메뉴 건너뛰기




Volumn 150, Issue 1, 2010, Pages 125-130

Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization

Author keywords

BCA (reducing sugars); Immobilisation; Sepabeads; Sucrose phosphorylase; Thermostability

Indexed keywords

IMMOBILISATION; REDUCING SUGARS; SEPABEADS; SUCROSE PHOSPHORYLASE; THERMOSTABILITY;

EID: 77957367702     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.07.029     Document Type: Article
Times cited : (41)

References (34)
  • 1
    • 78349282892 scopus 로고    scopus 로고
    • in press. Development of a constitutive expression system for 'minimal pipetting high throughput screening' (mpHTS). Eng. Life Sci. doi:10.1002/elsc.201000065
    • Aerts, D., Verhaeghe, T., De Mey, M., Desmet, T., Soetaert, W., in press. Development of a constitutive expression system for 'minimal pipetting high throughput screening' (mpHTS). Eng. Life Sci. doi:10.1002/elsc.201000065.
    • Aerts, D.1    Verhaeghe, T.2    De Mey, M.3    Desmet, T.4    Soetaert, W.5
  • 4
    • 0021737963 scopus 로고
    • A one-step enzymatic assay for sucrose with sucrose phosphorylase
    • Birnberg P.R., Brenner M.L. A one-step enzymatic assay for sucrose with sucrose phosphorylase. Anal. Biochem. 1984, 142:556-561.
    • (1984) Anal. Biochem. , vol.142 , pp. 556-561
    • Birnberg, P.R.1    Brenner, M.L.2
  • 5
  • 6
    • 0035104931 scopus 로고    scopus 로고
    • Thermozymes and their applications-a review of recent literature and patents
    • Bruins M.E., Janssen A.E.M., Boom R.M. Thermozymes and their applications-a review of recent literature and patents. Appl. Biochem. Biotechnol. 2001, 90:155-186.
    • (2001) Appl. Biochem. Biotechnol. , vol.90 , pp. 155-186
    • Bruins, M.E.1    Janssen, A.E.M.2    Boom, R.M.3
  • 7
    • 0028172607 scopus 로고
    • Can immobilization be exploited to modify enzyme-activity
    • Clark D.S. Can immobilization be exploited to modify enzyme-activity. Trends Biotechnol. 1994, 12:439-443.
    • (1994) Trends Biotechnol. , vol.12 , pp. 439-443
    • Clark, D.S.1
  • 9
    • 33747265618 scopus 로고    scopus 로고
    • Enhancing the thermal stability of sucrose phosphorylase from Streptococcus mutans by random mutagenesis
    • Fujii K., Liboshi M., Yanase M., Takaha T., Kuriki T. Enhancing the thermal stability of sucrose phosphorylase from Streptococcus mutans by random mutagenesis. J. Appl. Glycosci. 2006, 53:91-97.
    • (2006) J. Appl. Glycosci. , vol.53 , pp. 91-97
    • Fujii, K.1    Liboshi, M.2    Yanase, M.3    Takaha, T.4    Kuriki, T.5
  • 11
    • 70350538953 scopus 로고    scopus 로고
    • Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate
    • Goedl C, Nidetzky B. Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate. Chembiochem 2009, 10:2333-2337.
    • (2009) Chembiochem , vol.10 , pp. 2333-2337
    • Goedl, C.1    Nidetzky, B.2
  • 12
    • 33947188005 scopus 로고    scopus 로고
    • Recombinant sucrose phosphorylase from Leuconostoc mesenteroides: characterization, kinetic studies of transglucosylation, and application of immobilised enzyme for production of alpha-d-glucose 1-phosphate
    • Goedl C., Schwarz A., Minani A., Nidetzky B. Recombinant sucrose phosphorylase from Leuconostoc mesenteroides: characterization, kinetic studies of transglucosylation, and application of immobilised enzyme for production of alpha-d-glucose 1-phosphate. J. Biotechnol. 2007, 129:77-86.
    • (2007) J. Biotechnol. , vol.129 , pp. 77-86
    • Goedl, C.1    Schwarz, A.2    Minani, A.3    Nidetzky, B.4
  • 13
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino-acid-sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino-acid-sequence similarities. Biochem. J. 1991, 280:309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 15
    • 0034274420 scopus 로고    scopus 로고
    • Eupergit (R) C, a carrier for immobilization of enzymes of industrial potential
    • Katchalski-Katzir E., Kraemer D.M. Eupergit (R) C, a carrier for immobilization of enzymes of industrial potential. J. Mol. Catal. B: Enzym. 2000, 10:157-176.
    • (2000) J. Mol. Catal. B: Enzym. , vol.10 , pp. 157-176
    • Katchalski-Katzir, E.1    Kraemer, D.M.2
  • 16
    • 0000630613 scopus 로고
    • Enzymatic synthesis of 2 stable (-)-epigallocatechin gallate-glucosides by sucrose phosphorylase
    • Kitao S., Matsudo T., Saitoh M., Horiuchi T., Sekine H. Enzymatic synthesis of 2 stable (-)-epigallocatechin gallate-glucosides by sucrose phosphorylase. Biosci. Biotechnol. Biochem. 1995, 59:2167-2169.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 2167-2169
    • Kitao, S.1    Matsudo, T.2    Saitoh, M.3    Horiuchi, T.4    Sekine, H.5
  • 17
    • 0026183697 scopus 로고
    • Purification and some properties of sucrose phosphorylase from Leuconostoc mesenteroides
    • Koga T., Nakamura K., Shirokane Y., Mizusawa K., Kitao S., Kikuchi M. Purification and some properties of sucrose phosphorylase from Leuconostoc mesenteroides. Agr. Biol. Chem. 1991, 55:1805-1810.
    • (1991) Agr. Biol. Chem. , vol.55 , pp. 1805-1810
    • Koga, T.1    Nakamura, K.2    Shirokane, Y.3    Mizusawa, K.4    Kitao, S.5    Kikuchi, M.6
  • 18
    • 33745221455 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding the sucrose phosphorylase from Leuconostoc mesenteroides B-1149 and the expression in Escherichia coli
    • Lee J.H., Yoon S.H., Nam S.H., Moon Y.H., Moon Y.Y., Kim D. Molecular cloning of a gene encoding the sucrose phosphorylase from Leuconostoc mesenteroides B-1149 and the expression in Escherichia coli. Enzyme Microb. Technol. 2006, 39:612-620.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 612-620
    • Lee, J.H.1    Yoon, S.H.2    Nam, S.H.3    Moon, Y.H.4    Moon, Y.Y.5    Kim, D.6
  • 21
    • 0035988098 scopus 로고    scopus 로고
    • Epoxy sepabeads: a novel epoxy support for stabilization of industrial enzymes via very intense multipoint covalent attachment
    • Mateo C., Abian O., Fernandez-Lorente G., Pedroche J., Fernandez-Lafuente R., Guisan J.M. Epoxy sepabeads: a novel epoxy support for stabilization of industrial enzymes via very intense multipoint covalent attachment. Biotechnol. Prog. 2002, 18:629-634.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 629-634
    • Mateo, C.1    Abian, O.2    Fernandez-Lorente, G.3    Pedroche, J.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 22
    • 0141841817 scopus 로고    scopus 로고
    • Enzymatic transformations. Immobilized A-niger epoxide hydrolase as a novel biocatalytic tool for repeated-batch hydrolytic kinetic resolution of epoxides
    • Mateo C., Archelas A., Fernandez-Lafuente R., Guisan J.M., Furstoss R. Enzymatic transformations. Immobilized A-niger epoxide hydrolase as a novel biocatalytic tool for repeated-batch hydrolytic kinetic resolution of epoxides. Org. Biomol. Chem. 2003, 1:2739-2743.
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 2739-2743
    • Mateo, C.1    Archelas, A.2    Fernandez-Lafuente, R.3    Guisan, J.M.4    Furstoss, R.5
  • 25
    • 0014216416 scopus 로고
    • Purification and mechanism of action of sucrose phosphorylase
    • Silverstein R., Voet J., Reed D., Abeles R.H. Purification and mechanism of action of sucrose phosphorylase. J. Biol. Chem. 1967, 242:1338-1346.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1338-1346
    • Silverstein, R.1    Voet, J.2    Reed, D.3    Abeles, R.H.4
  • 27
    • 0026736384 scopus 로고
    • Enzymatic assay of inorganic phosphate with use of sucrose phosphorylase and phosphoglucomutase
    • Tedokon M., Suzuki K., Kayamori Y., Fujita S., Katayama Y. Enzymatic assay of inorganic phosphate with use of sucrose phosphorylase and phosphoglucomutase. Clin. Chem. 1992, 38:512-515.
    • (1992) Clin. Chem. , vol.38 , pp. 512-515
    • Tedokon, M.1    Suzuki, K.2    Kayamori, Y.3    Fujita, S.4    Katayama, Y.5
  • 28
    • 0038458838 scopus 로고    scopus 로고
    • A novel heterofunctional epoxy-amino sepabeads for a new enzyme immobilization protocol: immobilization-stabilization of beta-galactosidase from Aspergillus oryzae
    • Torres R., Mateo C., Fernandez-Lorente G., Ortiz C., Fuentes M., Palomo J.M., Guisan J.M., Fernandez-Lafuente R. A novel heterofunctional epoxy-amino sepabeads for a new enzyme immobilization protocol: immobilization-stabilization of beta-galactosidase from Aspergillus oryzae. Biotechnol. Prog. 2003, 19:1056-1060.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1056-1060
    • Torres, R.1    Mateo, C.2    Fernandez-Lorente, G.3    Ortiz, C.4    Fuentes, M.5    Palomo, J.M.6    Guisan, J.M.7    Fernandez-Lafuente, R.8
  • 30
    • 34547747311 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes-stability, activity and implementation strategies for high temperature applications
    • Unsworth L.D., van der Oost J., Koutsopoulos S. Hyperthermophilic enzymes-stability, activity and implementation strategies for high temperature applications. FEBS J. 2007, 274:4044-4056.
    • (2007) FEBS J. , vol.274 , pp. 4044-4056
    • Unsworth, L.D.1    van der Oost, J.2    Koutsopoulos, S.3
  • 32
    • 0029893110 scopus 로고    scopus 로고
    • Thermozymes: Identifying molecular determinants of protein structural and functional stability
    • Vieille C., Zeikus J.G. Thermozymes: Identifying molecular determinants of protein structural and functional stability. Trends Biotechnol. 1996, 14:183-190.
    • (1996) Trends Biotechnol. , vol.14 , pp. 183-190
    • Vieille, C.1    Zeikus, J.G.2
  • 33
    • 0023406022 scopus 로고
    • Assay of reducing sugars in the nanomole range with 2,2′-bicinchoninate
    • Waffenschmidt S., Jaenicke L. Assay of reducing sugars in the nanomole range with 2,2′-bicinchoninate. Anal. Biochem. 1987, 165:337-340.
    • (1987) Anal. Biochem. , vol.165 , pp. 337-340
    • Waffenschmidt, S.1    Jaenicke, L.2
  • 34
    • 0030867469 scopus 로고    scopus 로고
    • Alpha-1,4-d-glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering
    • Weinhausel A., Griessler R., Krebs A., Zipper P., Haltrich D., Kulbe K.D., Nidetzky B. alpha-1,4-d-glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering. Biochem. J. 1997, 326:773-783.
    • (1997) Biochem. J. , vol.326 , pp. 773-783
    • Weinhausel, A.1    Griessler, R.2    Krebs, A.3    Zipper, P.4    Haltrich, D.5    Kulbe, K.D.6    Nidetzky, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.