메뉴 건너뛰기




Volumn 5, Issue 5, 2011, Pages 1068-1076

Review of glucose oxidases and glucose dehydrogenases: A bird's eye view of glucose sensing enzymes

Author keywords

Biosensing; Glucose dehydrogenase; Glucose oxidase; Point of care testing; Self monitoring of blood glucose

Indexed keywords

GLUCOSE DEHYDROGENASE; GLUCOSE OXIDASE;

EID: 84857405775     PISSN: None     EISSN: 19322968     Source Type: Journal    
DOI: 10.1177/193229681100500507     Document Type: Conference Paper
Times cited : (365)

References (36)
  • 1
    • 10244223555 scopus 로고
    • Electrode systems for continuous monitoring in cardiovascular surgery
    • Clark LC Jr, Lyons C. Electrode systems for continuous monitoring in cardiovascular surgery. Ann N Y Acad Sci. 1962;102:29-45.
    • (1962) Ann N Y Acad Sci , vol.102 , pp. 29-45
    • Clark Jr., L.C.1    Lyons, C.2
  • 2
    • 0001553717 scopus 로고
    • The use of glucose oxidase for the determination of glucose in biological material and for the study of glucose-producing systems by manometric methods
    • Keilin D, Hartree EF. The use of glucose oxidase for the determination of glucose in biological material and for the study of glucose-producing systems by manometric methods. Biochem J. 1948;42(2):230-8.
    • (1948) Biochem J , vol.42 , Issue.2 , pp. 230-238
    • Keilin, D.1    Hartree, E.F.2
  • 3
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: A review
    • Romanos MA, Scorer CA, Clare JJ. Foreign gene expression in yeast: a review. Yeast. 1992;8(6):423-88.
    • (1992) Yeast , vol.8 , Issue.6 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3
  • 4
    • 0031968383 scopus 로고    scopus 로고
    • Structural and kinetic properties of nonglycosylated recombinant Penicillium amagasakiense glucose oxidase expressed in Escherichia coli
    • Witt S, Singh M, Kalisz HM. Structural and kinetic properties of nonglycosylated recombinant Penicillium amagasakiense glucose oxidase expressed in Escherichia coli. Appl Environ Microbiol. 1998;64(4):1405-11.
    • (1998) Appl Environ Microbiol , vol.64 , Issue.4 , pp. 1405-1411
    • Witt, S.1    Singh, M.2    Kalisz, H.M.3
  • 5
    • 0013863810 scopus 로고
    • The efect of hydrogen peroxide on glucose oxidase from Aspergillus niger
    • Kleppe K. The efect of hydrogen peroxide on glucose oxidase from Aspergillus niger. Biochemistry. 1966;5(1):139-43.
    • (1966) Biochemistry , vol.5 , Issue.1 , pp. 139-143
    • Kleppe, K.1
  • 6
    • 0034905899 scopus 로고    scopus 로고
    • A kinetic study on air oxidation of glucose catalyzed by immobilized glucose oxidase for production of calcium gluconate
    • Bao J, Furumoto K, Fukunaga K, Nakao K. A kinetic study on air oxidation of glucose catalyzed by immobilized glucose oxidase for production of calcium gluconate. Biochem Eng J. 2001;8:91-102.
    • (2001) Biochem Eng J , vol.8 , pp. 91-102
    • Bao, J.1    Furumoto, K.2    Fukunaga, K.3    Nakao, K.4
  • 7
    • 0037015415 scopus 로고    scopus 로고
    • Diauxic production of glucose oxidase by Aspergillus niger in submerged culture - A dynamic model
    • Mirón J, González MP, Pastrana L, Murado MA. Diauxic production of glucose oxidase by Aspergillus niger in submerged culture - a dynamic model. Enz Microb Technol. 2002;31:615-20.
    • (2002) Enz Microb Technol , vol.31 , pp. 615-620
    • Mirón, J.1    González, M.P.2    Pastrana, L.3    Murado, M.A.4
  • 8
    • 0030578372 scopus 로고    scopus 로고
    • Alcohol biosensors based on coupled oxidase-peroxidase systems
    • Vijayakumar AR, Csöregi E, Heller A, Gorton L. Alcohol biosensors based on coupled oxidase-peroxidase systems. Anal Chim Acta. 1996;327(3):223-34.
    • (1996) Anal Chim Acta , vol.327 , Issue.3 , pp. 223-234
    • Vijayakumar, A.R.1    Csöregi, E.2    Heller, A.3    Gorton, L.4
  • 11
    • 17444412699 scopus 로고    scopus 로고
    • Cast thin film biosensor design based on a Nafion backbone, a multiwalled carbon nanotube conduit, and a glucose oxidase function
    • Tsai YC, Li SC, Chen JM. Cast thin film biosensor design based on a Nafion backbone, a multiwalled carbon nanotube conduit, and a glucose oxidase function. Langmuir. 2005;21(8):3653-8.
    • (2005) Langmuir , vol.21 , Issue.8 , pp. 3653-3658
    • Tsai, Y.C.1    Li, S.C.2    Chen, J.M.3
  • 12
    • 33746825839 scopus 로고    scopus 로고
    • Carbon nanofiber-based glucose biosensor
    • Vamvakaki V, Tsagaraki K, Chaniotakis N. Carbon nanofiber-based glucose biosensor. Anal Chem. 2006;78(15):5538-42.
    • (2006) Anal Chem , vol.78 , Issue.15 , pp. 5538-5542
    • Vamvakaki, V.1    Tsagaraki, K.2    Chaniotakis, N.3
  • 13
    • 70349786339 scopus 로고    scopus 로고
    • Deglycosylation of glucose oxidase for direct and eficient glucose electrooxidation on a glassy carbon electrode
    • Courjean O, Gao F, Mano N. Deglycosylation of glucose oxidase for direct and eficient glucose electrooxidation on a glassy carbon electrode. Angew Chem Int Ed Engl. 2009;48(32):5897-9.
    • (2009) Angew Chem Int Ed Engl , vol.48 , Issue.32 , pp. 5897-5899
    • Courjean, O.1    Gao, F.2    Mano, N.3
  • 14
    • 0033135955 scopus 로고    scopus 로고
    • 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
    • Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ. 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 5):969-77.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 5 , pp. 969-977
    • Wohlfahrt, G.1    Witt, S.2    Hendle, J.3    Schomburg, D.4    Kalisz, H.M.5    Hecht, H.J.6
  • 15
    • 33750075455 scopus 로고    scopus 로고
    • Soluble aldose sugar dehydrogenase from Escherichia coli: A highly exposed active site conferring broad substrate specificity
    • Southall SM, Doel JJ, Richardson DJ, Oubrie A. Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity. J Biol Chem. 2006;281(41):30650-9.
    • (2006) J Biol Chem , vol.281 , Issue.41 , pp. 30650-30659
    • Southall, S.M.1    Doel, J.J.2    Richardson, D.J.3    Oubrie, A.4
  • 16
    • 0033517714 scopus 로고    scopus 로고
    • Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered K(m) values - site-directed mutagenesis studies on the putative active site
    • Igarashi S, Ohtera T, Yoshida H, Witarto AB, Sode K. Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered K(m) values - site-directed mutagenesis studies on the putative active site. Biochem Biophys Res Commun. 1999;264(3):820-4.
    • (1999) Biochem Biophys Res Commun , vol.264 , Issue.3 , pp. 820-824
    • Igarashi, S.1    Ohtera, T.2    Yoshida, H.3    Witarto, A.B.4    Sode, K.5
  • 19
    • 0036901886 scopus 로고    scopus 로고
    • Construction of engineered water-soluble PQQ glucose dehydrogenase with improved substrate specificity
    • Sode K, Igarashi S, Morimoto A, Yoshida H. Construction of engineered water-soluble PQQ glucose dehydrogenase with improved substrate specificity. Biocatal Biotransform. 2002;20:405-12.
    • (2002) Biocatal Biotransform , vol.20 , pp. 405-412
    • Sode, K.1    Igarashi, S.2    Morimoto, A.3    Yoshida, H.4
  • 20
    • 2042548037 scopus 로고    scopus 로고
    • Engineering PQQ glucose dehydrogenase with improved substrate specificity. Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase
    • Igarashi S, Hirokawa T, Sode K. Engineering PQQ glucose dehydrogenase with improved substrate specificity. Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase. Biomol Eng. 2004;21(2):81-9.
    • (2004) Biomol Eng , vol.21 , Issue.2 , pp. 81-89
    • Igarashi, S.1    Hirokawa, T.2    Sode, K.3
  • 21
    • 33750984509 scopus 로고    scopus 로고
    • Modified substrate specificity of pyrroloquinoline quinone glucose dehydrogenase by biased mutation assembling with optimized amino acid substitution
    • Hamamatsu N, Suzumura A, Nomiya Y, Sato M, Aita T, Nakajima M, Husimi Y, Shibanaka Y. Modified substrate specificity of pyrroloquinoline quinone glucose dehydrogenase by biased mutation assembling with optimized amino acid substitution. Appl Microbiol Biotechnol. 2006;73(3):607-17.
    • (2006) Appl Microbiol Biotechnol , vol.73 , Issue.3 , pp. 607-617
    • Hamamatsu, N.1    Suzumura, A.2    Nomiya, Y.3    Sato, M.4    Aita, T.5    Nakajima, M.6    Husimi, Y.7    Shibanaka, Y.8
  • 22
    • 0034079533 scopus 로고    scopus 로고
    • Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement
    • Sode K, Ootera T, Shirahane M, Witarto AB, Igarashi S, Yoshida H. Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement. Enzyme Microb Technol. 2000;26(7):491-6.
    • (2000) Enzyme Microb Technol , vol.26 , Issue.7 , pp. 491-496
    • Sode, K.1    Ootera, T.2    Shirahane, M.3    Witarto, A.B.4    Igarashi, S.5    Yoshida, H.6
  • 23
    • 0037809323 scopus 로고    scopus 로고
    • Stabilization of quaternary structure of water-soluble quinoprotein glucose dehydrogenase
    • Igarashi S, Sode K. Stabilization of quaternary structure of water-soluble quinoprotein glucose dehydrogenase. Mol Biotechnol. 2003;24(2):97-104.
    • (2003) Mol Biotechnol , vol.24 , Issue.2 , pp. 97-104
    • Igarashi, S.1    Sode, K.2
  • 24
    • 15444364022 scopus 로고    scopus 로고
    • Increasing stability of water-soluble PQQ glucose dehydrogenase by increasing hydrophobic interaction at dimeric interface
    • Tanaka S, Igarashi S, Ferri S, Sode K. Increasing stability of water-soluble PQQ glucose dehydrogenase by increasing hydrophobic interaction at dimeric interface. BMC Biochem. 2005;6:1.
    • (2005) BMC Biochem , vol.6 , pp. 1
    • Tanaka, S.1    Igarashi, S.2    Ferri, S.3    Sode, K.4
  • 25
    • 0037070511 scopus 로고    scopus 로고
    • Secretion of water soluble pyrroloquinoline quinone glucose dehydrogenase by recombinant Pichia pastoris
    • Yoshida H, Araki N, Tomisaka A, Sode K. Secretion of water soluble pyrroloquinoline quinone glucose dehydrogenase by recombinant Pichia pastoris. Enzyme Microb Technol. 2002;30(3):312-8.
    • (2002) Enzyme Microb Technol , vol.30 , Issue.3 , pp. 312-318
    • Yoshida, H.1    Araki, N.2    Tomisaka, A.3    Sode, K.4
  • 26
    • 0142245758 scopus 로고    scopus 로고
    • Surface charge engineering of PQQ glucose dehydrogenase for downstream processing
    • Koh H, Igarashi S, Sode K. Surface charge engineering of PQQ glucose dehydrogenase for downstream processing. Biotechnol Lett. 2003;25(20):1695-701.
    • (2003) Biotechnol Lett , vol.25 , Issue.20 , pp. 1695-1701
    • Koh, H.1    Igarashi, S.2    Sode, K.3
  • 27
    • 0022839871 scopus 로고
    • Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
    • Giardina P, de Biasi MG, de Rosa M, Gambacorta A, Buonocore V. Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem J. 1986;239(3):517-22.
    • (1986) Biochem J , vol.239 , Issue.3 , pp. 517-522
    • Giardina, P.1    De Biasi, M.G.2    De Rosa, M.3    Gambacorta, A.4    Buonocore, V.5
  • 28
    • 27844513782 scopus 로고    scopus 로고
    • Substrate specificity of glucose dehydrogenase (GDH) of Enterobacter asburiae PSI3 and rock phosphate solubilization with GDH substrates as C sources
    • Sharma V, Kumar V, Archana G, Kumar GN. Substrate specificity of glucose dehydrogenase (GDH) of Enterobacter asburiae PSI3 and rock phosphate solubilization with GDH substrates as C sources. Can J Microbiol. 2005;51(6):477-82.
    • (2005) Can J Microbiol , vol.51 , Issue.6 , pp. 477-482
    • Sharma, V.1    Kumar, V.2    Archana, G.3    Kumar, G.N.4
  • 29
    • 0017698813 scopus 로고
    • Conformational and functional aspects of the reversible dissociation and denaturation of glucose dehydrogenase
    • Pauly HE, Pfleiderer G. Conformational and functional aspects of the reversible dissociation and denaturation of glucose dehydrogenase. Biochemistry. 1977;16(21):4599-604.
    • (1977) Biochemistry , vol.16 , Issue.21 , pp. 4599-4604
    • Pauly, H.E.1    Pfleiderer, G.2
  • 30
    • 52449112953 scopus 로고    scopus 로고
    • Site directed mutagenesis studies of FAD-dependent glucose dehydrogenase catalytic subunit of Burkholderia cepacia
    • Yamaoka H, Yamashita Y, Ferri S, Sode K. Site directed mutagenesis studies of FAD-dependent glucose dehydrogenase catalytic subunit of Burkholderia cepacia. Biotechnol Lett. 2008;30(11):1967-72.
    • (2008) Biotechnol Lett , vol.30 , Issue.11 , pp. 1967-1972
    • Yamaoka, H.1    Yamashita, Y.2    Ferri, S.3    Sode, K.4
  • 32
    • 84856519362 scopus 로고
    • Untersuchungen über die Atmung und die Dehydrasesysteme von Aspergillus oryzae
    • Ogura Y, Nagahisa M. Untersuchungen über die Atmung und die Dehydrasesysteme von Aspergillus oryzae. Bot Mag Tokyo. 1937;51(606):597-612.
    • (1937) Bot Mag Tokyo , vol.51 , Issue.606 , pp. 597-612
    • Ogura, Y.1    Nagahisa, M.2
  • 33
    • 0014200117 scopus 로고
    • Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties
    • Bak TG. Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties. Biochim Biophys Acta. 1967;139(2):277-93.
    • (1967) Biochim Biophys Acta , vol.139 , Issue.2 , pp. 277-293
    • Bak, T.G.1
  • 35
    • 80053179412 scopus 로고    scopus 로고
    • Screening of Aspergillus-derived FAD: -Glucose dehydrogenases from fungal genome database
    • July 12, Epub ahead of print
    • Mori K, Nakajima M, Kojima K, Murakami K, Ferri S, Sode K. Screening of Aspergillus-derived FAD: -glucose dehydrogenases from fungal genome database. Biotechnol Lett. July 12, 2011. Epub ahead of print.
    • (2011) Biotechnol Lett
    • Mori, K.1    Nakajima, M.2    Kojima, K.3    Murakami, K.4    Ferri, S.5    Sode, K.6
  • 36
    • 0031761237 scopus 로고    scopus 로고
    • Positive interference of icodextrin metabolites in some enzymatic glucose methods
    • Janssen W, Harf G, Caers M, Schellekens A. Positive interference of icodextrin metabolites in some enzymatic glucose methods. Clin Chem. 1998;44(11):2379-80.
    • (1998) Clin Chem , vol.44 , Issue.11 , pp. 2379-2380
    • Janssen, W.1    Harf, G.2    Caers, M.3    Schellekens, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.