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Volumn 46, Issue 12, 2011, Pages 2347-2352

The kinetic behavior of dehydrogenase enzymes in solution and immobilized onto nanostructured carbon platforms

Author keywords

Alcohol dehydrogenase; Aldehyde dehydrogenase; Enzyme immobilization; PAMAM

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; CATALYST CONSUMPTION; ENZYMATIC ACTIVITIES; IMMOBILIZATION PROCESS; INFLUENCE OF PH; KINETIC BEHAVIOR; KINETIC CONSTANT; LAYER-BY-LAYERS; LITERATURE DATA; NANOSTRUCTURED CARBONS; PAMAM; PAMAM DENDRIMER; PHYSIOLOGICAL CONDITION; POLYAMIDOAMINE DENDRIMERS; STORAGE TIME;

EID: 80055003733     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.09.019     Document Type: Article
Times cited : (33)

References (31)
  • 1
    • 0040794548 scopus 로고    scopus 로고
    • Structure and function of yeast alcohol dehydrogenase
    • S. Trivic, and V. Leskovac Structure and function of yeast alcohol dehydrogenase J Serb Chem Soc 65 2000 207 227
    • (2000) J Serb Chem Soc , vol.65 , pp. 207-227
    • Trivic, S.1    Leskovac, V.2
  • 2
    • 33947466615 scopus 로고
    • Yeast alcohol dehydrogenase. III. Relation of alcohol structure to activity
    • J.V. Eys, and N.O. Kaplan Yeast alcohol dehydrogenase. III. Relation of alcohol structure to activity J Am Chem Soc 79 1957 2782 2786
    • (1957) J Am Chem Soc , vol.79 , pp. 2782-2786
    • Eys, J.V.1    Kaplan, N.O.2
  • 3
    • 0023654330 scopus 로고
    • Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity
    • A.J. Ganzhorn, D.W. Green, A.D. Hershey, R.M. Gould, and B.V. Plapp Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity J Biol Chem 262 1987 3754 3761
    • (1987) J Biol Chem , vol.262 , pp. 3754-3761
    • Ganzhorn, A.J.1    Green, D.W.2    Hershey, A.D.3    Gould, R.M.4    Plapp, B.V.5
  • 4
    • 0015577980 scopus 로고
    • A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates
    • F.M. Dickinson, and G.P. Monger A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates Biochem J 131 1973 261 270
    • (1973) Biochem J , vol.131 , pp. 261-270
    • Dickinson, F.M.1    Monger, G.P.2
  • 5
    • 0017809171 scopus 로고
    • Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases
    • C.J. Dickenson, and F.M. Dickinson Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases Biochem J 171 1978 613 627 (Pubitemid 8348735)
    • (1978) Biochemical Journal , vol.171 , Issue.3 , pp. 613-627
    • Dickenson, C.J.1    Dickinson, F.M.2
  • 6
    • 0017886724 scopus 로고
    • Estimation of rate and dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase
    • F.M. Dickinson, and C.J. Dickenson Estimation of rate dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase Biochem J 171 1978 629 637 (Pubitemid 8348736)
    • (1978) Biochemical Journal , vol.171 , Issue.3 , pp. 629-637
    • Dickinson, F.M.1    Dickenson, C.J.2
  • 8
    • 0015239352 scopus 로고
    • Ordered binding of substrates to yeast aldehyde dehydrogenase
    • S.L. Bradbury, and W.B. Jakoby Ordered binding of substrates to yeast aldehyde dehydrogenase J Biol Chem 246 1971 1834 1840
    • (1971) J Biol Chem , vol.246 , pp. 1834-1840
    • Bradbury, S.L.1    Jakoby, W.B.2
  • 9
    • 0003049606 scopus 로고
    • Immobilized enzymes
    • T. Nagodawithana, G. Reed, Academic Press New York
    • P. Adlercreutz Immobilized enzymes T. Nagodawithana, G. Reed, 3rd enzymes in food processing 1993 Academic Press New York 103 119
    • (1993) 3rd Enzymes in Food Processing , pp. 103-119
    • Adlercreutz, P.1
  • 10
    • 0025373701 scopus 로고
    • Starbust dendrimers: Molecular-level control of size, shape, surface chemistry, topology, and flexibility from atoms to macroscopic matter
    • D.A. Tomalia, A.M. Naylor, W.A. Goddard III, and Starburst Dendrimers: Molecular-level control of size, shape, surface chemistry, topology, and flexibility from atoms to macroscopic matter Angew Chem Int Ed Engl 29 1990 138 175 (Pubitemid 20142204)
    • (1990) Angewandte Chemie - International Edition in English , vol.29 , Issue.2 , pp. 138-175
    • Tomalia, D.A.1    Naylor, A.M.2    Goddard III, W.A.3
  • 11
    • 52149087979 scopus 로고    scopus 로고
    • Dendrimer-assisted immobilization of alcohol dehydrogenase in nanostructured films for biosensing: Ethanol detection using electrical capacitance measurements
    • A.C. Perinotto, L. Caseli, C.O. Hayasaka, A. Riul Jr. , O.N. Oliveira Jr. , and V. Zucolotto Dendrimer-assisted immobilization of alcohol dehydrogenase in nanostructured films for biosensing: ethanol detection using electrical capacitance measurements Thin Solid Films 516 2008 9002 9005
    • (2008) Thin Solid Films , vol.516 , pp. 9002-9005
    • Perinotto, A.C.1    Caseli, L.2    Hayasaka, C.O.3    Riul Jr., A.4    Oliveira Jr., O.N.5    Zucolotto, V.6
  • 12
    • 78650617705 scopus 로고    scopus 로고
    • Development of novel bioanodes for ethanol biofuel cell using PAMAM dendrimers as matrix for enzyme immobilization
    • J.C. Forti, S. Aquino Neto, V. Zucolotto, P. Ciancaglini, and A.R. De Andrade Development of novel bioanodes for ethanol biofuel cell using PAMAM dendrimers as matrix for enzyme immobilization Biosens Bioelectron 26 2011 2675 2679
    • (2011) Biosens Bioelectron , vol.26 , pp. 2675-2679
    • Forti, J.C.1    Aquino Neto, S.2    Zucolotto, V.3    Ciancaglini, P.4    De Andrade, A.R.5
  • 13
    • 78651371639 scopus 로고    scopus 로고
    • Development of nanostructured bioanodes containing dendrimers and dehydrogenases enzymes for application in ethanol biofuel cells
    • S. Aquino Neto, J.C. Forti, V. Zucolotto, P. Ciancaglini, and A.R. De Andrade Development of nanostructured bioanodes containing dendrimers and dehydrogenases enzymes for application in ethanol biofuel cells Biosens Bioelectron 26 2011 2922 2926
    • (2011) Biosens Bioelectron , vol.26 , pp. 2922-2926
    • Aquino Neto, S.1    Forti, J.C.2    Zucolotto, V.3    Ciancaglini, P.4    De Andrade, A.R.5
  • 14
    • 4143087202 scopus 로고    scopus 로고
    • Improving the environment for immobilized dehydrogenase enzymes by modifying nafion with tetraalkylammonium bromides
    • DOI 10.1021/bm0345256
    • C.M. Moore, N.L. Akers, A.D. Hill, Z.C. Johnson, and S.D. Minteer Improving the environment for immobilized dehydrogenase enzymes by modifying nafion with tetraalkylammonium bromides Biomacromolecules 5 2004 1241 1247 (Pubitemid 39089722)
    • (2004) Biomacromolecules , vol.5 , Issue.4 , pp. 1241-1247
    • Moore, C.M.1    Akers, N.L.2    Hill, A.D.3    Johnson, Z.C.4    Minteer, S.D.5
  • 15
    • 0030576644 scopus 로고    scopus 로고
    • The electrochemical polymerization of methylene green and its electrocatalysis for the oxidation of NADH
    • DOI 10.1016/0003-2670(96)00117-1
    • D. Zhou, H. Fang, H. Chen, H. Ju, and Y. Wang The electrochemical polymerization of methylene green and its electrocatalysis for the oxidation of NADH Anal Chim Acta 329 1996 41 48 (Pubitemid 26254973)
    • (1996) Analytica Chimica Acta , vol.329 , Issue.1-2 , pp. 41-48
    • Zhou, D.-M.1    Fang, H.-Q.2    Chen, H.-Y.3    Ju, H.-X.4    Wang, Y.5
  • 17
    • 0030398821 scopus 로고    scopus 로고
    • Improvement of electrochemical biosensors using enzyme immobilization from water-organic mixtures with a high content of organic solvent
    • A.A. Karyakin, E.E. Karyakina, and L. Gorton Improvement of electrochemical biosensors using enzyme immobilization from water-organic mixtures with a high content of organic solvent Anal Chem 68 1996 4335 4341
    • (1996) Anal Chem , vol.68 , pp. 4335-4341
    • Karyakin, A.A.1    Karyakina, E.E.2    Gorton, L.3
  • 18
    • 15344344385 scopus 로고    scopus 로고
    • 2 biofuel cells using salt-extracted tetrabutylammonium bromide/Nafion membranes to immobilize dehydrogenase enzymes
    • DOI 10.1016/j.electacta.2004.10.080, PII S0013468604010977
    • 2 biofuel cells using salt-extracted tetrabutylammonium bromide/nafion membranes to immobilize dehydrogenase enzymes Electrochim Acta 50 2005 2521 2525 (Pubitemid 40391144)
    • (2005) Electrochimica Acta , vol.50 , Issue.12 , pp. 2521-2525
    • Akers, N.L.1    Moore, C.M.2    Minteer, S.D.3
  • 20
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • H. Lineweaver, and D. Burk The determination of enzyme dissociation constants J Am Chem Soc 56 1934 658 666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 21
    • 0000802268 scopus 로고
    • Yeast alcohol dehydrogenase: Molecular weight, coenzyme binding, and reaction equilibria
    • J.E. Hayes, and S.F. Velick Yeast alcohol dehydrogenase: molecular weight, coenzyme binding, and reaction equilibria J Biol Chem 207 1953 225 244
    • (1953) J Biol Chem , vol.207 , pp. 225-244
    • Hayes, J.E.1    Velick, S.F.2
  • 22
    • 43749117524 scopus 로고    scopus 로고
    • Kinetics of ethanol oxidation catalyzed by yeast alcohol dehydrogenase in aqueous solutions of sodium dodecylsulfate
    • E. Abuin, E. Lissi, and L. León Kinetics of ethanol oxidation catalyzed by yeast alcohol dehydrogenase in aqueous solutions of sodium dodecylsulfate Protein J 27 2008 247 252
    • (2008) Protein J , vol.27 , pp. 247-252
    • Abuin, E.1    Lissi, E.2    León, L.3
  • 23
    • 0018077763 scopus 로고
    • Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae
    • K.A. Bostian, and G.F. Betts Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from saccharomyces cerevisiae J Biochem 173 1978 787 798 (Pubitemid 9010971)
    • (1978) Biochemical Journal , vol.173 , Issue.3 , pp. 787-798
    • Bostian, K.A.1    Betts, G.F.2
  • 24
    • 0014429124 scopus 로고
    • Yeast aldehyde dehydrogenase. II. Properties of the homogeneous enzyme preparation
    • C. Steinman, and W.B. Jakoby Yeast aldehyde dehydrogenase. II. Properties of the homogeneous enzyme preparation J Biol Chem 243 1948 730 734
    • (1948) J Biol Chem , vol.243 , pp. 730-734
    • Steinman, C.1    Jakoby, W.B.2
  • 25
    • 59049089641 scopus 로고    scopus 로고
    • Substrate specificity of human and yeast aldehyde dehydrogenases
    • M.F. Wang, C.L. Han, and S.J. Yin Substrate specificity of human and yeast aldehyde dehydrogenases Chem Biol Int 178 2009 36 39
    • (2009) Chem Biol Int , vol.178 , pp. 36-39
    • Wang, M.F.1    Han, C.L.2    Yin, S.J.3
  • 26
    • 0016794274 scopus 로고
    • A study of the pH- and temperature-dependence of the reactions of yeast alcohol dehydrogenase with ethanol, acetaldehyde and butyraldehyde as substrates
    • C.J. Dickenson, and F.M. Dickinson A study of the pH- and temperature-dependence of the reactions of yeast alcohol dehydrogenase with ethanol, acetaldehyde and butyraldehyde as substrates Biochem J 147 1975 303 311
    • (1975) Biochem J , vol.147 , pp. 303-311
    • Dickenson, C.J.1    Dickinson, F.M.2
  • 27
    • 33846220596 scopus 로고    scopus 로고
    • Colorimetric assay of ethanol using alcohol dehydrogenase from dry baker's yeast
    • DOI 10.1016/j.enzmictec.2006.07.029, PII S0141022906003735, International Conference on Enzyme Technology "RELATENZ 2005"
    • J.P. Zanon, M.F.S. Peres, and E.A.L. Gattás Colorimetric assay of ethanol using alcohol dehydrogenase from dry baker's yeast Enzyme Microb Technol 40 2007 466 470 (Pubitemid 46091693)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.3 , pp. 466-470
    • Zanon, J.P.1    Peres, M.F.S.2    Gattas, E.A.L.3
  • 28
    • 0030755078 scopus 로고    scopus 로고
    • + binding by yeast alcohol dehydrogenase in the presence of pyrazole and a new method for the determination of the enzyme active site concentration
    • DOI 10.1023/A:1018308830633
    • S. Trivic, J. Zeremski, and V. Leskovac NAD(+) binding by yeast alcohol-dehydrogenase in the presence of pyrazole and a new method for the determination of the enzyme active-site concentration Biotechnol Lett 8 1997 809 811 (Pubitemid 27367642)
    • (1997) Biotechnology Letters , vol.19 , Issue.8 , pp. 809-811
    • Trivic, S.1    Zeremski, J.2    Leskovac, V.3
  • 29
    • 65749088973 scopus 로고    scopus 로고
    • Citric acid cycle biomimic on a carbon electrode
    • D. Sokic-Lazic, and S.D. Minteer Citric acid cycle biomimic on a carbon electrode Biosens Bioelectron 24 2008 939 944
    • (2008) Biosens Bioelectron , vol.24 , pp. 939-944
    • Sokic-Lazic, D.1    Minteer, S.D.2
  • 30
    • 67651233807 scopus 로고    scopus 로고
    • Pyruvate/air enzymatic biofuel cell capable of complete oxidation
    • D. Sokic-Lazic, and S.D. Minteer Pyruvate/air enzymatic biofuel cell capable of complete oxidation Electrochem Solid-State Lett 9 2009 F26 F28
    • (2009) Electrochem Solid-State Lett , vol.9
    • Sokic-Lazic, D.1    Minteer, S.D.2


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