메뉴 건너뛰기




Volumn 110, Issue 1, 2013, Pages 68-77

Multi-enzymatic one-pot reduction of dehydrocholic acid to 12-keto-ursodeoxycholic acid with whole-cell biocatalysts

Author keywords

Biocatalysis; Cofactor regeneration; Hydroxysteroid dehydrogenase; Ursodeoxycholic acid; Whole cell biotransformation

Indexed keywords

BIOCATALYSIS; COFACTOR REGENERATION; HYDROXYSTEROID DEHYDROGENASE; URSODEOXYCHOLIC ACID; WHOLE-CELL BIOTRANSFORMATIONS;

EID: 84869829028     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24606     Document Type: Article
Times cited : (24)

References (37)
  • 2
    • 0032530505 scopus 로고    scopus 로고
    • Biocatalysis to amino acid-based chiral pharmaceuticals-Examples and perspectives
    • Bommarius AS, Schwarm M, Drauz K. 1998. Biocatalysis to amino acid-based chiral pharmaceuticals-Examples and perspectives. J Mol Catal B Enzym 5: 1-11.
    • (1998) J Mol Catal B Enzym , vol.5 , pp. 1-11
    • Bommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 4
    • 0030000525 scopus 로고    scopus 로고
    • A new enzymatic route to the synthesis of 12-ketoursodeoxycholic acid
    • Bovara R, Carrea G, Riva S, Secundo F. 1996. A new enzymatic route to the synthesis of 12-ketoursodeoxycholic acid. Biotechnol Lett 18: 305-308.
    • (1996) Biotechnol Lett , vol.18 , pp. 305-308
    • Bovara, R.1    Carrea, G.2    Riva, S.3    Secundo, F.4
  • 5
    • 79954593169 scopus 로고    scopus 로고
    • Biocatalytic process optimization based on mechanistic modeling of cholic acid oxidation with cofactor regeneration
    • Braun M, Link H, Liu L, Schmid RD, Weuster-Botz D. 2011. Biocatalytic process optimization based on mechanistic modeling of cholic acid oxidation with cofactor regeneration. Biotechnol Bioeng 108: 1307-1317.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1307-1317
    • Braun, M.1    Link, H.2    Liu, L.3    Schmid, R.D.4    Weuster-Botz, D.5
  • 6
    • 84872036582 scopus 로고    scopus 로고
    • Novel whole-cell biocatalysts with recombinant hydroxysteroid dehydrogenases for the asymmetric reduction of dehydrocholic acid
    • Braun M, Sun B, Anselment B, Weuster-Botz D. 2012. Novel whole-cell biocatalysts with recombinant hydroxysteroid dehydrogenases for the asymmetric reduction of dehydrocholic acid. Appl Microbiol Biotechnol 95(6): 1457-1468.
    • (2012) Appl Microbiol Biotechnol , vol.95 , Issue.6 , pp. 1457-1468
    • Braun, M.1    Sun, B.2    Anselment, B.3    Weuster-Botz, D.4
  • 8
    • 0027102182 scopus 로고
    • Enzymatic synthesis of 12-ketoursodeoxycholic acid from dehydrocholic acid in a membrane reactor
    • Carrea G, Pilotti A, Riva S, Canzi E, Ferrari A. 1992. Enzymatic synthesis of 12-ketoursodeoxycholic acid from dehydrocholic acid in a membrane reactor. Biotechnol Lett 14: 1131-1134.
    • (1992) Biotechnol Lett , vol.14 , pp. 1131-1134
    • Carrea, G.1    Pilotti, A.2    Riva, S.3    Canzi, E.4    Ferrari, A.5
  • 9
    • 33847273107 scopus 로고    scopus 로고
    • Permeability issues in whole-cell bioprocesses and cellular membrane engineering
    • Chen RR. 2007. Permeability issues in whole-cell bioprocesses and cellular membrane engineering. Appl Microbiol Biotechnol 74: 730-738.
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 730-738
    • Chen, R.R.1
  • 10
    • 0026857665 scopus 로고
    • NADPH regeneration by glucose dehydrogenase from Gluconobacter scleroides for l-leucovorin synthesis
    • Eguchi T, Kuge Y, Inoue K, Yoshikawa N, Mochida K, Uwajima T. 1992. NADPH regeneration by glucose dehydrogenase from Gluconobacter scleroides for l-leucovorin synthesis. Biosci Biotechnol Biochem 56: 701-703.
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 701-703
    • Eguchi, T.1    Kuge, Y.2    Inoue, K.3    Yoshikawa, N.4    Mochida, K.5    Uwajima, T.6
  • 11
    • 0000334097 scopus 로고
    • Oxidation of steroids. III. Selective oxidations and acylations in the bile acid series
    • Fieser LF, Rajagopalan S. 1950. Oxidation of steroids. III. Selective oxidations and acylations in the bile acid series. J Am Chem Soc 72: 5530-5536.
    • (1950) J Am Chem Soc , vol.72 , pp. 5530-5536
    • Fieser, L.F.1    Rajagopalan, S.2
  • 13
    • 0025992267 scopus 로고
    • The lack of relationship between hepatotoxicity and lithocholic-acid sulfation in biliary bile acids during chenodiol therapy in the National Cooperative Gallstone Study
    • Fisher RL, Hofmann AF, Converse JL, Rossi SS, Lan SP. 1991. The lack of relationship between hepatotoxicity and lithocholic-acid sulfation in biliary bile acids during chenodiol therapy in the National Cooperative Gallstone Study. Hepatology 14: 454-463.
    • (1991) Hepatology , vol.14 , pp. 454-463
    • Fisher, R.L.1    Hofmann, A.F.2    Converse, J.L.3    Rossi, S.S.4    Lan, S.P.5
  • 14
    • 0025357628 scopus 로고
    • Final outcome of ursodeoxycholic acid treatment in 126 patients with radiolucent gallstones
    • Gleeson D, Ruppin DC, Saunders A, Murphy GM, Dowling RH. 1990. Final outcome of ursodeoxycholic acid treatment in 126 patients with radiolucent gallstones. Q J Med 76: 711-729.
    • (1990) Q J Med , vol.76 , pp. 711-729
    • Gleeson, D.1    Ruppin, D.C.2    Saunders, A.3    Murphy, G.M.4    Dowling, R.H.5
  • 15
    • 0026021702 scopus 로고
    • Glucose dehydrogenase from Bacillus subtilis expressed in Escherichia coli. I: Purification, characterization and comparison with glucose dehydrogenase from Bacillus megaterium
    • Hilt W, Pfleiderer G, Fortnagel P. 1991. Glucose dehydrogenase from Bacillus subtilis expressed in Escherichia coli. I: Purification, characterization and comparison with glucose dehydrogenase from Bacillus megaterium Biochim Biophys Acta 1076: 298-304.
    • (1991) Biochim Biophys Acta , vol.1076 , pp. 298-304
    • Hilt, W.1    Pfleiderer, G.2    Fortnagel, P.3
  • 16
    • 0020329489 scopus 로고
    • Characterization of NADP-dependent 7 beta-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens
    • Hirano S, Masuda N. 1982. Characterization of NADP-dependent 7 beta-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens Appl Environ Microbiol 43: 1057-1063.
    • (1982) Appl Environ Microbiol , vol.43 , pp. 1057-1063
    • Hirano, S.1    Masuda, N.2
  • 17
    • 0001192237 scopus 로고
    • The preparation of chenodeoxycholic acid and its glycine and taurine conjugates
    • Hofmann AF. 1963. The preparation of chenodeoxycholic acid and its glycine and taurine conjugates. Acta Chem Scand 17: 173-186.
    • (1963) Acta Chem Scand , vol.17 , pp. 173-186
    • Hofmann, A.F.1
  • 19
    • 77956368203 scopus 로고    scopus 로고
    • Enantioselective reduction of prochiral ketones by engineered bifunctional fusion proteins
    • Hölsch K, Weuster-Botz D. 2010. Enantioselective reduction of prochiral ketones by engineered bifunctional fusion proteins. Biotechnol Appl Biochem 56: 131-140.
    • (2010) Biotechnol Appl Biochem , vol.56 , pp. 131-140
    • Hölsch, K.1    Weuster-Botz, D.2
  • 20
    • 33751290076 scopus 로고    scopus 로고
    • Open-loop control of the biomass concentration within the growth phase of recombinant protein production processes
    • Jenzsch M, Gnoth S, Beck M, Kleinschmidt M, Simutis R, Lübbert A. 2006. Open-loop control of the biomass concentration within the growth phase of recombinant protein production processes. J Biotechnol 127: 84-94.
    • (2006) J Biotechnol , vol.127 , pp. 84-94
    • Jenzsch, M.1    Gnoth, S.2    Beck, M.3    Kleinschmidt, M.4    Simutis, R.5    Lübbert, A.6
  • 21
    • 60849101844 scopus 로고    scopus 로고
    • Whole-cell bioreduction of aromatic alpha-keto esters using Candida tenuis xylose reductase and Candida boidinii formate dehydrogenase co-expressed in Escherichia coli
    • Kratzer R, Pukl M, Egger S, Nidetzky B. 2008. Whole-cell bioreduction of aromatic alpha-keto esters using Candida tenuis xylose reductase and Candida boidinii formate dehydrogenase co-expressed in Escherichia coli Microb Cell Fac 7: 37.
    • (2008) Microb Cell Fac , vol.7 , pp. 37
    • Kratzer, R.1    Pukl, M.2    Egger, S.3    Nidetzky, B.4
  • 23
    • 79954637488 scopus 로고    scopus 로고
    • Identification, cloning, heterologous expression, and characterization of a NADPH-dependent 7β-hydroxysteroid dehydrogenase from Collinsella aerofaciens
    • Liu L, Aigner A, Schmid RD. 2010. Identification, cloning, heterologous expression, and characterization of a NADPH-dependent 7β-hydroxysteroid dehydrogenase from Collinsella aerofaciens Appl Microbiol Biotechnol 90: 127-135.
    • (2010) Appl Microbiol Biotechnol , vol.90 , pp. 127-135
    • Liu, L.1    Aigner, A.2    Schmid, R.D.3
  • 24
    • 0020398862 scopus 로고
    • Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7 beta-hydroxysteroid dehydrogenase-elaborating Eubacterium aerofaciens strain cocultured with 7 alpha-hydroxysteroid dehydrogenase-elaborating organisms
    • MacDonald IA, Rochon YP, Hutchison DM, Holdeman LV. 1982. Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7 beta-hydroxysteroid dehydrogenase-elaborating Eubacterium aerofaciens strain cocultured with 7 alpha-hydroxysteroid dehydrogenase-elaborating organisms. Appl Environ Microbiol 44: 1187-1195.
    • (1982) Appl Environ Microbiol , vol.44 , pp. 1187-1195
    • MacDonald, I.A.1    Rochon, Y.P.2    Hutchison, D.M.3    Holdeman, L.V.4
  • 25
    • 67549130333 scopus 로고    scopus 로고
    • One-pot multienzymatic synthesis of 12-ketoursodeoxycholic acid: Subtle cofactor specificities rule the reaction equilibria of five biocatalysts working in a row
    • Monti D, Ferrandi EE, Zanellato I, Hua L, Polentini F, Carrea G, Riva S. 2009. One-pot multienzymatic synthesis of 12-ketoursodeoxycholic acid: Subtle cofactor specificities rule the reaction equilibria of five biocatalysts working in a row. Adv Synth Catal 351: 1303-1311.
    • (2009) Adv Synth Catal , vol.351 , pp. 1303-1311
    • Monti, D.1    Ferrandi, E.E.2    Zanellato, I.3    Hua, L.4    Polentini, F.5    Carrea, G.6    Riva, S.7
  • 27
    • 0021112693 scopus 로고
    • Glycerol protection and purification of Bacillus subtilis glucose dehydrogenase
    • Ramaley RF, Vasantha N. 1983. Glycerol protection and purification of Bacillus subtilis glucose dehydrogenase. J Biol Chem 258: 12558-12565.
    • (1983) J Biol Chem , vol.258 , pp. 12558-12565
    • Ramaley, R.F.1    Vasantha, N.2
  • 29
    • 0003162992 scopus 로고
    • Preparation of ursodeoxycholic acid and 3α,7β,12α-trihydroxycholanic acid
    • Samuelsson B. 1960. Preparation of ursodeoxycholic acid and 3α, 7β, 12α-trihydroxycholanic acid. Acta Chem Scand 14: 17-20.
    • (1960) Acta Chem Scand , vol.14 , pp. 17-20
    • Samuelsson, B.1
  • 31
    • 33847087242 scopus 로고
    • Enzyme-catalyzed organic synthesis: NADH regeneration by using formate dehydrogenase
    • Shaked Z, Whitesides GM. 1980. Enzyme-catalyzed organic synthesis: NADH regeneration by using formate dehydrogenase. J Am Chem Soc 102: 7104-7105.
    • (1980) J Am Chem Soc , vol.102 , pp. 7104-7105
    • Shaked, Z.1    Whitesides, G.M.2
  • 32
    • 0016164171 scopus 로고
    • On the 3alpha-hydroxysteroid dehydrogenase from Pseudomonas testosteroni. Purification and properties
    • Skålhegg BA. 1974. On the 3alpha-hydroxysteroid dehydrogenase from Pseudomonas testosteroni. Purification and properties. Eur J Biochem 46: 117-125.
    • (1974) Eur J Biochem , vol.46 , pp. 117-125
    • Skålhegg, B.A.1
  • 33
    • 0016409182 scopus 로고
    • 3alpha-hydroxysteroid dehydrogenase from Pseudomonas testosteroni: Kinetic properties with nad and its thionicotinamide analogue
    • Skålhegg BA. 1975. 3alpha-hydroxysteroid dehydrogenase from Pseudomonas testosteroni: Kinetic properties with nad and its thionicotinamide analogue. Eur J Biochem 50: 603-609.
    • (1975) Eur J Biochem , vol.50 , pp. 603-609
    • Skålhegg, B.A.1
  • 34
    • 0020334336 scopus 로고
    • The enzymic and chemical synthesis of ursodeoxycholic and chenodeoxycholic acid from cholic acid
    • Sutherland JD, Macdonald I, Forrest T. 1982. The enzymic and chemical synthesis of ursodeoxycholic and chenodeoxycholic acid from cholic acid. Prep Biochem Biotechnol 12: 307-321.
    • (1982) Prep Biochem Biotechnol , vol.12 , pp. 307-321
    • Sutherland, J.D.1    Macdonald, I.2    Forrest, T.3
  • 35
    • 4544304906 scopus 로고    scopus 로고
    • A novel NADH-dependent carbonyl reductase from Kluyveromyces aestuarii and comparison of NADH-regeneration system for the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate
    • Yamamoto H, Mitsuhashi K, Kimoto N, Matsuyama A, Esaki N, Kobayashi Y. 2004. A novel NADH-dependent carbonyl reductase from Kluyveromyces aestuarii and comparison of NADH-regeneration system for the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate. Biosci Biotechnol Biochem 68: 638-649.
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 638-649
    • Yamamoto, H.1    Mitsuhashi, K.2    Kimoto, N.3    Matsuyama, A.4    Esaki, N.5    Kobayashi, Y.6
  • 36
    • 0038242206 scopus 로고    scopus 로고
    • Simultaneous synthesis of enantiomerically pure (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine using omega-transaminase/alcohol dehydrogenase/glucose dehydrogenase coupling reaction
    • Yun H, Yang YH, Cho BK, Hwang BY, Kim BG. 2003. Simultaneous synthesis of enantiomerically pure (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine using omega-transaminase/alcohol dehydrogenase/glucose dehydrogenase coupling reaction. Biotechnol Lett 25: 809-814.
    • (2003) Biotechnol Lett , vol.25 , pp. 809-814
    • Yun, H.1    Yang, Y.H.2    Cho, B.K.3    Hwang, B.Y.4    Kim, B.G.5
  • 37
    • 59649110044 scopus 로고    scopus 로고
    • Bioreduction with efficient recycling of NADPH by coupled permeabilized microorganisms
    • Zhang W, O'Connor K, Wang DIC, Li Z. 2009. Bioreduction with efficient recycling of NADPH by coupled permeabilized microorganisms. Appl Environ Microbiol 75: 687-694.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 687-694
    • Zhang, W.1    O'Connor, K.2    Wang, D.I.C.3    Li, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.