메뉴 건너뛰기




Volumn 72, Issue 3, 2008, Pages 833-841

Purification and characterization of a carbohydrate:acceptor oxidoreductase from Paraconiothyrium sp. that produces lactobionic acid efficiently

Author keywords

Carbohydrate:acceptor oxidoreductase; Glucooligosaccharide oxidase; Lactobionic acid; Lactose; Paraconiothyrium

Indexed keywords

GLUCOOLIGOSACCHARIDE OXIDASE; LACTOBIONIC ACID; LACTOSE; PARACONIOTHYRIUM;

EID: 41549167845     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70701     Document Type: Article
Times cited : (33)

References (26)
  • 1
    • 0026648314 scopus 로고
    • An examination of the effects of solutions containing histidine and lactobionate for heart, pancreas, and liver preservation in the rat
    • Sumimoto, R., Dohi, K., Urushihara, T., Jamieson, N. V., Ito, H., Sumimoto, K., and Fukuda, Y., An examination of the effects of solutions containing histidine and lactobionate for heart, pancreas, and liver preservation in the rat. Transplantation, 53, 1206-1210 (1992).
    • (1992) Transplantation , vol.53 , pp. 1206-1210
    • Sumimoto, R.1    Dohi, K.2    Urushihara, T.3    Jamieson, N.V.4    Ito, H.5    Sumimoto, K.6    Fukuda, Y.7
  • 2
    • 0026634164 scopus 로고
    • A comparison of the catalytic properties of cellobiose: Quinone oxidoreductase and cellobiose oxidase from Phanerochaete chrysosporium
    • Samejima, M., and Eriksson, K. E. L., A comparison of the catalytic properties of cellobiose: quinone oxidoreductase and cellobiose oxidase from Phanerochaete chrysosporium. Eur. J. Biochem., 207, 103-107 (1992).
    • (1992) Eur. J. Biochem , vol.207 , pp. 103-107
    • Samejima, M.1    Eriksson, K.E.L.2
  • 3
    • 0026576254 scopus 로고
    • Evidence that cellobiose oxidase from Phanerochaete chrysosporium is primarily an Fe(III) reductase
    • Kremer, S. M., and Wood, P. M., Evidence that cellobiose oxidase from Phanerochaete chrysosporium is primarily an Fe(III) reductase. Eur. J. Biochem., 205, 133-138 (1992).
    • (1992) Eur. J. Biochem , vol.205 , pp. 133-138
    • Kremer, S.M.1    Wood, P.M.2
  • 4
    • 0032478243 scopus 로고    scopus 로고
    • Substrate specificity of cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Henriksson, G., Sild, V., Szabo, I. J., Pettersson, G., and Johansson, G., Substrate specificity of cellobiose dehydrogenase from Phanerochaete chrysosporium. Biochim. Biophys. Acta, 1383, 48-54 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 48-54
    • Henriksson, G.1    Sild, V.2    Szabo, I.J.3    Pettersson, G.4    Johansson, G.5
  • 5
    • 0032519528 scopus 로고    scopus 로고
    • Characterization of a cellobiose dehydrogenase from Humicola insolens
    • Schou, C., Christensen, M. H., and Schulein, M., Characterization of a cellobiose dehydrogenase from Humicola insolens. Biochem. J., 330, 565-571 (1998).
    • (1998) Biochem. J , vol.330 , pp. 565-571
    • Schou, C.1    Christensen, M.H.2    Schulein, M.3
  • 6
    • 0021813669 scopus 로고
    • Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum
    • Morpeth, F. F., Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum. Biochem. J., 228, 557-564 (1985).
    • (1985) Biochem. J , vol.228 , pp. 557-564
    • Morpeth, F.F.1
  • 7
    • 0033562157 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile
    • Subramaniam, S. S., Nagalla, S. R., and Renganathan, V., Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile. Arch. Biochem. Biophys., 365, 223-230 (1999).
    • (1999) Arch. Biochem. Biophys , vol.365 , pp. 223-230
    • Subramaniam, S.S.1    Nagalla, S.R.2    Renganathan, V.3
  • 9
    • 0022647411 scopus 로고
    • Resolution, purification and some properties of the multiple forms of cellobiose quinone dehydrogenase from the white-rot fungus Sporotrichum pulverulentum
    • Morpeth, F. F., and Jones, G. D., Resolution, purification and some properties of the multiple forms of cellobiose quinone dehydrogenase from the white-rot fungus Sporotrichum pulverulentum. Biochem. J., 236, 221-226 (1986).
    • (1986) Biochem. J , vol.236 , pp. 221-226
    • Morpeth, F.F.1    Jones, G.D.2
  • 11
    • 0026068184 scopus 로고
    • Purification and characterization of a novel glucooligosaccharide oxidase from Acremonium strictum T1
    • Lin, S. F., Yang, T. Y., Inukai, T., Yamasaki, M., and Tsai, Y. C., Purification and characterization of a novel glucooligosaccharide oxidase from Acremonium strictum T1. Biochim. Biophys. Acta, 118, 41-47 (1991).
    • (1991) Biochim. Biophys. Acta , vol.118 , pp. 41-47
    • Lin, S.F.1    Yang, T.Y.2    Inukai, T.3    Yamasaki, M.4    Tsai, Y.C.5
  • 12
    • 29144478790 scopus 로고    scopus 로고
    • Structural characterization of glucooligosaccharide oxidase from Acremonium strictum
    • Lee, M. H., Lai, W. L., Lin, S. F., Hsu, C. S., Liaw, S. H., and Tsai, Y. C., Structural characterization of glucooligosaccharide oxidase from Acremonium strictum. Appl. Environ. Microbiol., 71, 8881-8887 (2005).
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 8881-8887
    • Lee, M.H.1    Lai, W.L.2    Lin, S.F.3    Hsu, C.S.4    Liaw, S.H.5    Tsai, Y.C.6
  • 15
    • 33749592763 scopus 로고    scopus 로고
    • FCD1 encoding protein homologous to cellobiose: Quinone oxidoreductase in Fusarium oxysporum
    • Kawabe, M., Yoshida, T., Teraoka, T., and Arie, T., FCD1 encoding protein homologous to cellobiose: quinone oxidoreductase in Fusarium oxysporum. Gene, 382, 100-110 (2006).
    • (2006) Gene , vol.382 , pp. 100-110
    • Kawabe, M.1    Yoshida, T.2    Teraoka, T.3    Arie, T.4
  • 17
    • 78651153791 scopus 로고
    • Disk electrophoresis-II. Method and application to human serum proteins
    • Davis, B. J., Disk electrophoresis-II. Method and application to human serum proteins. Ann. NY Acad. Sci., 121, 404-427 (1964).
    • (1964) Ann. NY Acad. Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0029928876 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium
    • Li, B., Nagalla, S. R., and Renganathan, V., Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium. Appl. Environ. Microbiol., 62, 1329-1335 (1996).
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 1329-1335
    • Li, B.1    Nagalla, S.R.2    Renganathan, V.3
  • 21
    • 0034629232 scopus 로고    scopus 로고
    • A critical review of cellobiose dehydrogenase
    • Henriksson, G., Johansson, G., and Pettersson, G., A critical review of cellobiose dehydrogenase. J. Biotechnol., 78, 93-113 (2000).
    • (2000) J. Biotechnol , vol.78 , pp. 93-113
    • Henriksson, G.1    Johansson, G.2    Pettersson, G.3
  • 22
    • 0342953000 scopus 로고
    • Enzymic formation of lactobionic acid from lactose
    • Nishizuka, Y., and Hayaishi, O., Enzymic formation of lactobionic acid from lactose. J. Biol. Chem., 237, 2721-2728 (1962).
    • (1962) J. Biol. Chem , vol.237 , pp. 2721-2728
    • Nishizuka, Y.1    Hayaishi, O.2
  • 23
    • 0035931413 scopus 로고    scopus 로고
    • Continuous enzymatic regeneration of redox mediators used in biotransformation reactions employing flavoprotein
    • Baminger, U., Ludwig, R., Galhaup, C., Leitner, C., Kulbe, K. D., and Haltrich, D., Continuous enzymatic regeneration of redox mediators used in biotransformation reactions employing flavoprotein. J. Mol. Cat. B, 11, 541-550 (2001).
    • (2001) J. Mol. Cat. B , vol.11 , pp. 541-550
    • Baminger, U.1    Ludwig, R.2    Galhaup, C.3    Leitner, C.4    Kulbe, K.D.5    Haltrich, D.6
  • 24
    • 3042627355 scopus 로고    scopus 로고
    • Continuous enzymatic regeneration of electron acceptor used by flavoenzymes: Cellobiose dehydrogenase-catalyzed production of lactobionic acid as an example
    • Ludwig, R., Ozga, M., Zamocky, M., Peterbauer, C., Kulbe, K. D., and Haltrich, D., Continuous enzymatic regeneration of electron acceptor used by flavoenzymes: cellobiose dehydrogenase-catalyzed production of lactobionic acid as an example. Biocat. Biotrans., 22, 97-104 (2004).
    • (2004) Biocat. Biotrans , vol.22 , pp. 97-104
    • Ludwig, R.1    Ozga, M.2    Zamocky, M.3    Peterbauer, C.4    Kulbe, K.D.5    Haltrich, D.6
  • 25
    • 0031463294 scopus 로고    scopus 로고
    • Continuous enzymatic production of lactobionic acid using glucose-fructose oxidoreductase in ultrafiltration membrane reactor
    • Satory, M., Furlinger, M., Haltrich, D., Kulbe, K. D., Pittner, F., and Nidetzky, B., Continuous enzymatic production of lactobionic acid using glucose-fructose oxidoreductase in ultrafiltration membrane reactor. Biotechnol. Lett., 19, 1205-1208 (1997).
    • (1997) Biotechnol. Lett , vol.19 , pp. 1205-1208
    • Satory, M.1    Furlinger, M.2    Haltrich, D.3    Kulbe, K.D.4    Pittner, F.5    Nidetzky, B.6
  • 26
    • 0028169897 scopus 로고
    • 1H NMR evidence for conversion of β-cellobiose dehydrogenase from Phanerochaete chrysosporium
    • 1H NMR evidence for conversion of β-cellobiose dehydrogenase from Phanerochaete chrysosporium. FEBS Lett., 351, 128-132 (1994).
    • (1994) FEBS Lett , vol.351 , pp. 128-132
    • Higham, C.W.1    Gordon-Smith, D.2    Dempsey, C.E.3    Woos, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.