메뉴 건너뛰기




Volumn 152, Issue 3, 2011, Pages 87-92

Influence of reaction conditions on the enantioselectivity of biocatalyzed C-C bond formations under high pressure conditions

Author keywords

Benzoylformate decarboxylase; C C bond formation; Enantioselectivity; Enzymatic catalysis; High pressure catalysis; PH

Indexed keywords

ALKALINE CONDITIONS; ATMOSPHERIC CONDITIONS; C-C BOND FORMATION; DECARBOXYLASES; ENZYMATIC CATALYSIS; HIGH HYDROSTATIC PRESSURE; HIGH PRESSURE CATALYSIS; HIGH-PRESSURE CONDITION; PH VALUE; REACTION CONDITIONS; THIAMINE DIPHOSPHATES;

EID: 79952899156     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.01.020     Document Type: Article
Times cited : (20)

References (52)
  • 1
    • 21344491096 scopus 로고
    • Effects of high pressure on proteins
    • Balny C., Masson P. Effects of high pressure on proteins. Food Rev. Int. 1993, 9:611-628.
    • (1993) Food Rev. Int. , vol.9 , pp. 611-628
    • Balny, C.1    Masson, P.2
  • 2
    • 79952899186 scopus 로고    scopus 로고
    • High pressure enzyme kinetics
    • Springer Verlag, Berlin/Heidelberg, H. Ludwig (Ed.)
    • Balny C. High pressure enzyme kinetics. Advances in High Pressure Bioscience and Biotechnology 1998, 413-416. Springer Verlag, Berlin/Heidelberg. H. Ludwig (Ed.).
    • (1998) Advances in High Pressure Bioscience and Biotechnology , pp. 413-416
    • Balny, C.1
  • 4
    • 77951549438 scopus 로고    scopus 로고
    • Influence of the hydrostatic pressure and pH on the asymmetric 2-hydroxyketone formation catalyzed by Pseudomonas putida benzoylformate decarboxylase and variants thereof
    • Berheide M., Peper S., Kara S., Long W.S., Schenkel S., Pohl M., Niemeyer B., Liese A. Influence of the hydrostatic pressure and pH on the asymmetric 2-hydroxyketone formation catalyzed by Pseudomonas putida benzoylformate decarboxylase and variants thereof. Biotechnol. Bioeng. 2010, 106(1):18-26.
    • (2010) Biotechnol. Bioeng. , vol.106 , Issue.1 , pp. 18-26
    • Berheide, M.1    Peper, S.2    Kara, S.3    Long, W.S.4    Schenkel, S.5    Pohl, M.6    Niemeyer, B.7    Liese, A.8
  • 5
    • 0037171151 scopus 로고    scopus 로고
    • Pressure effects on intra- and intermolecular interactions within proteins
    • Boonyaratanakornkit B.B., Park C.B., Clark D.S. Pressure effects on intra- and intermolecular interactions within proteins. Biochim. Biophys. Acta 2002, 1595:235-249.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 235-249
    • Boonyaratanakornkit, B.B.1    Park, C.B.2    Clark, D.S.3
  • 6
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0037947252 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure and additives on the dynamics of water: a raman spectroscopy study
    • Cavaille D., Combes D. Effect of high hydrostatic pressure and additives on the dynamics of water: a raman spectroscopy study. J. Raman Spectrosc. 1996, 27:853-857.
    • (1996) J. Raman Spectrosc. , vol.27 , pp. 853-857
    • Cavaille, D.1    Combes, D.2
  • 8
    • 38949172001 scopus 로고    scopus 로고
    • Enantiomer selective acylation of racemic alcohols by lipases in continuous-flow bioreactors
    • Csajági C., Szatzker G., Töke E.R., Ürge L., Darvas F., Poppe L. Enantiomer selective acylation of racemic alcohols by lipases in continuous-flow bioreactors. Tetrahedron: Asymmetry 2008, 19:237-246.
    • (2008) Tetrahedron: Asymmetry , vol.19 , pp. 237-246
    • Csajági, C.1    Szatzker, G.2    Töke, E.R.3    Ürge, L.4    Darvas, F.5    Poppe, L.6
  • 10
    • 0037120881 scopus 로고    scopus 로고
    • Development of a donor-acceptor concept for enzymatic cross-coupling reactions of aldehydes: the first asymmetric cross-benzoin condensation
    • Dünkelmann P., Kolter-Jung D., Nitsche A., Demir A.S., Siegert P., Lingen B., Baumann M., Pohl M., Müller M. Development of a donor-acceptor concept for enzymatic cross-coupling reactions of aldehydes: the first asymmetric cross-benzoin condensation. J. Am. Chem. Soc. 2002, 124(41):12084-12085.
    • (2002) J. Am. Chem. Soc. , vol.124 , Issue.41 , pp. 12084-12085
    • Dünkelmann, P.1    Kolter-Jung, D.2    Nitsche, A.3    Demir, A.S.4    Siegert, P.5    Lingen, B.6    Baumann, M.7    Pohl, M.8    Müller, M.9
  • 11
    • 0034123380 scopus 로고    scopus 로고
    • Enantioselective synthesis of (S)-2-hydroxypropanone derivatives by benzoylformate decarboxylase catalyzed C-C bond formation
    • Dünnwald T., Demir A.S., Siegert P., Pohl M., Müller M. Enantioselective synthesis of (S)-2-hydroxypropanone derivatives by benzoylformate decarboxylase catalyzed C-C bond formation. Eur. J. Org. Chem. 2000, 2161-2170.
    • (2000) Eur. J. Org. Chem. , pp. 2161-2170
    • Dünnwald, T.1    Demir, A.S.2    Siegert, P.3    Pohl, M.4    Müller, M.5
  • 13
    • 0028220701 scopus 로고
    • Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross M., Jaenicke R. Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 1994, 221:617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 14
    • 0010344352 scopus 로고
    • The enzymatic conversion of mandelic acid to benzoic acid
    • Gunsalus I.C., Gunsalus F.C., Stanier R.Y. The enzymatic conversion of mandelic acid to benzoic acid. J. Bacteriol. 1953, 66:538-542.
    • (1953) J. Bacteriol. , vol.66 , pp. 538-542
    • Gunsalus, I.C.1    Gunsalus, F.C.2    Stanier, R.Y.3
  • 16
    • 0013892193 scopus 로고
    • Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida II Isolation and properties of blocked mutants
    • Hegeman G.D. Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida II Isolation and properties of blocked mutants. J. Bacteriol. 1966, 91:1155-1160.
    • (1966) J. Bacteriol. , vol.91 , pp. 1155-1160
    • Hegeman, G.D.1
  • 17
    • 0001792869 scopus 로고
    • From living systems to biomolecules
    • Montrouge, John Libbey Eurotext Ltd.
    • Heremans K. From living systems to biomolecules. High Pressure and Biotechnology 1992, 224:37-44. Montrouge, John Libbey Eurotext Ltd.
    • (1992) High Pressure and Biotechnology , vol.224 , pp. 37-44
    • Heremans, K.1
  • 18
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans K., Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta 1998, 1386:353-370.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 21
    • 3543076929 scopus 로고    scopus 로고
    • White is the hype-biocatalysts on the move
    • Jaeger K.-E., Eggert T. White is the hype-biocatalysts on the move. Curr. Opin. Biotechnol. 2004, 15:305-313.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 305-313
    • Jaeger, K.-E.1    Eggert, T.2
  • 22
    • 11144336544 scopus 로고    scopus 로고
    • Automated high-pressure plant for a continuous flow through a fixed bed-investigation of hydrodynamic behaviour
    • Jansen J., Niemeyer B. Automated high-pressure plant for a continuous flow through a fixed bed-investigation of hydrodynamic behaviour. J. Supercrit. Fluids 2005, 33:285-293.
    • (2005) J. Supercrit. Fluids , vol.33 , pp. 285-293
    • Jansen, J.1    Niemeyer, B.2
  • 23
    • 0037391206 scopus 로고    scopus 로고
    • Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions
    • Jordan F. Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions. Nat. Prod. Rep. 2003, 20:184-201.
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 184-201
    • Jordan, F.1
  • 24
    • 0034813459 scopus 로고    scopus 로고
    • A model of the pressure dependence of the enantioselectivity ofCandida rugosa lipase towards (±)-menthol
    • Kahlow U.H.M., Schmid R.D., Pleiss J. A model of the pressure dependence of the enantioselectivity ofCandida rugosa lipase towards (±)-menthol. Protein Sci. 2001, 10:1942-1952.
    • (2001) Protein Sci. , vol.10 , pp. 1942-1952
    • Kahlow, U.H.M.1    Schmid, R.D.2    Pleiss, J.3
  • 26
    • 33845395939 scopus 로고    scopus 로고
    • Factors mediating activity, selectivity, and substrate specificity for the thiamin diphosphate-dependent enzymes benzaldehyde lyase and benzoylformate decarboxylase
    • Knoll M., Müller M., Pleiss J., Pohl M. Factors mediating activity, selectivity, and substrate specificity for the thiamin diphosphate-dependent enzymes benzaldehyde lyase and benzoylformate decarboxylase. Chembiochem 2006, 7:1928-1934.
    • (2006) Chembiochem , vol.7 , pp. 1928-1934
    • Knoll, M.1    Müller, M.2    Pleiss, J.3    Pohl, M.4
  • 27
    • 33646014759 scopus 로고    scopus 로고
    • High pressure application for food biopolymers
    • Knorr D., Heinz V., Buckow R. High pressure application for food biopolymers. Biochim. Biophys. Acta 2006, 1764:619-631.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 619-631
    • Knorr, D.1    Heinz, V.2    Buckow, R.3
  • 30
    • 0036656222 scopus 로고    scopus 로고
    • Improving the carboligase activity of benzoylformate decarboxylase from pseudomonas putida by a combination of directed evolution and site-directed evolution
    • Lingen B., Grötzinger J., Kolter D., Kula M.-R., Pohl M. Improving the carboligase activity of benzoylformate decarboxylase from pseudomonas putida by a combination of directed evolution and site-directed evolution. Protein Eng. 2002, 15(7):585-593.
    • (2002) Protein Eng. , vol.15 , Issue.7 , pp. 585-593
    • Lingen, B.1    Grötzinger, J.2    Kolter, D.3    Kula, M.-R.4    Pohl, M.5
  • 31
    • 0037898048 scopus 로고    scopus 로고
    • Effects of high pressure on enzymes related to food quality
    • Kluwer Academic/Plenum Publisher, New York, M.E.G. Hendrickx, D. Knorr (Eds.)
    • Ludikhuyze L., Van Loey A., Indrawati, Denys S., Hendrickx M.E.G. Effects of high pressure on enzymes related to food quality. Ultra High Pressure Treatments of Foods 2002, 115-166. Kluwer Academic/Plenum Publisher, New York. M.E.G. Hendrickx, D. Knorr (Eds.).
    • (2002) Ultra High Pressure Treatments of Foods , pp. 115-166
    • Ludikhuyze, L.1    Van Loey, A.2    Indrawati3    Denys, S.4    Hendrickx, M.E.G.5
  • 32
    • 84953649642 scopus 로고
    • Ion product of water substance, 0-1000°C, 1-10,000 Bars new international formulation and its background
    • Marshall W.L., Franck E.U. Ion product of water substance, 0-1000°C, 1-10,000 Bars new international formulation and its background. J. Phys. Chem. Ref. Data. 1981, 10:295-304.
    • (1981) J. Phys. Chem. Ref. Data. , vol.10 , pp. 295-304
    • Marshall, W.L.1    Franck, E.U.2
  • 33
    • 0035914510 scopus 로고    scopus 로고
    • Control on enantioselectivity with pressure for lipase-catalyzed esterification in supercritical carbon dioxide
    • Matsuda T., Kanamaru R., Watanabe K., Harada T., Nakamura K. Control on enantioselectivity with pressure for lipase-catalyzed esterification in supercritical carbon dioxide. Tetrahedron Lett. 2001, 42:8319-8321.
    • (2001) Tetrahedron Lett. , vol.42 , pp. 8319-8321
    • Matsuda, T.1    Kanamaru, R.2    Watanabe, K.3    Harada, T.4    Nakamura, K.5
  • 34
    • 0038645392 scopus 로고    scopus 로고
    • Control of enantioselectivity of lipase catalyzed esterification in supercritical carbon dioxide by tuning the pressure and temperature
    • Matsuda T., Kanamaru R., Watanabe K., Kamitanaka T., Harada T., Nakamura K. Control of enantioselectivity of lipase catalyzed esterification in supercritical carbon dioxide by tuning the pressure and temperature. Tetrahedron: Asymmetry 2003, 14:2087-2091.
    • (2003) Tetrahedron: Asymmetry , vol.14 , pp. 2087-2091
    • Matsuda, T.1    Kanamaru, R.2    Watanabe, K.3    Kamitanaka, T.4    Harada, T.5    Nakamura, K.6
  • 35
    • 14344252375 scopus 로고    scopus 로고
    • Asymmetric synthesis using hydrolytic enzymes in supercritical carbon dioxide
    • Matsuda T., Harada T., Nakamura K., Ikariya T. Asymmetric synthesis using hydrolytic enzymes in supercritical carbon dioxide. Tetrahedron:Asymmetry 2005, 16:909-915.
    • (2005) Tetrahedron:Asymmetry , vol.16 , pp. 909-915
    • Matsuda, T.1    Harada, T.2    Nakamura, K.3    Ikariya, T.4
  • 37
    • 33749060930 scopus 로고    scopus 로고
    • Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions
    • Meersman F., Dobson C.M., Heremans K. Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions. Chem. Soc. Rev. 2006, 38(10):908-917.
    • (2006) Chem. Soc. Rev. , vol.38 , Issue.10 , pp. 908-917
    • Meersman, F.1    Dobson, C.M.2    Heremans, K.3
  • 38
    • 0017377899 scopus 로고
    • Pressure variation of enzymatic reaction rates: yeast and liver alcohol dehydrogenase
    • Morild E. Pressure variation of enzymatic reaction rates: yeast and liver alcohol dehydrogenase. Biophys. Chem. 1977, 6:351-362.
    • (1977) Biophys. Chem. , vol.6 , pp. 351-362
    • Morild, E.1
  • 39
    • 10144249599 scopus 로고    scopus 로고
    • Application of high hydrostatic pressure for increasing activity and stability of enzymes
    • Mozhaev V.V., Lange R., Kudryashova E.V., Balny C. Application of high hydrostatic pressure for increasing activity and stability of enzymes. Biotechnol. Bioeng. 1996, 52:320-331.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 320-331
    • Mozhaev, V.V.1    Lange, R.2    Kudryashova, E.V.3    Balny, C.4
  • 40
    • 0000748473 scopus 로고
    • Pressure dependence of weak acid ionization in aqueous buffers
    • Neumann R.C., Kauzmann W., Zipp A. Pressure dependence of weak acid ionization in aqueous buffers. J. Phys. Chem. 1973, 77:2687-2691.
    • (1973) J. Phys. Chem. , vol.77 , pp. 2687-2691
    • Neumann, R.C.1    Kauzmann, W.2    Zipp, A.3
  • 41
    • 33750686033 scopus 로고    scopus 로고
    • An innovative approach for sorptive separation of amphiphilic biomolecules applying high hydrostatic pressure
    • Niemeyer B., Jansen J. An innovative approach for sorptive separation of amphiphilic biomolecules applying high hydrostatic pressure. J. Supercrit. Fluids 2007, 39:354-361.
    • (2007) J. Supercrit. Fluids , vol.39 , pp. 354-361
    • Niemeyer, B.1    Jansen, J.2
  • 42
    • 0037171123 scopus 로고    scopus 로고
    • Effects of high pressure on enzymatic activity
    • Northrop D.B. Effects of high pressure on enzymatic activity. Biochim. Biophys Acta 2002, 1595:71-79.
    • (2002) Biochim. Biophys Acta , vol.1595 , pp. 71-79
    • Northrop, D.B.1
  • 43
    • 0042628455 scopus 로고    scopus 로고
    • Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric CC bond formation
    • Pohl M., Lingen B., Müller M. Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric CC bond formation. Chem. Eur. J. 2002, 8:5289-5295.
    • (2002) Chem. Eur. J. , vol.8 , pp. 5289-5295
    • Pohl, M.1    Lingen, B.2    Müller, M.3
  • 44
    • 39649112971 scopus 로고    scopus 로고
    • Industrial processes using lyases for C-C, C-N, and C-O bond formation
    • CRC Press Taylor & Francis Group, Florida, R.N. Patel (Ed.)
    • Pohl M., Liese A. Industrial processes using lyases for C-C, C-N, and C-O bond formation. Biocatalysis in the Pharmaceutical and Biotechnology Industries 2007, 661-676. CRC Press Taylor & Francis Group, Florida. R.N. Patel (Ed.).
    • (2007) Biocatalysis in the Pharmaceutical and Biotechnology Industries , pp. 661-676
    • Pohl, M.1    Liese, A.2
  • 46
    • 33748556286 scopus 로고    scopus 로고
    • Spectroscopic pH measurement for high temperatures, pressures and ionic strength
    • Raghuraman B., Gustavson G., Mullins O.C., Rabbito P. Spectroscopic pH measurement for high temperatures, pressures and ionic strength. AIChE J. 2006, 52:3257-3265.
    • (2006) AIChE J. , vol.52 , pp. 3257-3265
    • Raghuraman, B.1    Gustavson, G.2    Mullins, O.C.3    Rabbito, P.4
  • 47
    • 25844473249 scopus 로고    scopus 로고
    • Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida
    • Siegert P., McLeish M.J., Baumann M., Iding H., Kneen M.M., Kenyon G.L., Pohl M. Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida. Protein Eng. Des. Sel. 2005, 18(7):345-357.
    • (2005) Protein Eng. Des. Sel. , vol.18 , Issue.7 , pp. 345-357
    • Siegert, P.1    McLeish, M.J.2    Baumann, M.3    Iding, H.4    Kneen, M.M.5    Kenyon, G.L.6    Pohl, M.7
  • 48
    • 21144455026 scopus 로고    scopus 로고
    • Enantioselective C-C bond synthesis catalysed by enzymes
    • Sukumaran J., Hanefeld U. Enantioselective C-C bond synthesis catalysed by enzymes. Chem. Soc. Rev. 2005, 34:530-542.
    • (2005) Chem. Soc. Rev. , vol.34 , pp. 530-542
    • Sukumaran, J.1    Hanefeld, U.2
  • 50
    • 0026848784 scopus 로고
    • Factors affecting 2-hydroxypropiophenone formation by benzoylformate decarboxylase from Pseudomonas putida
    • Wilcocks R., Ward O.P. Factors affecting 2-hydroxypropiophenone formation by benzoylformate decarboxylase from Pseudomonas putida. Biotechnol. Bioeng. 1991, 39:1058-1062.
    • (1991) Biotechnol. Bioeng. , vol.39 , pp. 1058-1062
    • Wilcocks, R.1    Ward, O.P.2
  • 52
    • 0032879602 scopus 로고    scopus 로고
    • Enantioselectivity by altering alcohol concentration for esterification in supercritical CO2
    • Wu J., Liang M.-T. Enantioselectivity by altering alcohol concentration for esterification in supercritical CO2. J. Chem. Eng. JPN 1999, 32(3):338-340.
    • (1999) J. Chem. Eng. JPN , vol.32 , Issue.3 , pp. 338-340
    • Wu, J.1    Liang, M.-T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.