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Volumn 108, Issue 6, 2011, Pages 1307-1317

Biocatalytic process optimization based on mechanistic modeling of cholic acid oxidation with cofactor regeneration

Author keywords

Biocatalysis; Cofactor regeneration; Hydroxysteroid dehydrogenase; In silico optimization; Mechanistic model; Process modelling

Indexed keywords

BIOCATALYSIS; COFACTOR REGENERATION; HYDROXYSTEROID DEHYDROGENASE; IN-SILICO; MECHANISTIC MODELS; PROCESS MODELLING;

EID: 79954593169     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.23047     Document Type: Article
Times cited : (23)

References (30)
  • 1
    • 13244252072 scopus 로고    scopus 로고
    • Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA.
    • Bisswanger H. 2002. Enzyme kinetics. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 193 p.
    • (2002) Enzyme kinetics , pp. 193
    • Bisswanger, H.1
  • 2
    • 0026033216 scopus 로고
    • 12 alpha-Hydroxysteroid dehydrogenase from Clostridium group P, strain C 48-50 production, purification and characterization
    • Braun M, Lünsdorf H, Bückmann AF. 1991. 12 alpha-Hydroxysteroid dehydrogenase from Clostridium group P, strain C 48-50 production, purification and characterization. Eur J Biochem/FEBS 196:439-450.
    • (1991) Eur J Biochem/FEBS , vol.196 , pp. 439-450
    • Braun, M.1    Lünsdorf, H.2    Bückmann, A.F.3
  • 3
    • 33745230163 scopus 로고    scopus 로고
    • Incremental identification of kinetic models for homogeneous reaction systems
    • Brendel M, Bonvin D, Marquardt W. 2006. Incremental identification of kinetic models for homogeneous reaction systems. Chem Eng Sci 61:5404-5420.
    • (2006) Chem Eng Sci , vol.61 , pp. 5404-5420
    • Brendel, M.1    Bonvin, D.2    Marquardt, W.3
  • 4
    • 0021423717 scopus 로고
    • Enzymatic preparation of 12-ketochenodeoxycholic acid with NADP regeneration
    • Carrea G, Bovara R, Cremonesi P, Lodi R. 1984. Enzymatic preparation of 12-ketochenodeoxycholic acid with NADP regeneration. Biotechnol Bioeng 26:560-563.
    • (1984) Biotechnol Bioeng , vol.26 , pp. 560-563
    • Carrea, G.1    Bovara, R.2    Cremonesi, P.3    Lodi, R.4
  • 5
    • 0022240850 scopus 로고
    • Preparation of 12-ketochenodeoxycholic acid from cholic acid using coimmobilized 12α-hydroxysteroid dehydrogenase and glutamate dehydrogenase with NADP+ cycling at high efficiency
    • Carrea G, Bovara R, Longhi R, Riva S. 1985. Preparation of 12-ketochenodeoxycholic acid from cholic acid using coimmobilized 12α-hydroxysteroid dehydrogenase and glutamate dehydrogenase with NADP+ cycling at high efficiency. Enzyme Microb Technol 7:597-600.
    • (1985) Enzyme Microb Technol , vol.7 , pp. 597-600
    • Carrea, G.1    Bovara, R.2    Longhi, R.3    Riva, S.4
  • 6
    • 34248174364 scopus 로고    scopus 로고
    • Modelling and optimisation of a transketolase-mediated carbon-carbon bond formation reaction
    • Chen B, Baganz F, Woodley J. 2007. Modelling and optimisation of a transketolase-mediated carbon-carbon bond formation reaction. Chem Eng Sci 62:3178-3184.
    • (2007) Chem Eng Sci , vol.62 , pp. 3178-3184
    • Chen, B.1    Baganz, F.2    Woodley, J.3
  • 7
    • 0034841038 scopus 로고    scopus 로고
    • Quantitative analysis of the time courses of enzyme-catalyzed reactions
    • Duggleby RG. 2001. Quantitative analysis of the time courses of enzyme-catalyzed reactions. Methods 24:168-174.
    • (2001) Methods , vol.24 , pp. 168-174
    • Duggleby, R.G.1
  • 8
    • 2442646281 scopus 로고    scopus 로고
    • Use of an ionic liquid in a two-phase system to improve an alcohol dehydrogenase catalysed reduction
    • Eckstein M, Villela Filho 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 (Cambridge, England) (9): 1084-1085.
    • (2004) Chem Commun (Cambridge, England) , Issue.9 , pp. 1084-1085
    • Eckstein, M.1    Villela Filho, M.2    Liese, A.3    Kragl, U.4
  • 9
    • 0027625031 scopus 로고
    • Kinetic models for synthesis by a thermophilic alcohol dehydrogenase
    • Ford JB, Askins KJ, Taylor KB. 1993. Kinetic models for synthesis by a thermophilic alcohol dehydrogenase. Biotechnol Bioeng 42:367-375.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 367-375
    • Ford, J.B.1    Askins, K.J.2    Taylor, K.B.3
  • 10
    • 33646025554 scopus 로고    scopus 로고
    • Exploitation of the alcohol dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid
    • Fossati E, Polentini F, Carrea G, Riva S. 2006. Exploitation of the alcohol dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid. Biotechnol Bioeng 93:1216-1220.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 1216-1220
    • Fossati, E.1    Polentini, F.2    Carrea, G.3    Riva, S.4
  • 11
    • 0018277495 scopus 로고
    • Partial purification and characterization of NADP-dependent 12alpha-hydroxysteroid dehydrogenase from Clostridium leptum
    • Harris JN, Hylemon PB. 1978. Partial purification and characterization of NADP-dependent 12alpha-hydroxysteroid dehydrogenase from Clostridium leptum. Biochim Biophys Acta 528:148-157.
    • (1978) Biochim Biophys Acta , vol.528 , pp. 148-157
    • Harris, J.N.1    Hylemon, P.B.2
  • 12
    • 0033485581 scopus 로고    scopus 로고
    • Large-scale applications of NAD(P)-dependent oxidoreductases: Recent developments
    • Hummel W. 1999. Large-scale applications of NAD(P)-dependent oxidoreductases: Recent developments. Trends Biotechnol 17:487-492.
    • (1999) Trends Biotechnol , vol.17 , pp. 487-492
    • Hummel, W.1
  • 13
    • 0019864171 scopus 로고
    • Cholesterol gallstone dissolution in bile: Dissolution kinetics of crystalline (anhydrate and monohydrate) cholesterol with chenodeoxycholate, ursodeoxycholate, and their glycine and taurine conjugates
    • Igimi H, Carey MC. 1981. Cholesterol gallstone dissolution in bile: Dissolution kinetics of crystalline (anhydrate and monohydrate) cholesterol with chenodeoxycholate, ursodeoxycholate, and their glycine and taurine conjugates. J Lipid Res 22:254-270.
    • (1981) J Lipid Res , vol.22 , pp. 254-270
    • Igimi, H.1    Carey, M.C.2
  • 14
    • 0032763588 scopus 로고    scopus 로고
    • Design of immobilized enzyme reactors for the continuous production of fructose syrup from whey permeate
    • Illanes A, Wilson L, Raiman L. 1999. Design of immobilized enzyme reactors for the continuous production of fructose syrup from whey permeate. Bioprocess Eng 21:0509.
    • (1999) Bioprocess Eng , vol.21 , pp. 0509
    • Illanes, A.1    Wilson, L.2    Raiman, L.3
  • 15
    • 0037442854 scopus 로고    scopus 로고
    • Thermodynamics of the reduction of NADP with 2-propanol catalyzed by an NADP-dependent alcohol dehydrogenase
    • King MT. 2003. Thermodynamics of the reduction of NADP with 2-propanol catalyzed by an NADP-dependent alcohol dehydrogenase. Arch Biochem Biophys 410:280-286.
    • (2003) Arch Biochem Biophys , vol.410 , pp. 280-286
    • King, M.T.1
  • 16
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King EL, Altman C. 1956. A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J Phys Chem 60:1375-1378.
    • (1956) J Phys Chem , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 17
    • 1942439106 scopus 로고    scopus 로고
    • Biocatalytic oxidation of primary and secondary alcohols
    • Kroutil W, Mang H, Edegger K, Faber K. 2004. Biocatalytic oxidation of primary and secondary alcohols. Adv Synth Catal 346:125-142.
    • (2004) Adv Synth Catal , vol.346 , pp. 125-142
    • Kroutil, W.1    Mang, H.2    Edegger, K.3    Faber, K.4
  • 18
    • 0017102437 scopus 로고
    • 3alpha-, 7alpha- and 12alpha-Hydroxysteroid dehydrogenase activities from Clostridium perfringens
    • Macdonald IA, Meier EC, Mahony DE, Costain GA. 1976. 3alpha-, 7alpha- and 12alpha-Hydroxysteroid dehydrogenase activities from Clostridium perfringens. Biochim Biophys Acta 450:142-153.
    • (1976) Biochim Biophys Acta , vol.450 , pp. 142-153
    • Macdonald, I.A.1    Meier, E.C.2    Mahony, D.E.3    Costain, G.A.4
  • 19
    • 0018763451 scopus 로고
    • Bile salt 3 alpha- and 12 alpha-hydroxysteroid dehydrogenases from Eubacterium lentum and related organisms
    • Macdonald IA, Jellett JF, Mahony DE, Holdeman LV. 1979. Bile salt 3 alpha- and 12 alpha-hydroxysteroid dehydrogenases from Eubacterium lentum and related organisms. Appl Environ Microbiol 37:992-1000.
    • (1979) Appl Environ Microbiol , vol.37 , pp. 992-1000
    • Macdonald, I.A.1    Jellett, J.F.2    Mahony, D.E.3    Holdeman, L.V.4
  • 20
    • 0018438183 scopus 로고
    • 12alpha-Hydroxysteroid dehydrogenase from Clostridium group P strain 48-50 ATCC No. 29733: Partial purification and characterization
    • Macdonald IA, Jellett JF, Mahony DE. 1979. 12alpha-Hydroxysteroid dehydrogenase from Clostridium group P strain 48-50 ATCC No. 29733: Partial purification and characterization. J Lipid Res 20:234-239.
    • (1979) J Lipid Res , vol.20 , pp. 234-239
    • Macdonald, I.A.1    Jellett, J.F.2    Mahony, D.E.3
  • 23
    • 34147155935 scopus 로고    scopus 로고
    • Development of a fed-batch process for the production of the cytochrome P450 monooxygenase CYP102A1 from Bacillus megaterium in E. coli
    • Pflug S, Richter SM, Urlacher VB. 2007. Development of a fed-batch process for the production of the cytochrome P450 monooxygenase CYP102A1 from Bacillus megaterium in E. coli. J Biotech 129(3): 481-488.
    • (2007) J Biotech , vol.129 , Issue.3 , pp. 481-488
    • Pflug, S.1    Richter, S.M.2    Urlacher, V.B.3
  • 24
    • 33244467651 scopus 로고    scopus 로고
    • Bile salt biotransformations by human intestinal bacteria
    • Ridlon JM, Kang D, Hylemon PB. 2006. Bile salt biotransformations by human intestinal bacteria. J Lipid Res 47:241-259.
    • (2006) J Lipid Res , vol.47 , pp. 241-259
    • Ridlon, J.M.1    Kang, D.2    Hylemon, P.B.3
  • 25
    • 0020566692 scopus 로고
    • A bioluminescent assay for 12-alpha-hydroxy bile acids using immobilized enzymes
    • Schoelmerich J, Hinkley J, Macdonald I, Hofmann A, Deluca M. 1983. A bioluminescent assay for 12-alpha-hydroxy bile acids using immobilized enzymes. Anal Biochem 133:244-250.
    • (1983) Anal Biochem , vol.133 , pp. 244-250
    • Schoelmerich, J.1    Hinkley, J.2    Macdonald, I.3    Hofmann, A.4    Deluca, M.5
  • 26
    • 73249131640 scopus 로고    scopus 로고
    • Application of modeling and simulation tools for the evaluation of biocatalytic processes: A future perspective
    • Sin G, Woodley JM, Gernaey KV. 2009. Application of modeling and simulation tools for the evaluation of biocatalytic processes: A future perspective. Biotechnol Progr 25:1529-1538.
    • (2009) Biotechnol Progr , vol.25 , pp. 1529-1538
    • Sin, G.1    Woodley, J.M.2    Gernaey, K.V.3
  • 27
    • 0030571276 scopus 로고    scopus 로고
    • New constraints between kinetic parameters explain the (Un)identifiability of enzymatic rate constants
    • Straathof AJ, Heijnen JJ. 1996. New constraints between kinetic parameters explain the (Un)identifiability of enzymatic rate constants. Biotechnol Bioeng 52:433-437.
    • (1996) Biotechnol Bioeng , vol.52 , pp. 433-437
    • Straathof, A.J.1    Heijnen, J.J.2
  • 28
    • 0020334336 scopus 로고
    • The enzymic and chemical synthesis of ursodeoxycholic and chenodeoxycholic acid from cholic acid
    • Sutherland JD, Macdonald IA, Forrest TP. 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.A.2    Forrest, T.P.3
  • 29
    • 0042933788 scopus 로고    scopus 로고
    • Recent developments in pyridine nucleotide regeneration
    • van der Donk WA, Zhao H. 2003. Recent developments in pyridine nucleotide regeneration. Curr Opin Biotechnol 14:421-426.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 421-426
    • van der Donk, W.A.1    Zhao, H.2
  • 30
    • 0035809226 scopus 로고    scopus 로고
    • Development of a process model to describe the synthesis of (R)-mandelonitrile by Prunus amygdalus hydroxynitrile lyase in an aqueous-organic biphasic reactor
    • Willeman WF, Gerrits PJ, Hanefeld U, Brussee J, Straathof AJ, van der Gen A, Heijnen JJ. 2002. Development of a process model to describe the synthesis of (R)-mandelonitrile by Prunus amygdalus hydroxynitrile lyase in an aqueous-organic biphasic reactor. Biotechnol Bioeng 77:239-247.
    • (2002) Biotechnol Bioeng , vol.77 , pp. 239-247
    • Willeman, W.F.1    Gerrits, P.J.2    Hanefeld, U.3    Brussee, J.4    Straathof, A.J.5    van der Gen, A.6    Heijnen, J.J.7


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