메뉴 건너뛰기




Volumn 48, Issue 1, 1997, Pages 34-40

Production, purification and characterization of glucose oxidase from a newly isolated strain of Penicillium pinophilum

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE OXIDASE; GLYCOPROTEIN;

EID: 0030805067     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530051011     Document Type: Article
Times cited : (68)

References (47)
  • 1
    • 0009877782 scopus 로고
    • Malate dehydrogenase: Oxaloacetate to malate reaction
    • Bergmeyer HU (ed) Verlag Chemie, Weinheim
    • Bergmeyer HU, Bernt E (1983) Malate dehydrogenase: oxaloacetate to malate reaction. In: Bergmeyer HU (ed) Methods of enzymatic analysis 3rd edn, vol 3. Verlag Chemie, Weinheim, pp 171-175
    • (1983) Methods of Enzymatic Analysis 3rd Edn , vol.3 , pp. 171-175
    • Bergmeyer, H.U.1    Bernt, E.2
  • 2
    • 8544258586 scopus 로고
    • D-Glucose-Oxydasen aus Penicillium notatum (Notatin) und Aspergillus niger (Nigerin). Isolierung und einige molekulare Eigenschaften
    • Bodmann O, Walter M (1965) D-Glucose-Oxydasen aus Penicillium notatum (Notatin) und Aspergillus niger (Nigerin). Isolierung und einige molekulare Eigenschaften. Biochim Biophys Acta 110: 496-506
    • (1965) Biochim Biophys Acta , vol.110 , pp. 496-506
    • Bodmann, O.1    Walter, M.2
  • 3
    • 0002941117 scopus 로고
    • Glucose-transforming enzymes
    • Fogarty WM, Kelly CE (eds) Elsevier, London, New York
    • Crueger A, Crueger W (1990) Glucose-transforming enzymes. In: Fogarty WM, Kelly CE (eds) Microbial enzymes and biotechnology, 2nd edn. Elsevier, London, New York, pp 177-227
    • (1990) Microbial Enzymes and Biotechnology, 2nd Edn. , pp. 177-227
    • Crueger, A.1    Crueger, W.2
  • 4
    • 0026955806 scopus 로고
    • Goal-oriented screening method for carbohydrate oxidases produced by filamentous fungi
    • Danneel H-J, Ullrich M, Giffhorn F (1992) Goal-oriented screening method for carbohydrate oxidases produced by filamentous fungi. Enzyme Microb Technol 14: 898-903
    • (1992) Enzyme Microb Technol , vol.14 , pp. 898-903
    • Danneel, H.-J.1    Ullrich, M.2    Giffhorn, F.3
  • 5
    • 0027310313 scopus 로고
    • Purification and characterization of a pyranose oxidase from the basidiomycete Peniophora gigantea and chemical analyses of its reaction products
    • Danneel H-J, Rössner E, Zeeck A, Giffhorn F (1993) Purification and characterization of a pyranose oxidase from the basidiomycete Peniophora gigantea and chemical analyses of its reaction products. Eur J Biochem 214: 795-802
    • (1993) Eur J Biochem , vol.214 , pp. 795-802
    • Danneel, H.-J.1    Rössner, E.2    Zeeck, A.3    Giffhorn, F.4
  • 6
    • 0025127363 scopus 로고
    • Intensification of glucose oxidase synthesis with Aspergillus niger by the way of multistage mutagenization
    • Fiedurek J, Rogalski J, Ilczuk Z (1990) Intensification of glucose oxidase synthesis with Aspergillus niger by the way of multistage mutagenization. Acta Biotechnol 10: 371-376
    • (1990) Acta Biotechnol , vol.10 , pp. 371-376
    • Fiedurek, J.1    Rogalski, J.2    Ilczuk, Z.3
  • 10
    • 0029690049 scopus 로고    scopus 로고
    • Influence of medium components and metabolic inhibitors on glucose oxidase production by Aspergillus niger mycelium
    • Gromada A, Fiedurek J (1996) Influence of medium components and metabolic inhibitors on glucose oxidase production by Aspergillus niger mycelium. Acta Microbiol Polon 45: 37-43
    • (1996) Acta Microbiol Polon , vol.45 , pp. 37-43
    • Gromada, A.1    Fiedurek, J.2
  • 12
    • 0027397187 scopus 로고
    • Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution
    • Hecht HJ, Kalisz HM, Hendle J, Schmid RD, Schomburg D (1993) Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution. J Mol Biol 229: 153-172
    • (1993) J Mol Biol , vol.229 , pp. 153-172
    • Hecht, H.J.1    Kalisz, H.M.2    Hendle, J.3    Schmid, R.D.4    Schomburg, D.5
  • 13
    • 0028820720 scopus 로고
    • Optimization of glucose oxidase production by Aspergillus niger using genetic- and process-engineering techniques
    • Hellmuth K, Pluschkell S, Jung JK, Ruttkowski E, Rinas U (1995) Optimization of glucose oxidase production by Aspergillus niger using genetic- and process-engineering techniques. Appl Microbiol Biotechnol 43: 978-984
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 978-984
    • Hellmuth, K.1    Pluschkell, S.2    Jung, J.K.3    Ruttkowski, E.4    Rinas, U.5
  • 14
    • 0000608931 scopus 로고
    • Adenosine 5′1-diphosphate and adenosine 5′-monophosphate. UV-method
    • Bergmeyer HU (ed) Verlag Chemie, Weinheim
    • Jaworek D, Welsch J (1985) Adenosine 5′1-diphosphate and adenosine 5′-monophosphate. UV-method. In: Bergmeyer HU (ed) Methods of enzymatic analysis. 3rd edn, vol 7. Verlag Chemie, Weinheim, pp 365-370
    • (1985) Methods of Enzymatic Analysis. 3rd Edn , vol.7 , pp. 365-370
    • Jaworek, D.1    Welsch, J.2
  • 16
    • 0025939670 scopus 로고
    • Effects of carbohydrate depletion on the structure, stability and activity of glucose oxidase from Aspergillus niger
    • Kalisz HM, Hecht H-J, Schomburg D, Schmid RD (1991) Effects of carbohydrate depletion on the structure, stability and activity of glucose oxidase from Aspergillus niger. Biochim Biophys Acta 1080: 138-142
    • (1991) Biochim Biophys Acta , vol.1080 , pp. 138-142
    • Kalisz, H.M.1    Hecht, H.-J.2    Schomburg, D.3    Schmid, R.D.4
  • 17
    • 0025972606 scopus 로고
    • Comparison of Penicillium amagasakiense glucose oxidase purified as glyco- and aglyco- proteins
    • Kim JM, Schmid RD (1991) Comparison of Penicillium amagasakiense glucose oxidase purified as glyco- and aglyco- proteins. FEMS Microbiol Letters 78: 221-226
    • (1991) FEMS Microbiol Letters , vol.78 , pp. 221-226
    • Kim, J.M.1    Schmid, R.D.2
  • 18
    • 0025253349 scopus 로고
    • Production, purification, and properties of glucose oxidase from the biocontrol fungus Talaromyces flavus
    • Kim KK, Fravel DR, Papavizas G (1990) Production, purification, and properties of glucose oxidase from the biocontrol fungus Talaromyces flavus. Can J Microbiol 36: 199-205
    • (1990) Can J Microbiol , vol.36 , pp. 199-205
    • Kim, K.K.1    Fravel, D.R.2    Papavizas, G.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0027970337 scopus 로고
    • Enhancement of glucose oxidase fermentation by addition of hydrocarbon
    • Li T-H, Chen T-L (1994) Enhancement of glucose oxidase fermentation by addition of hydrocarbon. J Ferment Bioeng 78: 298-303
    • (1994) J Ferment Bioeng , vol.78 , pp. 298-303
    • Li, T.-H.1    Chen, T.-L.2
  • 22
    • 0021710777 scopus 로고
    • The kinetics and physiology of stipitatic acid and gluconate production by carbon sufficient cultures of Penicillium stipitatum growing in continuous culture
    • Linton JD, Austin RM, Haugh DE (1984) The kinetics and physiology of stipitatic acid and gluconate production by carbon sufficient cultures of Penicillium stipitatum growing in continuous culture. Biotechnol Bioeng 26: 1455-1464
    • (1984) Biotechnol Bioeng , vol.26 , pp. 1455-1464
    • Linton, J.D.1    Austin, R.M.2    Haugh, D.E.3
  • 24
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behaviour of enzymes: Application to protein mixtures
    • Martin RG, Ames BN (1961) A method for determining the sedimentation behaviour of enzymes: application to protein mixtures. J Biol Chem 236: 1372-1379
    • (1961) J Biol Chem , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 25
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins
    • Merril CR, Goldman D, Sedman SA, Ebert MH (1981) Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins. Science 211: 1437-1438
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 26
    • 0013361081 scopus 로고
    • n-gluconate (D-glucono-γ-lactone) and D-gluconate 6-phosphate
    • Bergmeyer HU (ed) Verlag Chemie, Weinheim
    • Moellering GH, Bergmeyer HU (1984) n-gluconate (D-glucono-γ-lactone) and D-gluconate 6-phosphate. In: Bergmeyer HU (ed) Methods of enzymatic analysis, 3rd edn, vol 6. Verlag Chemie, Weinheim, pp 220-227
    • (1984) Methods of Enzymatic Analysis, 3rd Edn , vol.6 , pp. 220-227
    • Moellering, G.H.1    Bergmeyer, H.U.2
  • 27
    • 84981776413 scopus 로고
    • Antigen-antibody reactions in gels, types of reactions in coordinated systems of diffusion
    • Ouchterlony Ö (1953) Antigen-antibody reactions in gels, types of reactions in coordinated systems of diffusion. Acta Pathol Microbiol Scand 32: 231-240
    • (1953) Acta Pathol Microbiol Scand , vol.32 , pp. 231-240
    • Ouchterlony, Ö.1
  • 28
    • 0009660169 scopus 로고
    • Glucose oxidase from Aspergillus niger
    • Pazur JH (1966) Glucose oxidase from Aspergillus niger. Methods Enzymol 9: 82-87
    • (1966) Methods Enzymol , vol.9 , pp. 82-87
    • Pazur, J.H.1
  • 29
    • 0027428792 scopus 로고
    • Glucose oxidase production by Penicillium variabile P16: Effect of medium composition
    • Petruccioli M, Federici F (1993) Glucose oxidase production by Penicillium variabile P16: effect of medium composition. J Appl Bacteriol 75: 369-372
    • (1993) J Appl Bacteriol , vol.75 , pp. 369-372
    • Petruccioli, M.1    Federici, F.2
  • 30
    • 4344563110 scopus 로고
    • Über das Vitamin B 12-Bedürfnis phototropher Schwefelbakterien
    • Pfennig N, Lippert KD (1966) Über das Vitamin B 12-Bedürfnis phototropher Schwefelbakterien. Arch Microbiol 55: 245-256
    • (1966) Arch Microbiol , vol.55 , pp. 245-256
    • Pfennig, N.1    Lippert, K.D.2
  • 31
    • 8544279414 scopus 로고
    • Control of 8-bromo-AMP and 8-(6-aminohexyl)-amino-AMP synthesis by HPLC
    • Raffin JP, Leray C (1980) Control of 8-bromo-AMP and 8-(6-aminohexyl)-amino-AMP synthesis by HPLC. J Chromatogr 196: 323-330
    • (1980) J Chromatogr , vol.196 , pp. 323-330
    • Raffin, J.P.1    Leray, C.2
  • 32
    • 0020696219 scopus 로고
    • Adaptation of Rhodopseudomonas sphaeroides to growth on D-(-)-tartrate and large-scale production of a constitutive D-(-)-tartrate dehydratase during growth on DL-malate
    • Rode H, Giffhorn F (1983) Adaptation of Rhodopseudomonas sphaeroides to growth on D-(-)-tartrate and large-scale production of a constitutive D-(-)-tartrate dehydratase during growth on DL-malate. Appl Environ Microbiol 45: 716-719
    • (1983) Appl Environ Microbiol , vol.45 , pp. 716-719
    • Rode, H.1    Giffhorn, F.2
  • 34
    • 0029908625 scopus 로고    scopus 로고
    • Purification by immunoaffinity chromatography, characterization, and structural analysis of a thermostable pyranose oxidase from the white rot fungus Phlebiopsis gigantea
    • Schäfer A, Bieg S, Huwig A, Kohring G-W, Giffhom F (1996) Purification by immunoaffinity chromatography, characterization, and structural analysis of a thermostable pyranose oxidase from the white rot fungus Phlebiopsis gigantea. Appl Environ Microbiol 62: 2586-2592
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2586-2592
    • Schäfer, A.1    Bieg, S.2    Huwig, A.3    Kohring, G.-W.4    Giffhom, F.5
  • 35
    • 0003169214 scopus 로고
    • Biosensors and "bioelectronics"
    • Rehm HJ, Reed G (eds) Verlag Chemie, Weinheim
    • Schmid RD, Karube I (1988) Biosensors and "bioelectronics". In: Rehm HJ, Reed G (eds) Biotechnology, vol 6b. Verlag Chemie, Weinheim, pp 317-365
    • (1988) Biotechnology , vol.6 B , pp. 317-365
    • Schmid, R.D.1    Karube, I.2
  • 36
    • 34250946567 scopus 로고
    • Die Carotinoide der Thiorhodaceae. I. Okenon als Hauptearotinoid von Chromatium okenii Perty
    • Schmidt K, Liaaen Jensen S, Schlegel HG (1963) Die Carotinoide der Thiorhodaceae. I. Okenon als Hauptearotinoid von Chromatium okenii Perty. Arch Mikrobiol 46: 117-126
    • (1963) Arch Mikrobiol , vol.46 , pp. 117-126
    • Schmidt, K.1    Liaaen Jensen, S.2    Schlegel, H.G.3
  • 37
    • 30344463700 scopus 로고
    • Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfate
    • Segrest JP, Jackson RL (1972) Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Methods Enzymol 28: 54-63
    • (1972) Methods Enzymol , vol.28 , pp. 54-63
    • Segrest, J.P.1    Jackson, R.L.2
  • 38
    • 0026454644 scopus 로고
    • Expression and overproduction of glucose oxidase in Aspergillus niger
    • Sharif FA, Alaeddinoglu NG (1992) Expression and overproduction of glucose oxidase in Aspergillus niger. Appl Microbiol Biotechnol 38: 115-116
    • (1992) Appl Microbiol Biotechnol , vol.38 , pp. 115-116
    • Sharif, F.A.1    Alaeddinoglu, N.G.2
  • 39
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation
    • Siegel EM, Monty KJ (1966) Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Biochim Biophys Acta 112: 346-362
    • (1966) Biochim Biophys Acta , vol.112 , pp. 346-362
    • Siegel, E.M.1    Monty, K.J.2
  • 40
    • 0000475128 scopus 로고
    • Purification and properties of glucose oxidase from Aspergillus niger
    • Swoboda BEP, Massey V (1965) Purification and properties of glucose oxidase from Aspergillus niger. J Biol Chem 24: 2209-2215
    • (1965) J Biol Chem , vol.24 , pp. 2209-2215
    • Swoboda, B.E.P.1    Massey, V.2
  • 41
    • 0030269984 scopus 로고    scopus 로고
    • Analysis of various sugars by means of immobilized enzyme coupled flow injection analysis (FIA)
    • Weigel B, Hitzmann B, Kretzmer G, Schügerl K, Huwig A, Giffhorn F (1996) Analysis of various sugars by means of immobilized enzyme coupled flow injection analysis (FIA) J Biotechnol 50: 93-106
    • (1996) J Biotechnol , vol.50 , pp. 93-106
    • Weigel, B.1    Hitzmann, B.2    Kretzmer, G.3    Schügerl, K.4    Huwig, A.5    Giffhorn, F.6
  • 43
    • 0026511368 scopus 로고
    • Localization of glucose oxidase and catalase activity in Aspergillus niger
    • Witteveen CFB, Veenhuis M, Visser J (1992) Localization of glucose oxidase and catalase activity in Aspergillus niger. Appl Environ Microbiol 58: 1190-1194
    • (1992) Appl Environ Microbiol , vol.58 , pp. 1190-1194
    • Witteveen, C.F.B.1    Veenhuis, M.2    Visser, J.3
  • 44
    • 0014301425 scopus 로고
    • Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli
    • Valentine RC, Shapiro BM, Stadtman ER (1968) Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli. Biochemistry 7: 2143-2152
    • (1968) Biochemistry , vol.7 , pp. 2143-2152
    • Valentine, R.C.1    Shapiro, B.M.2    Stadtman, E.R.3
  • 45
    • 0000307813 scopus 로고
    • Properties of choline oxidase of Cylindrocarpon didymun M-1
    • Yamada H, Mori N, Tani Y (1979) Properties of choline oxidase of Cylindrocarpon didymun M-1. Agric Biol Chem 43: 2173-2177
    • (1979) Agric Biol Chem , vol.43 , pp. 2173-2177
    • Yamada, H.1    Mori, N.2    Tani, Y.3
  • 46
    • 0014786105 scopus 로고
    • The role of aeration and agitation in the production of glucose oxidase in submerged cultures. II
    • Zetelaki KZ (1970) The role of aeration and agitation in the production of glucose oxidase in submerged cultures. II. Biotechnol Bioeng 12: 379-397
    • (1970) Biotechnol Bioeng , vol.12 , pp. 379-397
    • Zetelaki, K.Z.1
  • 47
    • 0014981447 scopus 로고
    • An X-ray small angle study of bacteriophages fr and R17
    • Zipper P, Kratky O, Herrmenn R, Hohn T (1971 ) An X-ray small angle study of bacteriophages fr and R17. Eur J Biochem 18: 1 9
    • (1971) Eur J Biochem , vol.18 , pp. 19
    • Zipper, P.1    Kratky, O.2    Herrmenn, R.3    Hohn, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.