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Volumn 130, Issue 1, 2007, Pages 67-74

A novel variant of Thermotoga neapolitana β-glucosidase B is an efficient catalyst for the synthesis of alkyl glucosides by transglycosylation

Author keywords

Glucosidase; Alkyl glycosides; Biosynthesis; Glycoside hydrolase family 3; Thermostable enzyme

Indexed keywords

ALKYL GLUCOSIDES; THERMOSTABLE ENZYMES; THERMOSTABLE VARIANTS; TRANSGLYCOSYLATION;

EID: 34247375264     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.02.016     Document Type: Article
Times cited : (66)

References (29)
  • 1
    • 0031554925 scopus 로고    scopus 로고
    • Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability
    • Aguilar C.F., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M., and Pearl L.H. Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J. Mol. Biol. 271 (1997) 789-802
    • (1997) J. Mol. Biol. , vol.271 , pp. 789-802
    • Aguilar, C.F.1    Sanderson, I.2    Moracci, M.3    Ciaramella, M.4    Nucci, R.5    Rossi, M.6    Pearl, L.H.7
  • 2
    • 0035816504 scopus 로고    scopus 로고
    • A kinetic study of almond-β-glucosidase catalysed synthesis of hexyl-glycosides in low aqueous media influence of glycosyl donor and water activity
    • Andersson M., and Adlercreutz P. A kinetic study of almond-β-glucosidase catalysed synthesis of hexyl-glycosides in low aqueous media influence of glycosyl donor and water activity. J. Mol. Catal. B: Enzym. 14 (2001) 69-76
    • (2001) J. Mol. Catal. B: Enzym. , vol.14 , pp. 69-76
    • Andersson, M.1    Adlercreutz, P.2
  • 3
    • 0037060960 scopus 로고    scopus 로고
    • Synthesis of octyl glucopyranoside by almond β-glucosidase adsorbed onto Celite R-640
    • Basso A., Ducret A., Gardossi L., and Lortie R. Synthesis of octyl glucopyranoside by almond β-glucosidase adsorbed onto Celite R-640. Tetrahedron Lett. 43 (2002) 2005-2008
    • (2002) Tetrahedron Lett. , vol.43 , pp. 2005-2008
    • Basso, A.1    Ducret, A.2    Gardossi, L.3    Lortie, R.4
  • 4
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: an integrated database approach
    • Gilbert H.J., Davies G., Henrissat B., and Svensson B. (Eds), The Royal Society of Chemistry, Cambridge
    • Coutinho P.M., and Henrissat B. Carbohydrate-active enzymes: an integrated database approach. In: Gilbert H.J., Davies G., Henrissat B., and Svensson B. (Eds). Recent Advances in Carbohydrate Bioengineering (1999), The Royal Society of Chemistry, Cambridge 3-12
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 5
    • 0032125968 scopus 로고    scopus 로고
    • A xyloglucan oligosaccharide-active, transglycosylating β-d-glucosidase from the cotyledons of nasturtium (Tropaeolum majus L.) seedlings: purification, properties and characterization of a cDNA clone
    • Crombie H.J., Chengappa S., Hellyer A., and Reid J.S.G. A xyloglucan oligosaccharide-active, transglycosylating β-d-glucosidase from the cotyledons of nasturtium (Tropaeolum majus L.) seedlings: purification, properties and characterization of a cDNA clone. Plant J. 15 (1998) 27-38
    • (1998) Plant J. , vol.15 , pp. 27-38
    • Crombie, H.J.1    Chengappa, S.2    Hellyer, A.3    Reid, J.S.G.4
  • 6
    • 24044490195 scopus 로고    scopus 로고
    • A cultivation technique for E. coli fed-batch cultivations operating close to the maximum oxygen transfer capacity of the reactor
    • de Maré L., Velut S., Ledung E., Cimander C., Norrman B., Karlsson E.N., Hoist O., and Hagander P. A cultivation technique for E. coli fed-batch cultivations operating close to the maximum oxygen transfer capacity of the reactor. Biotechnol. Lett. 27 (2005) 983-990
    • (2005) Biotechnol. Lett. , vol.27 , pp. 983-990
    • de Maré, L.1    Velut, S.2    Ledung, E.3    Cimander, C.4    Norrman, B.5    Karlsson, E.N.6    Hoist, O.7    Hagander, P.8
  • 7
    • 0036204403 scopus 로고    scopus 로고
    • The family-3 glycoside hydrolases: from housekeeping functions to host-microbe interactions
    • Faure D. The family-3 glycoside hydrolases: from housekeeping functions to host-microbe interactions. Appl. Environ. Microbiol. 68 (2002) 1485-1490
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1485-1490
    • Faure, D.1
  • 8
    • 0035965060 scopus 로고    scopus 로고
    • Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity
    • Goyal K., Selvakumar P., and Hayashi K. Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J. Mol. Catal. B: Enzym. 15 (2001) 45-53
    • (2001) J. Mol. Catal. B: Enzym. , vol.15 , pp. 45-53
    • Goyal, K.1    Selvakumar, P.2    Hayashi, K.3
  • 9
    • 0034054726 scopus 로고    scopus 로고
    • The crystal structure of β-glucosidase from Bacillus circulans sp. alkalophilus: ability to form long polymeric assemblies
    • Hakulinen N., Paavilainen S., Korpela T., and Rouvinen J. The crystal structure of β-glucosidase from Bacillus circulans sp. alkalophilus: ability to form long polymeric assemblies. J. Struct. Biol. 129 (2000) 69-79
    • (2000) J. Struct. Biol. , vol.129 , pp. 69-79
    • Hakulinen, N.1    Paavilainen, S.2    Korpela, T.3    Rouvinen, J.4
  • 10
    • 0035924115 scopus 로고    scopus 로고
    • Enhanced transglucosylation/hydrolysis ratio of mutants of Pyrococcus furiosus β-glucosidase: effects of donor concentration, water content, and temperature on activity and selectivity in hexanol
    • Hansson T., and Adlercreutz P. Enhanced transglucosylation/hydrolysis ratio of mutants of Pyrococcus furiosus β-glucosidase: effects of donor concentration, water content, and temperature on activity and selectivity in hexanol. Biotechnol. Bioeng. 75 (2001) 656-665
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 656-665
    • Hansson, T.1    Adlercreutz, P.2
  • 11
    • 0035813475 scopus 로고    scopus 로고
    • Influence of water activity on the competition between β-glycosidase-catalysed transglycosylation and hydrolysis in aqueous hexanol
    • Hansson T., Andersson M., Wehtje E., and Adlercreutz P. Influence of water activity on the competition between β-glycosidase-catalysed transglycosylation and hydrolysis in aqueous hexanol. Enzyme Microb. Technol. 29 (2001) 527-534
    • (2001) Enzyme Microb. Technol. , vol.29 , pp. 527-534
    • Hansson, T.1    Andersson, M.2    Wehtje, E.3    Adlercreutz, P.4
  • 12
    • 9944239242 scopus 로고    scopus 로고
    • Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1,3)-β-glucosidase from the white-rot fungus Phanerochaete chrysosporium
    • Kawai R., Igarashi K., Kitaoka M., Ishii T., and Samejima M. Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1,3)-β-glucosidase from the white-rot fungus Phanerochaete chrysosporium. Carbohydr. Res. 339 (2004) 2851-2857
    • (2004) Carbohydr. Res. , vol.339 , pp. 2851-2857
    • Kawai, R.1    Igarashi, K.2    Kitaoka, M.3    Ishii, T.4    Samejima, M.5
  • 13
    • 0034736427 scopus 로고    scopus 로고
    • Synthesis of alkyl glycosides through β-glucosidase-catalyzed condensation in an aqueous-organic biphasic system and estimation of the equilibrium constants for their formation
    • Kobayashi T., Adachi S., Nakanishi K., and Matsuno R. Synthesis of alkyl glycosides through β-glucosidase-catalyzed condensation in an aqueous-organic biphasic system and estimation of the equilibrium constants for their formation. J. Mol. Catal. B: Enzym. 11 (2000) 13-21
    • (2000) J. Mol. Catal. B: Enzym. , vol.11 , pp. 13-21
    • Kobayashi, T.1    Adachi, S.2    Nakanishi, K.3    Matsuno, R.4
  • 14
    • 0035733162 scopus 로고    scopus 로고
    • Synthesis of alkyl glycosides by β-glucosidases in a system of reverse micelles
    • Kouptsova O.S., Klyachko N.L., and Levashov A.V. Synthesis of alkyl glycosides by β-glucosidases in a system of reverse micelles. Russ. J. Bioorganic Chem. 27 (2001) 380-384
    • (2001) Russ. J. Bioorganic Chem. , vol.27 , pp. 380-384
    • Kouptsova, O.S.1    Klyachko, N.L.2    Levashov, A.V.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 16
    • 0028166876 scopus 로고
    • Enzymatic synthesis of octyl-β-glucoside in octanol at controlled water activity
    • Ljunger G., Adlercreutz P., and Mattiasson B. Enzymatic synthesis of octyl-β-glucoside in octanol at controlled water activity. Enzyme Microb. Technol. 16 (1994) 751-755
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 751-755
    • Ljunger, G.1    Adlercreutz, P.2    Mattiasson, B.3
  • 17
    • 0036729340 scopus 로고    scopus 로고
    • Enzymatic properties and intracellular localization of the novel Trichoderma reesei β-glucosidase BGLII (CellA)
    • Saloheimo M., Kuja-Panula J., Ylösmäki E., Ward M., and Penttilä M. Enzymatic properties and intracellular localization of the novel Trichoderma reesei β-glucosidase BGLII (CellA). Appl. Environ. Microbiol. 68 (2002) 4546-4553
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4546-4553
    • Saloheimo, M.1    Kuja-Panula, J.2    Ylösmäki, E.3    Ward, M.4    Penttilä, M.5
  • 18
    • 0032559380 scopus 로고    scopus 로고
    • Crystal structure of β-glucosidase A from Bacilluspolymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases
    • Sanz-Aparicio J., Hermoso J.A., Martínez-Ripoll M., Lequerica J.L., and Polaina J. Crystal structure of β-glucosidase A from Bacilluspolymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases. J. Mol. Biol. 275 (1998) 491-502
    • (1998) J. Mol. Biol. , vol.275 , pp. 491-502
    • Sanz-Aparicio, J.1    Hermoso, J.A.2    Martínez-Ripoll, M.3    Lequerica, J.L.4    Polaina, J.5
  • 19
    • 17744362070 scopus 로고    scopus 로고
    • Transglucosidic reactions of the Aspergillus niger family 3 β-glucosidase: qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH
    • Seidle H.F., and Huber R.E. Transglucosidic reactions of the Aspergillus niger family 3 β-glucosidase: qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH. Arch. Biochem. Biophys. 436 (2005) 254-264
    • (2005) Arch. Biochem. Biophys. , vol.436 , pp. 254-264
    • Seidle, H.F.1    Huber, R.E.2
  • 20
    • 1842588421 scopus 로고    scopus 로고
    • Transglycosylation catalyzed by almond β-glucosidase and cloned Pichia etchellsii β-glucosidase II using glycosylasparagine mimetics as novel acceptors
    • Thanukrishnan K., Loganathan D., Bhatia Y., Mishra S., and Bisaria V.S. Transglycosylation catalyzed by almond β-glucosidase and cloned Pichia etchellsii β-glucosidase II using glycosylasparagine mimetics as novel acceptors. Biocatal. Biotransfor. 22 (2004) 1-7
    • (2004) Biocatal. Biotransfor. , vol.22 , pp. 1-7
    • Thanukrishnan, K.1    Loganathan, D.2    Bhatia, Y.3    Mishra, S.4    Bisaria, V.S.5
  • 22
    • 10644275363 scopus 로고    scopus 로고
    • Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration
    • Turner P., Hoist O., and Nordberg Karlsson E. Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration. Protein Expr. Purif. 39 (2005) 54-60
    • (2005) Protein Expr. Purif. , vol.39 , pp. 54-60
    • Turner, P.1    Hoist, O.2    Nordberg Karlsson, E.3
  • 24
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley β-d-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese J.N., Hrmova M., and Fincher G.B. Three-dimensional structure of a barley β-d-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 7 (1999) 179-190
    • (1999) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 25
    • 0029593613 scopus 로고
    • Synthesis of allyl and benzyl β-d-glucopyranosides, and allyl β-d-galactopyranoside from d-glucose or d-galactose and the corresponding alcohol using almond β-d-glucosidase
    • Vic G., and Crout D.H.G. Synthesis of allyl and benzyl β-d-glucopyranosides, and allyl β-d-galactopyranoside from d-glucose or d-galactose and the corresponding alcohol using almond β-d-glucosidase. Carbohydr. Res. 279 (1995) 315-319
    • (1995) Carbohydr. Res. , vol.279 , pp. 315-319
    • Vic, G.1    Crout, D.H.G.2
  • 26
    • 0032486443 scopus 로고    scopus 로고
    • Alkyl polyglycosides: properties and applications of a new class of surfactants
    • von Rybinski W., and Hill K. Alkyl polyglycosides: properties and applications of a new class of surfactants. Angew. Chem. Int. Ed. 37 (1998) 1328-1345
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 1328-1345
    • von Rybinski, W.1    Hill, K.2
  • 27
    • 0031834858 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens β-glucosidase us also and effective β-xylosidase, and has a high transglycosylation activity in the presence of alcohols
    • Watt D.K., Ono H., and Hayashi K. Agrobacterium tumefaciens β-glucosidase us also and effective β-xylosidase, and has a high transglycosylation activity in the presence of alcohols. Biochim. Biophys. Acta 1385 (1998) 78-88
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 78-88
    • Watt, D.K.1    Ono, H.2    Hayashi, K.3
  • 28
    • 0344012180 scopus 로고    scopus 로고
    • Iminosugar glycosidase inhibitors: structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycinto β-glucosidases
    • Zechel D.L., Boraston A.B., Gloster T., Boraston C.M., Macdonald J.M., Tilbrook D.M.G., Stick R.V., and Davies G. Iminosugar glycosidase inhibitors: structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycinto β-glucosidases. J. Am. Chem. Soc. 125 (2003) 14313-14323
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14313-14323
    • Zechel, D.L.1    Boraston, A.B.2    Gloster, T.3    Boraston, C.M.4    Macdonald, J.M.5    Tilbrook, D.M.G.6    Stick, R.V.7    Davies, G.8
  • 29
    • 0030680965 scopus 로고    scopus 로고
    • Thermotoga neapolitana bglB gene, upstream of lamA, encodes a highly thermostable β-glucosidase that is a laminaribiase
    • Zverlov V.V., Volkov I.Y., Vehkodvorskaya T.V., and Schwarz W.H. Thermotoga neapolitana bglB gene, upstream of lamA, encodes a highly thermostable β-glucosidase that is a laminaribiase. Microbiology 143 (1997) 3537-3542
    • (1997) Microbiology , vol.143 , pp. 3537-3542
    • Zverlov, V.V.1    Volkov, I.Y.2    Vehkodvorskaya, T.V.3    Schwarz, W.H.4


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