemistry. Org Biomol Chem 9(22):7941-7950
    • (2011) Org Biomol Chem , vol.9 , Issue.22 , pp. 7941-7950
    • Frohlich, P.1    Albert, K.2    Bertau, M.3
  • 19
    • 0035825143 scopus 로고    scopus 로고
    • The first synthetic application of a monooxygenase employing indirect electrochemical NADH regeneration
    • 1:CAS:528:DC%2BD3MXltlKqtw%3D%3D 10.1002/1521-3773(20010105)40:1<169: AID-ANIE169>3.0.CO;2-T
    • Hollmann F, Schmid A, Steckhan E (2001) The first synthetic application of a monooxygenase employing indirect electrochemical NADH regeneration. Angew Chem Int Ed 40(1):169-171
    • (2001) Angew Chem Int Ed , vol.40 , Issue.1 , pp. 169-171
    • Hollmann, F.1    Schmid, A.2    Steckhan, E.3
  • 20
    • 0033586405 scopus 로고    scopus 로고
    • An integrated process for the production of toxic catechols from toxic phenols based on a designer biocatalyst
    • 1:CAS:528:DyaK1MXhtVens7s%3D 10.1002/(SICI)1097-0290(19990320)62: 6<641: AID-BIT3>3.0.CO;2-H
    • Held M, Schmid A, Kohler HPE, Suske W, Witholt B, Wubbolts MG (1999) An integrated process for the production of toxic catechols from toxic phenols based on a designer biocatalyst. Biotechnol Bioeng 62(6):641-648
    • (1999) Biotechnol Bioeng , vol.62 , Issue.6 , pp. 641-648
    • Held, M.1    Schmid, A.2    Kohler, H.P.E.3    Suske, W.4    Witholt, B.5    Wubbolts, M.G.6
  • 21
    • 0002817727 scopus 로고    scopus 로고
    • Preparative scale production of 3-substituted catechols using a novel monooxygenase from Pseudomonas azelaica HBP 1
    • 1:CAS:528:DyaK1cXltlersbg%3D 10.1016/S1381-1177(98)00012-5
    • Held M, Suske W, Schmid A, Engesser KH, Kohler HPE, Witholt B, Wubbolts MG (1998) Preparative scale production of 3-substituted catechols using a novel monooxygenase from Pseudomonas azelaica HBP 1. J Mol Catal B Enzym 5(1-4):87-93
    • (1998) J Mol Catal B Enzym , vol.5 , Issue.1-4 , pp. 87-93
    • Held, M.1    Suske, W.2    Schmid, A.3    Engesser, K.H.4    Kohler, H.P.E.5    Witholt, B.6    Wubbolts, M.G.7
  • 22
    • 0030777335 scopus 로고    scopus 로고
    • Purification and characterization of 2-hydroxybiphenyl 3-monooxygenase, a novel NADH-dependent, FAD-containing aromatic hydroxylase from Pseudomonas azelaica HBP1
    • 10.1074/jbc.272.39.24257 1:CAS:528:DyaK2sXmsFamsro%3D 10.1074/jbc.272.39.24257
    • Suske WA, Held M, Schmid A, Fleischmann T, Wubbolts MG, Kohler H-PE (1997) Purification and characterization of 2-hydroxybiphenyl 3-monooxygenase, a novel NADH-dependent, FAD-containing aromatic hydroxylase from Pseudomonas azelaica HBP1. J Biol Chem 272(39):24257-24265. doi: 10.1074/jbc.272.39.24257
    • (1997) J Biol Chem , vol.272 , Issue.39 , pp. 24257-24265
    • Suske, W.A.1    Held, M.2    Schmid, A.3    Fleischmann, T.4    Wubbolts, M.G.5    Kohler, H.-P.6
  • 23
    • 0032530489 scopus 로고    scopus 로고
    • E-coli JM109 pHBP461, a recombinant biocatalyst for the regioselective monohydroxylation of ortho-substituted phenols to their corresponding 3-substituted catechols
    • 1:CAS:528:DyaK1cXltleqs7k%3D 10.1016/S1381-1177(98)00058-7
    • Schmid A, Kohler HPE, Engesser KH (1998) E-coli JM109 pHBP461, a recombinant biocatalyst for the regioselective monohydroxylation of ortho-substituted phenols to their corresponding 3-substituted catechols. J Mol Catal B Enzym 5(1-4):311-316
    • (1998) J Mol Catal B Enzym , vol.5 , Issue.1-4 , pp. 311-316
    • Schmid, A.1    Kohler, H.P.E.2    Engesser, K.H.3
  • 24
    • 0034011107 scopus 로고    scopus 로고
    • Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues
    • 10.1046/j.1432-1327.2000.01123.x 1:CAS:528:DC%2BD3cXhvVagsrw%3D 10.1046/j.1432-1327.2000.01123.x
    • Slusarczyk H, Felber S, Kula MR, Pohl M (2000) Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues. Eur J Biochem 267(5):1280-1289. doi: 10.1046/j.1432-1327.2000.01123.x
    • (2000) Eur J Biochem , vol.267 , Issue.5 , pp. 1280-1289
    • Slusarczyk, H.1    Felber, S.2    Kula, M.R.3    Pohl, M.4
  • 25
    • 0033584866 scopus 로고    scopus 로고
    • Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1
    • 10.1074/jbc.274.47.33355 1:CAS:528:DyaK1MXns1aqu74%3D 10.1074/jbc.274.47.33355
    • Suske WA, van Berkel WJH, Kohler H-PE (1999) Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1. J Biol Chem 274(47):33355-33365. doi: 10.1074/jbc.274.47.33355
    • (1999) J Biol Chem , vol.274 , Issue.47 , pp. 33355-33365
    • Suske, W.A.1    Van Berkel, W.J.H.2    Kohler, H.-P.3
  • 27
    • 80055044069 scopus 로고    scopus 로고
    • Recent advances in alcohol dehydrogenase-catalyzed asymmetric production of hydrophobic alcohols
    • 10.1039/c1cy00160d 1:CAS:528:DC%2BC3MXhtlaksr%2FJ 10.1039/c1cy00160d
    • Musa MM, Phillips RS (2011) Recent advances in alcohol dehydrogenase-catalyzed asymmetric production of hydrophobic alcohols. Catal Sci Technol 1(8):1311-1323. doi: 10.1039/c1cy00160d
    • (2011) Catal Sci Technol , vol.1 , Issue.8 , pp. 1311-1323
    • Musa, M.M.1    Phillips, R.S.2
  • 28
    • 77953490670 scopus 로고    scopus 로고
    • Alcohol dehydrogenase in non-aqueous media using high-pressure technologies: Reaction set-up and deactivation determination
    • 10.1002/jctb.2411 1:CAS:528:DC%2BC3cXnsFyhtLw%3D 10.1002/jctb.2411
    • Thorey P, Knez Z, Habulin M (2010) Alcohol dehydrogenase in non-aqueous media using high-pressure technologies: reaction set-up and deactivation determination. J Chem Technol Biotechnol 85(7):1011-1016. doi: 10.1002/jctb.2411
    • (2010) J Chem Technol Biotechnol , vol.85 , Issue.7 , pp. 1011-1016
    • Thorey, P.1    Knez, Z.2    Habulin, M.3
  • 29
    • 50949118754 scopus 로고    scopus 로고
    • An exceptionally DMSO-tolerant alcohol dehydrogenase for the stereoselective reduction of ketones
    • 10.1002/cssc.200800032 1:CAS:528:DC%2BD1cXntlWjsrk%3D 10.1002/cssc.200800032
    • Lavandera I, Kern A, Schaffenberger M, Gross J, Glieder A, de Wildeman S, Kroutil W (2008) An exceptionally DMSO-tolerant alcohol dehydrogenase for the stereoselective reduction of ketones. ChemSusChem 1(5):431-436. doi: 10.1002/cssc.200800032
    • (2008) ChemSusChem , vol.1 , Issue.5 , pp. 431-436
    • Lavandera, I.1    Kern, A.2    Schaffenberger, M.3    Gross, J.4    Glieder, A.5    De Wildeman, S.6    Kroutil, W.7
  • 30
    • 0034694931 scopus 로고    scopus 로고
    • Stability and activity of alcohol dehydrogenases in W/O-microemulsions: Enantioselective reduction including cofactor regeneration
    • 1:CAS:528:DC%2BD3cXoslajtLw%3D 10.1002/1097-0290(20001220)70:6<638: AID-BIT5>3.0.CO;2-#
    • Orlich B, Berger H, Lade M, Schomacker R (2000) Stability and activity of alcohol dehydrogenases in W/O-microemulsions: enantioselective reduction including cofactor regeneration. Biotechnol Bioeng 70(6):638-646
    • (2000) Biotechnol Bioeng , vol.70 , Issue.6 , pp. 638-646
    • Orlich, B.1    Berger, H.2    Lade, M.3    Schomacker, R.4
  • 31
    • 0034617885 scopus 로고    scopus 로고
    • Alcohol dehydrogenase is active in supercritical carbon dioxide
    • 10.1039/b004069j
    • Matsuda T, Harada T, Nakamura K (2000) Alcohol dehydrogenase is active in supercritical carbon dioxide. Chem Comm 23(15):1367-1368
    • (2000) Chem Comm , vol.23 , Issue.15 , pp. 1367-1368
    • Matsuda, T.1    Harada, T.2    Nakamura, K.3
  • 32
    • 33845374385 scopus 로고
    • Asymmetric oxidoreductions catalyzed by alcohol dehydrogenase in organic solvents
    • 10.1021/ja00281a044 1:CAS:528:DyaL28Xls1OksLg%3D 10.1021/ja00281a044
    • Grunwald J, Wirz B, Scollar MP, Klibanov AM (1986) Asymmetric oxidoreductions catalyzed by alcohol dehydrogenase in organic solvents. J Am Chem Soc 108(21):6732-6734. doi: 10.1021/ja00281a044
    • (1986) J Am Chem Soc , vol.108 , Issue.21 , pp. 6732-6734
    • Grunwald, J.1    Wirz, B.2    Scollar, M.P.3    Klibanov, A.M.4
  • 33
    • 0042933786 scopus 로고    scopus 로고
    • Asymmetric enzymatic oxidoreductions in organic solvents
    • 1:CAS:528:DC%2BD3sXmslenu70%3D 10.1016/S0958-1669(03)00074-0
    • Klibanov AM (2003) Asymmetric enzymatic oxidoreductions in organic solvents. Curr Opin Biotechnol 14(4):427-431
    • (2003) Curr Opin Biotechnol , vol.14 , Issue.4 , pp. 427-431
    • Klibanov, A.M.1
  • 34
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • 1:CAS:528:DC%2BD3MXlvFWiuw%3D%3D 10.1038/35051719
    • Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409(6817):241-246
    • (2001) Nature , vol.409 , Issue.6817 , pp. 241-246
    • Klibanov, A.M.1


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