메뉴 건너뛰기




Volumn 5, Issue 11, 2010, Pages 1192-1197

Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial applications

Author keywords

Biocatalysis; Cross linked enzyme aggregate; Enzyme immobilization; Sucrose phosphorylase; Thermostability

Indexed keywords

BIFIDOBACTERIUM ADOLESCENTIS; BIOCATALYSIS; COMMERCIAL POTENTIAL; CONSECUTIVE REACTION; CROSS-LINKED ENZYME AGGREGATES; DONOR SUBSTRATES; IMMOBILIZED ENZYME; MICROBIAL CONTAMINATION; SMALL MOLECULES; SOLUBLE ENZYMES; SUCROSE PHOSPHORYLASE; THERMAL STABILITY; THERMOSTABILITY;

EID: 78349258236     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201000202     Document Type: Article
Times cited : (41)

References (30)
  • 1
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: The quest for optimum performance.
    • Sheldon, R. A., Enzyme immobilization: The quest for optimum performance. Adv. Synth. Catal. 2007, 349, 1289-1307.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 2
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilisation.
    • Brady, D., Jordaan, J., Advances in enzyme immobilisation. Biotechnol. Lett. 2009, 31, 1639-1650.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 4
    • 0041528514 scopus 로고    scopus 로고
    • Immobilizing enzymes: How to create more suitable biocatalysts.
    • Bornscheuer, U. T., Immobilizing enzymes: How to create more suitable biocatalysts. Angew. Chem. Int. Ed. 2003, 42, 3336-3337.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 3336-3337
    • Bornscheuer, U.T.1
  • 5
    • 0034682159 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates: A simple and effective method for the immobilization of penicillin acylase.
    • Cao, L. Q., van Rantwijk, F., Sheldon, R. A., Cross-linked enzyme aggregates: A simple and effective method for the immobilization of penicillin acylase. Org. Lett. 2000, 2, 1361-1364.
    • (2000) Org. Lett. , vol.2 , pp. 1361-1364
    • Cao, L.Q.1    van Rantwijk, F.2    Sheldon, R.A.3
  • 7
    • 0033179684 scopus 로고    scopus 로고
    • Immobilized enzymes: Crystals or carriers?
    • Tischer, W., Kasche, V., Immobilized enzymes: Crystals or carriers? Trends Biotechnol. 1999, 17, 326-335.
    • (1999) Trends Biotechnol. , vol.17 , pp. 326-335
    • Tischer, W.1    Kasche, V.2
  • 8
    • 1942517812 scopus 로고    scopus 로고
    • Crosslinked enzyme crystals of glucoamylase as a potent catalyst for biotransformations.
    • Abraham, T. E., Joseph, J. R., Bindhu, L. B. V., Jayakumar, K. K., Crosslinked enzyme crystals of glucoamylase as a potent catalyst for biotransformations. Carbohydr. Res. 2004, 339, 1099-1104.
    • (2004) Carbohydr. Res. , vol.339 , pp. 1099-1104
    • Abraham, T.E.1    Joseph, J.R.2    Bindhu, L.B.V.3    Jayakumar, K.K.4
  • 9
    • 33745221455 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding the sucrose phosphorylase from Leuconostoc mesenteroides B-1149 and the expression in
    • Lee, J. H., Yoon, S. H., Nam, S. H., Moon, Y. H. et al., 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) Escherichia coli. Enzyme Microb. Technol. , vol.39 , pp. 612-620
    • Lee, J.H.1    Yoon, S.H.2    Nam, S.H.3    Moon, Y.H.4
  • 10
    • 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
  • 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
    • 0842283893 scopus 로고    scopus 로고
    • Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis.
    • Sprogoe, D., van den Broek, L. A. M., Mirza, O., Kastrup, J. S. et al., Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis. Biochemistry 2004, 43, 1156-1162.
    • (2004) Biochemistry , vol.43 , pp. 1156-1162
    • Sprogoe, D.1    van den Broek, L.A.M.2    Mirza, O.3    Kastrup, J.S.4
  • 13
    • 0026736384 scopus 로고
    • Enzymatic assay of inorganic phosphate with use of sucrose phosphorylase and phosphoglucomutase.
    • Tedokon, M., Suzuki, K., Kayamori, Y., Fujita, S. et al., 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
  • 14
    • 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
  • 15
    • 33947188005 scopus 로고    scopus 로고
    • Recombinant sucrose phosphorylase fromLeuconostoc 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 fromLeuconostoc 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
  • 16
    • 0000630613 scopus 로고
    • Enzymatic synthesis of 2 stable (-)-epigallocatechin gallate-glucosides by sucrose phosphorylase.
    • Kitao, S., Matsudo, T., Saitoh, M., Horiuchi, T. et al., 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
  • 17
    • 70349808079 scopus 로고    scopus 로고
    • Single-step enzymatic synthesis of (R)-2-O-alpha-D-glucopyranosyl glycerate, a compatible solute from micro-organisms that functions as a protein stabiliser.
    • Sawangwan, T., Goedl, C., Nidetzky, B., Single-step enzymatic synthesis of (R)-2-O-alpha-D-glucopyranosyl glycerate, a compatible solute from micro-organisms that functions as a protein stabiliser. Org. Biomol. Chem. 2009, 7, 4267-4270.
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 4267-4270
    • Sawangwan, T.1    Goedl, C.2    Nidetzky, B.3
  • 18
    • 57749102704 scopus 로고    scopus 로고
    • A high-yielding biocatalytic process for the production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient.
    • Goedl, C., Sawangwan, T., Mueller, M., Schwarz, A. et al., A high-yielding biocatalytic process for the production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient. Angew. Chem. Int. Ed. 2008, 47, 10086-10089.
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 10086-10089
    • Goedl, C.1    Sawangwan, T.2    Mueller, M.3    Schwarz, A.4
  • 19
    • 74549196321 scopus 로고    scopus 로고
    • Sucrose phosphorylase: A powerful transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals.
    • Goedl, C., Sawangwan, T., Wildberger, P., Nidetzky, B., Sucrose phosphorylase: A powerful transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals. Biocatal. Biotransformation 2010, 28, 10-21.
    • (2010) Biocatal. Biotransformation , vol.28 , pp. 10-21
    • Goedl, C.1    Sawangwan, T.2    Wildberger, P.3    Nidetzky, B.4
  • 20
    • 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
  • 21
    • 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
  • 23
    • 34547471980 scopus 로고    scopus 로고
    • Construction and model-based analysis of a promoter library for E. coli: An indispensable tool for metabolic engineering.
    • De Mey, M., Maertens, J., Lequeux, G. J., Soetaert, W. K. et al., Construction and model-based analysis of a promoter library for E. coli: An indispensable tool for metabolic engineering. BCM Biotechnol. 2007, 18, 34-39.
    • (2007) BCM Biotechnol. , vol.18 , pp. 34-39
    • De Mey, M.1    Maertens, J.2    Lequeux, G.J.3    Soetaert, W.K.4
  • 24
    • 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
  • 25
    • 34250489053 scopus 로고
    • Wielinge, H, Properties of a new chromogen for determination of glucose in blood according to god/pod-method.
    • Werner, W., Rey, H. G., Wielinge, H, Properties of a new chromogen for determination of glucose in blood according to god/pod-method. Z. Anal. Chem. 1970, 252, 224.
    • (1970) Z. Anal. Chem. , vol.252 , pp. 224
    • Werner, W.1    Rey, H.G.2
  • 26
    • 58249140161 scopus 로고    scopus 로고
    • Effect of the degree of cross-linking on the properties of different CLEAs of penicillin acylase.
    • Wilson, L., Manes, A., Soler, L., Henriquez, M. J., Effect of the degree of cross-linking on the properties of different CLEAs of penicillin acylase. Process Biochem. 2009, 44, 322-326.
    • (2009) Process Biochem. , vol.44 , pp. 322-326
    • Wilson, L.1    Manes, A.2    Soler, L.3    Henriquez, M.J.4
  • 27
    • 2342420355 scopus 로고    scopus 로고
    • A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates.
    • Mateo, C., Palomo, J. M., van Langen, L. M., van Rantwijk, F. et al., A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates. Biotechnol. Bioeng. 2004, 86, 273-276.
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 273-276
    • Mateo, C.1    Palomo, J.M.2    van Langen, L.M.3    van Rantwijk, F.4
  • 28
    • 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
  • 29
    • 37749025783 scopus 로고    scopus 로고
    • Advances in the design of new epoxy supports for enzyme immobilization-stabilization.
    • Mateo, C., Grazu, V., Pessela, B. C. C., Montes, T. et al., Advances in the design of new epoxy supports for enzyme immobilization-stabilization. Biochem. Soc. Trans. 2007, 35, 1593-1601.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1593-1601
    • Mateo, C.1    Grazu, V.2    Pessela, B.C.C.3    Montes, T.4
  • 30
    • 78349282892 scopus 로고    scopus 로고
    • A constitutive expression system for high-throughput screening.
    • DOI: 10.1002/elsc.201000065
    • Aerts, D., Verhaeghe, T., De Mey, M., Desnet, T., Soetaert, N. et al., A constitutive expression system for high-throughput screening. Eng. Life Sci. 2010, DOI: 10.1002/elsc.201000065
    • (2010) Eng. Life Sci.
    • Aerts, D.1    Verhaeghe, T.2    De Mey, M.3    Desnet, T.4    Soetaert, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.