메뉴 건너뛰기




Volumn 22, Issue 4, 2002, Pages 375-407

Microbial β-glucosidases: Cloning, properties, and applications

Author keywords

Glycosynthases; Microbial glucosidases; Recombinant glucosidases; Transglycosylation

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CELLS; CRYSTALLOGRAPHY; ENZYMES; POLYSACCHARIDES; YEAST;

EID: 0036448608     PISSN: 07388551     EISSN: None     Source Type: Journal    
DOI: 10.1080/07388550290789568     Document Type: Review
Times cited : (450)

References (132)
  • 1
    • 0023229446 scopus 로고
    • The synthesis of oligosaccharides by the reversed hydrolysis reaction of β-glucosidase at high temperature
    • Ajisaka, K., Nishida, H., and Fujimoto, H. 1987. The synthesis of oligosaccharides by the reversed hydrolysis reaction of β-glucosidase at high temperature. Biotechnol. Lett. 9: 243-248.
    • (1987) Biotechnol. Lett. , vol.9 , pp. 243-248
    • Ajisaka, K.1    Nishida, H.2    Fujimoto, H.3
  • 2
    • 0030023387 scopus 로고    scopus 로고
    • Studies of the activities of lysosomal enzymes in serum and buccal pouch tissue of hamsters during 7, 12-dimethylbenz[a]anthracene induced carcinogenesis
    • Balasubramanian, S., Nagarjun, B., and Govindaswamy, S. 1996. Studies of the activities of lysosomal enzymes in serum and buccal pouch tissue of hamsters during 7, 12-dimethylbenz[a]anthracene induced carcinogenesis. Cancer Lett. 101: 9-14.
    • (1996) Cancer Lett. , vol.101 , pp. 9-14
    • Balasubramanian, S.1    Nagarjun, B.2    Govindaswamy, S.3
  • 3
    • 14744272350 scopus 로고
    • Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates
    • Barnett, C.C., Berka, R.M., and Fowler, T. 1991. Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates. Bio/Technol. 9: 552-567.
    • (1991) Bio/Technol. , vol.9 , pp. 552-567
    • Barnett, C.C.1    Berka, R.M.2    Fowler, T.3
  • 5
    • 0025168749 scopus 로고
    • Molecular biology of cellulose degradation
    • Beguin, P. 1990. Molecular biology of cellulose degradation. Ann Rev. Microbiol. 44: 219-248.
    • (1990) Ann Rev. Microbiol. , vol.44 , pp. 219-248
    • Beguin, P.1
  • 7
    • 0036658176 scopus 로고    scopus 로고
    • Biosynthetic activity of recombinant Escherichia coli expressed Pichia etchellsii β-glucosidase II
    • Bhatia, Y., Mishra, S., and Bisaria, V.S. 2002. Biosynthetic activity of recombinant Escherichia coli expressed Pichia etchellsii β-glucosidase II. Appl. Biochem. Biotechnol. 102-103, 367-369.
    • (2002) Appl. Biochem. Biotechnol. , pp. 102-103
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 8
    • 0024352613 scopus 로고
    • Regulatory aspects of cellulase biosynthesis and secretion
    • Bisaria, V.S. and Mishra, S. 1989. Regulatory aspects of cellulase biosynthesis and secretion. CRC Crit. Rev. Biotechnol. 9: 61-103.
    • (1989) CRC Crit. Rev. Biotechnol. , vol.9 , pp. 61-103
    • Bisaria, V.S.1    Mishra, S.2
  • 11
    • 0026521573 scopus 로고
    • Cloning and sequencing of an Agrobacterium tumefaciens β-glucosidase gene involved in modifying a vir-inducing plant signal molecule
    • Castle, L. A., Smith, K. D., and Morris, R. O. 1992. Cloning and sequencing of an Agrobacterium tumefaciens β-glucosidase gene involved in modifying a vir-inducing plant signal molecule. J. Bacteriol. 174: 1478-1486.
    • (1992) J. Bacteriol. , vol.174 , pp. 1478-1486
    • Castle, L.A.1    Smith, K.D.2    Morris, R.O.3
  • 13
    • 0026581629 scopus 로고
    • Effect of water acivity on enzymatic synthesis of alkyl-glycosides
    • Chahid, Z., Montet, D., Pina, M., and Graille, J. 1992. Effect of water acivity on enzymatic synthesis of alkyl-glycosides. Biotechnol. Lett. 14: 281-284.
    • (1992) Biotechnol. Lett. , vol.14 , pp. 281-284
    • Chahid, Z.1    Montet, D.2    Pina, M.3    Graille, J.4
  • 14
  • 15
    • 0023928782 scopus 로고
    • Inactivation of bovine thrombin by water-soluble carbodiimides: The essential carboxyl group has a pKa of 5.51
    • Chan, V.W.F., Jorgensen, A.M., and Borders, C.L. 1988. Inactivation of bovine thrombin by water-soluble carbodiimides: The essential carboxyl group has a pKa of 5.51. Biochem. Biophys. Res. Commun. 151: 709-716.
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 709-716
    • Chan, V.W.F.1    Jorgensen, A.M.2    Borders, C.L.3
  • 16
    • 0034237786 scopus 로고    scopus 로고
    • Kinetices of inhibition of β-glucosidase from Ampullarium crossean by bromoacetic acid
    • Chen, Q-X., Zhang, Z., Zhou, X-W., and Zhuang, Z-L. 2000. Kinetices of inhibition of β-glucosidase from Ampullarium crossean by bromoacetic acid. Int. J. Biochem. Cell Biol. 32: 717-723.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 717-723
    • Chen, Q.-X.1    Zhang, Z.2    Zhou, X.-W.3    Zhuang, Z.-L.4
  • 17
    • 0028179585 scopus 로고
    • Optimization of β-glucosidase catalysed synthesis of trisaccharides from cellobiose and gentiobiose
    • Christakopoulos, P., Kekos, D., Macris, B.J., Goodenough, P.W., and Bhat, M.K.1994. Optimization of β-glucosidase catalysed synthesis of trisaccharides from cellobiose and gentiobiose. Biotechnol. Lett. 16: 587-592.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 587-592
    • Christakopoulos, P.1    Kekos, D.2    Macris, B.J.3    Goodenough, P.W.4    Bhat, M.K.5
  • 18
    • 0033586978 scopus 로고    scopus 로고
    • Expression of soluble and catalytically active plant (monocot) β-glycosidases in E. coli
    • Cicek, M. and Esen, A. 1999. Expression of soluble and catalytically active plant (monocot) β-glycosidases in E. coli. Biotechnol. Bioeng. 63: 92-400.
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 92-400
    • Cicek, M.1    Esen, A.2
  • 19
    • 0025045601 scopus 로고
    • Chemical modification of a β-glucosidase from Schizophyllum commune: Evidence for essential carboxylic groups
    • Clarke, A.J. 1990. Chemical modification of a β-glucosidase from Schizophyllum commune: Evidence for essential carboxylic groups. Biochim. Biophys. Acta. 1040: 145-152.
    • (1990) Biochim. Biophys. Acta , vol.1040 , pp. 145-152
    • Clarke, A.J.1
  • 20
    • 0028972691 scopus 로고
    • Safety evaluation of β-glucanase derived from Trichoderma reesei: Summary of toxicological data
    • Coenen, T.M., Schoenmakers, A.E., and Verhagen, H. 1995. Safety evaluation of β-glucanase derived from Trichoderma reesei: Summary of toxicological data. Food Chem. Toxicol. 33: 859-866.
    • (1995) Food Chem. Toxicol. , vol.33 , pp. 859-866
    • Coenen, T.M.1    Schoenmakers, A.E.2    Verhagen, H.3
  • 21
    • 0034610330 scopus 로고    scopus 로고
    • The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA,-DIMBOAG1c, and-dhurrin complexes
    • Czjzek, M., Cicek, M., Zamboni, V., Bevan, D.R., Henrissat, B., and Esen, A. 2000. The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA,-DIMBOAG1c, and-dhurrin complexes. Proc. Nat. Acad. Sci. USA 97: 13555-13560.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 13555-13560
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Bevan, D.R.4    Henrissat, B.5    Esen, A.6
  • 22
    • 0035865504 scopus 로고    scopus 로고
    • Crystal structure of a monocotyledon (maize Zm Glu1) β-glucosidase and a model of its complex with p-nitrophenyl β-D-thioglucoside
    • Czjzek, M., Cicek, M., Zamboni, V., Burmeister, W. P., Bevan D.R., Henrissat, B., and Esen, A. 2001. Crystal structure of a monocotyledon (maize Zm Glu1) β-glucosidase and a model of its complex with p-nitrophenyl β-D-thioglucoside. Biochem. J. 354: 37-46.
    • (2001) Biochem. J. , vol.354 , pp. 37-46
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Burmeister, W.P.4    Bevan, D.R.5    Henrissat, B.6    Esen, A.7
  • 24
    • 0034681333 scopus 로고    scopus 로고
    • Cloning, expression, characterization and nucleophile identification of family 3 Aspergillus niger β-glucosidase
    • Dan, S., Marton, T., Dekol, M., Bravdo, B.A. He, S., Withers, S.G., and Shoserov, O. 2000. Cloning, expression, characterization and nucleophile identification of family 3 Aspergillus niger β-glucosidase. J. Biol. Chem. 275: 4973-4980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4973-4980
    • Dan, S.1    Marton, T.2    Dekol, M.3    Bravdo, B.A.4    He, S.5    Withers, S.G.6    Shoserov, O.7
  • 25
    • 8044229430 scopus 로고    scopus 로고
    • Transglycosylation of extracellular β-glucosidase of Trichoderma pseudokoningii S38 and its function in regulation of cellulase biosynthesis
    • Dong, W., Yinbo, Q.U., and Peiji, G. 1996. Transglycosylation of extracellular β-glucosidase of Trichoderma pseudokoningii S38 and its function in regulation of cellulase biosynthesis. J. Gen. Appl. Microbiol. 42: 363-369.
    • (1996) J. Gen. Appl. Microbiol. , vol.42 , pp. 363-369
    • Dong, W.1    Yinbo, Q.U.2    Peiji, G.3
  • 26
    • 0035904435 scopus 로고    scopus 로고
    • Cloning, sequence and structure of a gene encoding an antifungal glucan 1,3-β-glucosidase from Trichoderma atroviride (T. harzianum)
    • Donzelli, B.G.G., Lorito, M., Scala, F., and Harman, G.E. 2001. Cloning, sequence and structure of a gene encoding an antifungal glucan 1,3-β-glucosidase from Trichoderma atroviride (T. harzianum). Gene 277: 199-208.
    • (2001) Gene , vol.277 , pp. 199-208
    • Donzelli, B.G.G.1    Lorito, M.2    Scala, F.3    Harman, G.E.4
  • 27
    • 0034101163 scopus 로고    scopus 로고
    • Glycosidase inhibitors and their chemotherapeutic value, Part 3
    • ElAshry, E.S.H., Rashed, N., and Shobier, A.H.S. 2000. Glycosidase inhibitors and their chemotherapeutic value, Part 3. Pharmazie 55: 403-415.
    • (2000) Pharmazie , vol.55 , pp. 403-415
    • ElAshry, E.S.H.1    Rashed, N.2    Shobier, A.H.S.3
  • 28
    • 0002335391 scopus 로고
    • β-glucosidases: Overview
    • Esen, A., Ed., American Chemical Society, Washington, DC
    • Esen, A. 1993. β-glucosidases: Overview, in β-Glucosidases: Biochemistry and Molecular Biology, Esen, A., Ed., American Chemical Society, Washington, DC, 1-14.
    • (1993) β-Glucosidases: Biochemistry and Molecular Biology , pp. 1-14
    • Esen, A.1
  • 29
    • 0032962411 scopus 로고    scopus 로고
    • Growth of Azospirillum irakense KBC 1 on the aryl β-glucoside salicin requires either Sal A or Sal B
    • Faure, D., Desair J., Keijers, V., Bekri, M.A., Proost, P., Henrissat, B., and Vanderleyden, J. 1999. Growth of Azospirillum irakense KBC 1 on the aryl β-glucoside salicin requires either Sal A or Sal B. J. Bacteriol. 181: 3003-3009.
    • (1999) J. Bacteriol. , vol.181 , pp. 3003-3009
    • Faure, D.1    Desair, J.2    Keijers, V.3    Bekri, M.A.4    Proost, P.5    Henrissat, B.6    Vanderleyden, J.7
  • 30
    • 0030061364 scopus 로고    scopus 로고
    • Catalytical potency of β-glucosidase from the extremophile Pyrococcus furiosus in glycoconjugate biosynthesis
    • Fischer, L., Bronmann, R., Kengen, S.W.M., DeVos, W.M., and Wagner, F. 1996. Catalytical potency of β-glucosidase from the extremophile Pyrococcus furiosus in glycoconjugate biosynthesis. Bio/Technology 14: 88-91.
    • (1996) Bio/Technology , vol.14 , pp. 88-91
    • Fischer, L.1    Bronmann, R.2    Kengen, S.W.M.3    DeVos, W.M.4    Wagner, F.5
  • 31
    • 0034682044 scopus 로고    scopus 로고
    • Determination of β-glucosidase enzymatic function of the Histoplasma capsulatum H antigen using a native expression system
    • Fisher, K.L. and Woods, J.P. 2000. Determination of β-glucosidase enzymatic function of the Histoplasma capsulatum H antigen using a native expression system. Gene 247: 191-197.
    • (2000) Gene , vol.247 , pp. 191-197
    • Fisher, K.L.1    Woods, J.P.2
  • 32
    • 2242472244 scopus 로고
    • (Stanbury, J.B., Wygnaarden, J.B., and Fredrickson, D.S., Eds.) McGraw-Hill, New York
    • Fredrickson, D.S., and Sloan, H.R. 1972. The Metabolic Basis of Inherited Disease. (Stanbury, J.B., Wygnaarden, J.B., and Fredrickson, D.S., Eds.) McGraw-Hill, New York, 7730.
    • (1972) The Metabolic Basis of Inherited Disease , pp. 7730
    • Fredrickson, D.S.1    Sloan, H.R.2
  • 33
    • 0032552812 scopus 로고    scopus 로고
    • Enzymatic tranformations in supersaturated substrate solutions. I. A general study with glycosidases
    • Fureby, A.M., Gill, I.S., and Vulfson, E.N. 1998. Enzymatic tranformations in supersaturated substrate solutions. I. A general study with glycosidases. Biotechnol. Bioeng. 60: 190-196.
    • (1998) Biotechnol. Bioeng. , vol.60 , pp. 190-196
    • Fureby, A.M.1    Gill, I.S.2    Vulfson, E.N.3
  • 34
    • 0027420381 scopus 로고
    • Purification and properties of a recombinant β-glucosidase of the hyperthermophilic bacterium Thermotoga maritima
    • Gabelsberger, J., Liebl, W., and Schleifer, K.H. 1993. Purification and properties of a recombinant β-glucosidase of the hyperthermophilic bacterium Thermotoga maritima. Appl. Microbiol. Biotechnol. 40: 44-52.
    • (1993) Appl. Microbiol. Biotechnol. , vol.40 , pp. 44-52
    • Gabelsberger, J.1    Liebl, W.2    Schleifer, K.H.3
  • 35
    • 0028882930 scopus 로고
    • Substrate induced inactivation of a crippled β-glucosidase mutant: Identification of the labelled amino acid and mutagenic analysis of its role
    • Gebler, J.C., Trimbur, D.E., Warren, R.A.J., Aebersold, R., Namchur, M., and Withers, S.G. 1995. Substrate induced inactivation of a crippled β-glucosidase mutant: Identification of the labelled amino acid and mutagenic analysis of its role. Biochemistry 34: 14547-14553.
    • (1995) Biochemistry , vol.34 , pp. 14547-14553
    • Gebler, J.C.1    Trimbur, D.E.2    Warren, R.A.J.3    Aebersold, R.4    Namchur, M.5    Withers, S.G.6
  • 36
    • 0039596881 scopus 로고    scopus 로고
    • Molecular cloning and analysis of strictosidine β-D-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus
    • Geerlings, A., Ibanez, M.M.L., Memelinks, J., Heijden, R.V.D., and Verpoorte, R. 2000. Molecular cloning and analysis of strictosidine β-D-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus. J. Biol. Chem. 275: 3051-3056.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3051-3056
    • Geerlings, A.1    Ibanez, M.M.L.2    Memelinks, J.3    Heijden, R.V.D.4    Verpoorte, R.5
  • 37
    • 0040735677 scopus 로고    scopus 로고
    • Directed evolution of β-glucosidase A from Paenibacillus polymyxa to thermal resistance
    • Gonzalez-Blasco, G., Sanz-Aparicio, J., Gonzalez, B., Hermoso, J.A., and Polaina, J. 2000. Directed evolution of β-glucosidase A from Paenibacillus polymyxa to thermal resistance. J. Biol. Chem. 275: 13708-13712.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13708-13712
    • Gonzalez-Blasco, G.1    Sanz-Aparicio, J.2    Gonzalez, B.3    Hermoso, J.A.4    Polaina, J.5
  • 39
    • 0028157443 scopus 로고
    • Analysis of human acid β-glucosidase by site directed mutagenesis and heterologous expression
    • Grace, M.E., Newman, K.M., Scheinker, V., Bery-Fussman, A., and Grabowski, G.A. 1994. Analysis of human acid β-glucosidase by site directed mutagenesis and heterologous expression. J. Biol. Chem. 269: 2283-2290.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2283-2290
    • Grace, M.E.1    Newman, K.M.2    Scheinker, V.3    Bery-Fussman, A.4    Grabowski, G.A.5
  • 40
    • 0024659050 scopus 로고
    • Nucleotide sequence of the Clostridium thermocellum bglB gene encoding thermostable β-glucosidase B: Homology to fungal β-glucosidases
    • Graebnitz, F., Ruecknagel, K. P., Seiss, M., and Staudenbauer, W. L. 1989. Nucleotide sequence of the Clostridium thermocellum bglB gene encoding thermostable β-glucosidase B: Homology to fungal β-glucosidases. Mol. Gen. Genet. 217: 70-76.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 70-76
    • Graebnitz, F.1    Ruecknagel, K.P.2    Seiss, M.3    Staudenbauer, W.L.4
  • 41
    • 0025874582 scopus 로고
    • Structure of the β-glucosidase gene bglA of Clostridium thermocellum. Sequence analysis reveals a uperfamily of cellulases and β-glycosidases including human lactase/phlorizin hydrolase
    • Graebnitz, F., Seiss, M., Ruecknagel, K. P., and Staudenbauer, W. L. 1991. Structure of the β-glucosidase gene bglA of Clostridium thermocellum. Sequence analysis reveals a uperfamily of cellulases and β-glycosidases including human lactase/phlorizin hydrolase. Eur. J. Biochem. 200:3 01-309.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 301-309
    • Graebnitz, F.1    Seiss, M.2    Ruecknagel, K.P.3    Staudenbauer, W.L.4
  • 42
    • 0030988789 scopus 로고    scopus 로고
    • Purification and characterization of an intracellular β-glucosidase from a new strain of Leuconostoc mesenteroides isolated from cassava
    • Gueguen, Y., Chemardin, P., Labrot, P., Arnaud, A., and Galzy, P. 1997a. Purification and characterization of an intracellular β-glucosidase from a new strain of Leuconostoc mesenteroides isolated from cassava. J. Appl. Microbiol. 82: 469-476.
    • (1997) J. Appl. Microbiol. , vol.82 , pp. 469-476
    • Gueguen, Y.1    Chemardin, P.2    Labrot, P.3    Arnaud, A.4    Galzy, P.5
  • 43
    • 0031552603 scopus 로고    scopus 로고
    • Enhancement of aromatic quality of muscat wine by the use of immobilized β-glucosidase
    • Gueguen, Y., Chemardin, P., Pien, S., Arnaud, A., and Galzy, P. 1997b. Enhancement of aromatic quality of muscat wine by the use of immobilized β-glucosidase. J. Biotechnol. 55: 151-156.
    • (1997) J. Biotechnol. , vol.55 , pp. 151-156
    • Gueguen, Y.1    Chemardin, P.2    Pien, S.3    Arnaud, A.4    Galzy, P.5
  • 44
    • 25744469930 scopus 로고
    • The aroma of grapes. I. Extraction and determination of free and glycosidically bound fractions of some grape aroma components
    • Gunata, Y.Z., Bayonove, C.L., Baumes, R.L., and Cordonnier, R.E. 1985. The aroma of grapes. I. Extraction and determination of free and glycosidically bound fractions of some grape aroma components. J. Chromatogr. 331: 83-90.
    • (1985) J. Chromatogr. , vol.331 , pp. 83-90
    • Gunata, Y.Z.1    Bayonove, C.L.2    Baumes, R.L.3    Cordonnier, R.E.4
  • 45
    • 0028636468 scopus 로고
    • Enzymatic synthesis of monoterpenyl β-glucosides by various β-glucosidases
    • Gunata, Z., Vallier, M.J., Sapis, J.C., Baumes, R., and Bayonove, C. 1994. Enzymatic synthesis of monoterpenyl β-glucosides by various β-glucosidases. Enz. Microb. Technol. 16: 1055-1058.
    • (1994) Enz. Microb. Technol. , vol.16 , pp. 1055-1058
    • Gunata, Z.1    Vallier, M.J.2    Sapis, J.C.3    Baumes, R.4    Bayonove, C.5
  • 46
    • 0000622594 scopus 로고
    • Reactions of hydrolysis and transglycosylation catalyzed by cellobiase. Kinetics and mathematical model of the process
    • Gusakov, A.V., Sinitsyn, A.P., Klesov, A.A., and Goldshteins, G.K. 1984. Reactions of hydrolysis and transglycosylation catalyzed by cellobiase. Kinetics and mathematical model of the process. Biokhimiya 49: 1110-1120.
    • (1984) Biokhimiya , vol.49 , pp. 1110-1120
    • Gusakov, A.V.1    Sinitsyn, A.P.2    Klesov, A.A.3    Goldshteins, G.K.4
  • 47
    • 0034054726 scopus 로고    scopus 로고
    • The crystal structure of β-glucosidase from Bacillus circulans sub sp. alkalophilus: Ability to form long polymeric assemblies
    • Hakulinen, N., Paavilainen, S., Korpela, T., and Rouvinen, J. 2000. The crystal structure of β-glucosidase from Bacillus circulans sub sp. alkalophilus: Ability to form long polymeric assemblies. J. Struct. Biol. 129: 69-79.
    • (2000) J. Struct. Biol. , vol.129 , pp. 69-79
    • Hakulinen, N.1    Paavilainen, S.2    Korpela, T.3    Rouvinen, J.4
  • 48
    • 0035810688 scopus 로고    scopus 로고
    • Improved oligosaccharide synthesis by protein engineering of β-glucosidase CelB from hyperthermophilic Pyrococcus furiosus
    • Hansson, T., Kaper, T., VanderOost, J., DeVos, W.M., and Adlercreutz, P. 2001. Improved oligosaccharide synthesis by protein engineering of β-glucosidase CelB from hyperthermophilic Pyrococcus furiosus. Biotechnol. Bioeng. 73: 203-210.
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 203-210
    • Hansson, T.1    Kaper, T.2    VanderOost, J.3    DeVos, W.M.4    Adlercreutz, P.5
  • 49
    • 0032437109 scopus 로고    scopus 로고
    • Molecular cloning of two genes for β-D-glucosidase in Bacillus sp. GL1 and identification of one as a gellan degrading enzyme
    • Hashimoto, W., Miki, H., Nankai, H., Sato, N., Kawai, S., and Murata, K. 1998. Molecular cloning of two genes for β-D-glucosidase in Bacillus sp. GL1 and identification of one as a gellan degrading enzyme. Arch. Biochem. Biophys. 360: 1-9.
    • (1998) Arch. Biochem. Biophys. , vol.360 , pp. 1-9
    • Hashimoto, W.1    Miki, H.2    Nankai, H.3    Sato, N.4    Kawai, S.5    Murata, K.6
  • 51
    • 0027225980 scopus 로고
    • A classification of glycosyl-hydrolases based on amino acid sequence similarities
    • Henrissat, B. 1991. A classification of glycosyl-hydrolases based on amino acid sequence similarities. Biochem. J. 293: 781-788.
    • (1991) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1
  • 52
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and Bairoch, A. 1996. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316: 695-696.
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 53
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence based classification of glycosyl hydrolases
    • Henrissat, B. and Davies, G.J. 1997. Structural and sequence based classification of glycosyl hydrolases. Curr. Opin. Struct. Biol. 7: 637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.J.2
  • 54
    • 0030575197 scopus 로고    scopus 로고
    • Molecular cloning and bacterial expression of a cDNA encoding furastanol glycoside 2, 6-O-β-glucosidase of Costus speciosus
    • Inoue, K., Shibuya, M., Yamamoto, K., and Ebizuka, Y. 1996. Molecular cloning and bacterial expression of a cDNA encoding furastanol glycoside 2, 6-O-β-glucosidase of Costus speciosus. FEBS Lett. 389: 273-277.
    • (1996) FEBS Lett. , vol.389 , pp. 273-277
    • Inoue, K.1    Shibuya, M.2    Yamamoto, K.3    Ebizuka, Y.4
  • 55
    • 0029997172 scopus 로고    scopus 로고
    • Enzymatic synthesis of butylglycosides by glycosidases
    • Ismail, A. and Ghoul, M. 1996. Enzymatic synthesis of butylglycosides by glycosidases. Biotechnol. Lett. 18: 1199-204.
    • (1996) Biotechnol. Lett. , vol.18 , pp. 1199-1204
    • Ismail, A.1    Ghoul, M.2
  • 56
    • 0032736467 scopus 로고    scopus 로고
    • The bgl gene of Aspergillus kawachii encodes both extracellular and wall bound β-glucosidases
    • Iwashita, K., Nagahara, T., Kimura, H., Takano, M., Shimoi, K., and Ito K. 1999. The bgl gene of Aspergillus kawachii encodes both extracellular and wall bound β-glucosidases. Appl. Environ. Microbiol. 65: 5546-53.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5546-5553
    • Iwashita, K.1    Nagahara, T.2    Kimura, H.3    Takano, M.4    Shimoi, K.5    Ito, K.6
  • 57
    • 0028973426 scopus 로고
    • Cloning and sequencing of the β-glucosidase encoding gene from Candida molischiana strain 35M5N
    • Janbon, G., Magnet, R., Arnaud, A., and Galzy, P. 1995. Cloning and sequencing of the β-glucosidase encoding gene from Candida molischiana strain 35M5N. Gene 165: 109-113.
    • (1995) Gene , vol.165 , pp. 109-113
    • Janbon, G.1    Magnet, R.2    Arnaud, A.3    Galzy, P.4
  • 58
    • 0028956984 scopus 로고
    • β-Glucosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with a 8-fold α/β architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven
    • Jenkins, J., Leggio, L.L., Harris, G., and Pickersgill, R. 1995. β-Glucosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with a 8-fold α/β architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven. FEBS Lett. 362: 281-285.
    • (1995) FEBS Lett. , vol.362 , pp. 281-285
    • Jenkins, J.1    Leggio, L.L.2    Harris, G.3    Pickersgill, R.4
  • 59
    • 0040776974 scopus 로고    scopus 로고
    • Comparative structural analysis and substrate specificity engineering of the hyperthermostable β-glucosidase CelB from Pyrococcus furiosus
    • Kaper, T., Lebbink, J. H.G., Pouwels, J., Kopp, J., Schulz, G.E., van der Oost. J., and de Vos, W.M. 2000. Comparative structural analysis and substrate specificity engineering of the hyperthermostable β-glucosidase CelB from Pyrococcus furiosus. Biochemistry 39: 4963-4970.
    • (2000) Biochemistry , vol.39 , pp. 4963-4970
    • Kaper, T.1    Lebbink, J.H.G.2    Pouwels, J.3    Kopp, J.4    Schulz, G.E.5    Van der Oost, J.6    De Vos, W.M.7
  • 60
    • 0026234342 scopus 로고
    • Characterization of a β-glucosidase encoded by a gene from Cellovibrio gilvus
    • Kashiwagi, Y., Iijima, C., Sasaki, T., and Taniguchi, H. 1991. Characterization of a β-glucosidase encoded by a gene from Cellovibrio gilvus. Agric. Biol. Chem. 55: 2553-2559.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2553-2559
    • Kashiwagi, Y.1    Iijima, C.2    Sasaki, T.3    Taniguchi, H.4
  • 61
    • 0028020172 scopus 로고
    • Investigation of the active site of the cyanogenic β-glucosidase (Linamarase) from Manihot esculenta Crantz (cassava). Evidence for an essential carboxylate and a reactive histidine residue in a single catalytic center
    • Keresztessy, Z., Kiss, L., and Hughes, M.A. 1994. Investigation of the active site of the cyanogenic β-glucosidase (Linamarase) from Manihot esculenta Crantz (cassava). Evidence for an essential carboxylate and a reactive histidine residue in a single catalytic center. Arch. Biochem. Biophys. 314: 142-152.
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 142-152
    • Keresztessy, Z.1    Kiss, L.2    Hughes, M.A.3
  • 62
    • 0022021723 scopus 로고
    • Application of synthetic alkylglucoside vesicles as drug carriers. I. Preparation and physical properties
    • Kiwada, H., Niimura, H., Fujisaki, Y., Yamada, S., and Kato, Y. 1985. Application of synthetic alkylglucoside vesicles as drug carriers. I. Preparation and physical properties. Chem. Pharm. Bull. 33: 753-759.
    • (1985) Chem. Pharm. Bull. , vol.33 , pp. 753-759
    • Kiwada, H.1    Niimura, H.2    Fujisaki, Y.3    Yamada, S.4    Kato, Y.5
  • 63
    • 2442462549 scopus 로고    scopus 로고
    • Reverse hydrolytic process for O-alkylation of glucose catalysed by immobilized α- and β-glucosidases
    • Kosary, J., Banyai-Stefanovits, E., and Boross, L. 1998. Reverse hydrolytic process for O-alkylation of glucose catalysed by immobilized α- and β-glucosidases. J. Biotechnol. 66: 83-86.
    • (1998) J. Biotechnol. , vol.66 , pp. 83-86
    • Kosary, J.1    Banyai-Stefanovits, E.2    Boross, L.3
  • 64
    • 0027551663 scopus 로고
    • The Trichoderma cellulase regulatory puzzle: From the interior life of a secretory fungus
    • Kubicek, C.P., Messner, R., Gruber, F., Mach, R.L., and Kubicek-Pranz, E.M. 1993. The Trichoderma cellulase regulatory puzzle: From the interior life of a secretory fungus. Enz. Microb. Technol. 15: 90-99.
    • (1993) Enz. Microb. Technol. , vol.15 , pp. 90-99
    • Kubicek, C.P.1    Messner, R.2    Gruber, F.3    Mach, R.L.4    Kubicek-Pranz, E.M.5
  • 65
    • 0026814918 scopus 로고
    • Inactivation of β-glucosidase from Arthrobotrys conoides by diethylpyrocarbonate: Evidence of hisfidine at the active site
    • Kumble, K. D., Kumble, S., and Jaffar, M. B. 1992. Inactivation of β-glucosidase from Arthrobotrys conoides by diethylpyrocarbonate: Evidence of hisfidine at the active site. Indian J. Exp. Biol. 30: 99-102.
    • (1992) Indian J. Exp. Biol. , vol.30 , pp. 99-102
    • Kumble, K.D.1    Kumble, S.2    Jaffar, M.B.3
  • 66
    • 0001433833 scopus 로고
    • Some properties of transglycosylation activity of sesame β-glucosidase
    • Kuriyama, K., Tsuchiya, K., and Murui, T. 1995. Some properties of transglycosylation activity of sesame β-glucosidase. Biosci. Biotech. Biochem. 59: 1142-1143.
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 1142-1143
    • Kuriyama, K.1    Tsuchiya, K.2    Murui, T.3
  • 67
    • 0026566614 scopus 로고
    • Glucoside synthesis by glucoamylase or β-glucosidase in organic solvents
    • Laroute, V. and Willemot, R.M. 1992. Glucoside synthesis by glucoamylase or β-glucosidase in organic solvents. Biotechnol. Lett. 14: 169-174.
    • (1992) Biotechnol. Lett. , vol.14 , pp. 169-174
    • Laroute, V.1    Willemot, R.M.2
  • 68
    • 0029012960 scopus 로고
    • Biochemical and molecular characterization of a barley seed β-glucosidase
    • Leah, R., Kiegel, J., Suendson, I.B., and Mundy, J. 1995. Biochemical and molecular characterization of a barley seed β-glucosidase. J. Biol. Chem. 22: 15789-15796.
    • (1995) J. Biol. Chem. , vol.22 , pp. 15789-15796
    • Leah, R.1    Kiegel, J.2    Suendson, I.B.3    Mundy, J.4
  • 70
    • 0031841226 scopus 로고    scopus 로고
    • Gene cloning and characterization of a novel cellulose binding β-glucosidase from Phanerochaete chrysosporium
    • Li, B. and Ranganathan, V. 1998. Gene cloning and characterization of a novel cellulose binding β-glucosidase from Phanerochaete chrysosporium. Appl. Environ. Microbiol. 64: 2748-54.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2748-2754
    • Li, B.1    Ranganathan, V.2
  • 71
    • 0035340638 scopus 로고    scopus 로고
    • Catalytic mechanism of a family 3 β-glucosidase and mutagenesis study on residue Asp-247
    • Li, Y.K., Chir, J., and Chen, F.Y. 2001. Catalytic mechanism of a family 3 β-glucosidase and mutagenesis study on residue Asp-247. Biochem. J. 355: 835-840.
    • (2001) Biochem. J. , vol.355 , pp. 835-840
    • Li, Y.K.1    Chir, J.2    Chen, F.Y.3
  • 72
    • 0344061541 scopus 로고    scopus 로고
    • Cloning and expression of β-glucosidase from Flavobacteruim meningosepticum: A new member of family B β-glucosidase
    • Li, Y.K. and Lee, J.A. 1999. Cloning and expression of β-glucosidase from Flavobacteruim meningosepticum: A new member of family B β-glucosidase. Enz. Microb. Technol. 24: 144-150.
    • (1999) Enz. Microb. Technol. , vol.24 , pp. 144-150
    • Li, Y.K.1    Lee, J.A.2
  • 73
    • 0025032040 scopus 로고
    • Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a β-glucosidase
    • Lin, L. L., Rumbak, E., Zappe, H., Thompson, J. A., and Woods, D. R. 1990. Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a β-glucosidase. J. Gen. Microbiol. 136: 1567-1576.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1567-1576
    • Lin, L.L.1    Rumbak, E.2    Zappe, H.3    Thompson, J.A.4    Woods, D.R.5
  • 74
    • 0024254393 scopus 로고
    • Nucleotide sequences of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae
    • Machida. M., Ohtsuki, I., Fukui, S., and Yamashita, I. 1988. Nucleotide sequences of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 54: 3147-3155.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 3147-3155
    • Machida, M.1    Ohtsuki, I.2    Fukui, S.3    Yamashita, I.4
  • 75
    • 0029033496 scopus 로고
    • Cloning and nucleotide sequence of bglA from Erwinia herbicola and expression of β-glucosidase activity in Escherichia coli
    • Marri, L., Valentini, S., and Venditti, D. 1995. Cloning and nucleotide sequence of bglA from Erwinia herbicola and expression of β-glucosidase activity in Escherichia coli. FEMS Microbiol. Lett. 128: 135-138.
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 135-138
    • Marri, L.1    Valentini, S.2    Venditti, D.3
  • 76
    • 0028225107 scopus 로고
    • Solubilization of a novel isoflavone glycoside hydrolysing β-glucosidase from Lactobacillus casei subsp. rhamnosus
    • Matsuda, S., Norimoto, F., Matsumoto, Y., Ohba, R., Teramoto, Y., Ohta, N., and Veda, S. 1994. Solubilization of a novel isoflavone glycoside hydrolysing β-glucosidase from Lactobacillus casei subsp. rhamnosus. J. Ferment. Bioeng. 77: 439-441.
    • (1994) J. Ferment. Bioeng. , vol.77 , pp. 439-441
    • Matsuda, S.1    Norimoto, F.2    Matsumoto, Y.3    Ohba, R.4    Teramoto, Y.5    Ohta, N.6    Veda, S.7
  • 77
    • 0033977063 scopus 로고    scopus 로고
    • Novel substrate specificity of a membrane-bound β-glycosidase from the hyperthermophilic archeon Pyrococcus horikoshii
    • Matsui, I., Sakai, Y., Matsui, E., Kikuchi, M., Kawarabayasi, Y., and Honda K. 2000. Novel substrate specificity of a membrane-bound β-glycosidase from the hyperthermophilic archeon Pyrococcus horikoshii. FEBS Lett. 467: 195-200.
    • (2000) FEBS Lett. , vol.467 , pp. 195-200
    • Matsui, I.1    Sakai, Y.2    Matsui, E.3    Kikuchi, M.4    Kawarabayasi, Y.5    Honda, K.6
  • 79
    • 0033954715 scopus 로고    scopus 로고
    • The E358S mutant of Agrobacterium sp. is a greatly improved glycosynthase
    • Mayer, C., Zechel, D.L., Reid, S.P., Warren, R.A.J., and Withers, S.G. 2000. The E358S mutant of Agrobacterium sp. is a greatly improved glycosynthase. FEBS Lett. 466: 40-44.
    • (2000) FEBS Lett. , vol.466 , pp. 40-44
    • Mayer, C.1    Zechel, D.L.2    Reid, S.P.3    Warren, R.A.J.4    Withers, S.G.5
  • 80
    • 0025367234 scopus 로고
    • cDNA cloning and expression of a Talaromyces emersonii β-glucosidase determinant in Escherichia coli
    • Morrison, J., Jackson, E.A., Bunni, L., Coleman, D., M.C., and Hale, A.P. 1990. cDNA cloning and expression of a Talaromyces emersonii β-glucosidase determinant in Escherichia coli. Biochim. Biophys. Acta 1049: 27-32.
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 27-32
    • Morrison, J.1    Jackson, E.A.2    Bunni, L.3    Coleman, D.4    Hale, A.P.5
  • 81
    • 0031896304 scopus 로고    scopus 로고
    • Synthesis of aromatic n-alkyl-glucoside esters in a coupled β-glucosidase and lipase reaction
    • Otto, R.T., Bornsheuer, U.T., Syldatk, C., and Schmic, R.D. 1998. Synthesis of aromatic n-alkyl-glucoside esters in a coupled β-glucosidase and lipase reaction. Biotechnol. Lett. 20: 437-440.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 437-440
    • Otto, R.T.1    Bornsheuer, U.T.2    Syldatk, C.3    Schmic, R.D.4
  • 82
    • 0027469655 scopus 로고
    • Purification, characterization, gene cloning and sequencing of a new β-glucosidase from Bacillus circulans sub sp. alkalophilus
    • Paavilainen, S., Hellman, J., and Korpela, T. 1993. Purification, characterization, gene cloning and sequencing of a new β-glucosidase from Bacillus circulans sub sp. alkalophilus. Appl. Environ. Microbiol. 59: 927-932.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 927-932
    • Paavilainen, S.1    Hellman, J.2    Korpela, T.3
  • 83
    • 0026770535 scopus 로고
    • Purification and characterization of a Bacillus polymyxa β-glucosidase expressed in Escherichia coli
    • Painbeni, E., Valles, S., Poliana, J., and Flors, A. 1992. Purification and characterization of a Bacillus polymyxa β-glucosidase expressed in Escherichia coli. J. Bacteriol. 174: 3087-3091.
    • (1992) J. Bacteriol. , vol.174 , pp. 3087-3091
    • Painbeni, E.1    Valles, S.2    Poliana, J.3    Flors, A.4
  • 84
    • 0029417088 scopus 로고
    • Cloning and expression of β-glucosidase gene from the yeast Pichia etchellsii
    • Pandey, M. and Mishra, S. 1995. Cloning and expression of β-glucosidase gene from the yeast Pichia etchellsii. J. Ferment. Bioeng. 80: 446-453.
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 446-453
    • Pandey, M.1    Mishra, S.2
  • 85
    • 0030960324 scopus 로고    scopus 로고
    • Expression and characterization of Pichia etchellsii β-glucosidase in Escherichia coli
    • Pandey, M. and Mishra S. 1997. Expression and characterization of Pichia etchellsii β-glucosidase in Escherichia coli. Gene 190: 45-51.
    • (1997) Gene , vol.190 , pp. 45-51
    • Pandey, M.1    Mishra, S.2
  • 86
    • 0028985131 scopus 로고
    • Equilibrium yield of n-alkyl-β-D-glucoside through condensation of glucose and n-alcohol by β-glucosidase in a biphasic system
    • Panintrarux, C., Adachi, S., Araki, Y., Kimura, Y., and Matsuno, R. 1995. Equilibrium yield of n-alkyl-β-D-glucoside through condensation of glucose and n-alcohol by β-glucosidase in a biphasic system. Enz. Microb. Technol. 17: 32-40.
    • (1995) Enz. Microb. Technol. , vol.17 , pp. 32-40
    • Panintrarux, C.1    Adachi, S.2    Araki, Y.3    Kimura, Y.4    Matsuno, R.5
  • 87
    • 0029100735 scopus 로고
    • Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)
    • Perez-Pons, J.-A., Rebordosa, X., and Querol, E. 1995b. Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238) Biochim. Biophys. Acta 1251: 145-153.
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 145-153
    • Perez-Pons, J.-A.1    Rebordosa, X.2    Querol, E.3
  • 88
    • 0342981063 scopus 로고    scopus 로고
    • Enzymatic glycosidations in dry media on mineral supports
    • Pujic, G. M., Guibe Jampel, E., and Loupy, A. 1997. Enzymatic glycosidations in dry media on mineral supports. Tetrahedron 53: 17247-17252.
    • (1997) Tetrahedron , vol.53 , pp. 17247-17252
    • Pujic, G.M.1    Guibe Jampel, E.2    Loupy, A.3
  • 89
    • 0031468696 scopus 로고    scopus 로고
    • Novel bioconversions for the production of designer antioxidant and colourant flavonoides using polyphenol oxidases
    • Ridgway, T., Tucker, G., and Wiseman, H. 1997. Novel bioconversions for the production of designer antioxidant and colourant flavonoides using polyphenol oxidases. Biotechnol. Genet. Eng. Rev. 14: 165-190.
    • (1997) Biotechnol. Genet. Eng. Rev. , vol.14 , pp. 165-190
    • Ridgway, T.1    Tucker, G.2    Wiseman, H.3
  • 90
    • 0026782362 scopus 로고
    • Characterization of the gene CelD and its encoded product 1,4 β-D-glucan glucohydrolase D from Pseudomonas fluorescens sub sp. cellulosa
    • Rixon, J.E., Ferreira, L.M.A., Durrant, A.J., Laurie, J.I., Hazlewood, P.J., and Gilbert, H.J. 1992. Characterization of the gene CelD and its encoded product 1,4 β-D-glucan glucohydrolase D from Pseudomonas fluorescens sub sp. cellulosa. Biochem. J. 285: 947-955.
    • (1992) Biochem. J. , vol.285 , pp. 947-955
    • Rixon, J.E.1    Ferreira, L.M.A.2    Durrant, A.J.3    Laurie, J.I.4    Hazlewood, P.J.5    Gilbert, H.J.6
  • 91
    • 34250134090 scopus 로고
    • Characterization of naringinase from Aspergillus niger
    • Roitner, M., Schalkhammer, T., and Pittner, F. 1984. Characterization of naringinase from Aspergillus niger. Monatsh. Chem. 115: 1255-1267.
    • (1984) Monatsh. Chem. , vol.115 , pp. 1255-1267
    • Roitner, M.1    Schalkhammer, T.2    Pittner, F.3
  • 92
    • 0029554594 scopus 로고
    • β-glucosidase families revealed by computer analysis of protein sequences
    • Rojas, A., Arola, Li., and Romeu, A. 1995. β-Glucosidase families revealed by computer analysis of protein sequences. Biochem. Mol. Biol. Int. 35: 1223-1231.
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 1223-1231
    • Rojas, A.1    Arola, Li.2    Romeu, A.3
  • 93
    • 0027594752 scopus 로고
    • Purification and properties of the Clostridium thermocellum bglB gene product expressed in Escherichia coli
    • Romaniec, M.P.M., Huskisson, N., Barker, P., and Demain, A.L. 1993. Purification and properties of the Clostridium thermocellum bglB gene product expressed in Escherichia coli. Enz. Microb. Technol. 15: 393-400.
    • (1993) Enz. Microb. Technol. , vol.15 , pp. 393-400
    • Romaniec, M.P.M.1    Huskisson, N.2    Barker, P.3    Demain, A.L.4
  • 94
    • 0028173153 scopus 로고
    • Characterization of β-glucosidase activity in yeasts of enological origin
    • Rosi, I., Vinella, M., and Domezio, M. 1994. Characterization of β-glucosidase activity in yeasts of enological origin. J. Appl. Bact. 77: 519-527.
    • (1994) J. Appl. Bact. , vol.77 , pp. 519-527
    • Rosi, I.1    Vinella, M.2    Domezio, M.3
  • 95
    • 2242421111 scopus 로고
    • A new enzymatic method for the extraction of precarthamine pigment from dyer's saffron florets
    • Saito, K. 1993. A new enzymatic method for the extraction of precarthamine pigment from dyer's saffron florets. Z. Lebensm. Unters. Forsch. 197: 34-36.
    • (1993) Z. Lebensm. Unters. Forsch. , vol.197 , pp. 34-36
    • Saito, K.1
  • 96
    • 0030880652 scopus 로고    scopus 로고
    • A gene encoding an exo- β-glucosidase from Cellovibrio mixtus
    • Sakellaris, H., Manners, J. M., and Pemberton, J. M. 1997. A gene encoding an exo- β-glucosidase from Cellovibrio mixtus. Curr. Microbiol. 35: 228-232.
    • (1997) Curr. Microbiol. , vol.35 , pp. 228-232
    • Sakellaris, H.1    Manners, J.M.2    Pemberton, J.M.3
  • 97
    • 0032559380 scopus 로고    scopus 로고
    • Crystal structure of β-glucosidase A from Bacillus polymyxa: Insights into the catalytic activity in family 1 glycosyl hydrolases
    • Sanz-Aparicio, J., Hermoso, J.A., Martinez-Ripoll, M., Lequerica, J.L., and Poliana, J. 1998. Crystal structure of β-glucosidase A from Bacillus polymyxa: Insights into the catalytic activity in family 1 glycosyl hydrolases. J. Mol. Biol. 275: 491-502.
    • (1998) J. Mol. Biol. , vol.275 , pp. 491-502
    • Sanz-Aparicio, J.1    Hermoso, J.A.2    Martinez-Ripoll, M.3    Lequerica, J.L.4    Poliana, J.5
  • 98
    • 0002596553 scopus 로고    scopus 로고
    • Cloning, characterization of Pichia etchellsii β-glucosidase II and the effect of media composition and feeding strategy on its production in a bioreactor
    • Sethi, B., Jain, M., Chowdhary, M., Soni, Y., Bhatia, Y., Sahai, V., and Mishra, S. 2002. Cloning, characterization of Pichia etchellsii β-glucosidase II and the effect of media composition and feeding strategy on its production in a bioreactor. Biotechnol. Bioprocess Eng. 7: 43-51.
    • (2002) Biotechnol. Bioprocess Eng. , vol.7 , pp. 43-51
    • Sethi, B.1    Jain, M.2    Chowdhary, M.3    Soni, Y.4    Bhatia, Y.5    Sahai, V.6    Mishra, S.7
  • 99
    • 0031922229 scopus 로고    scopus 로고
    • Purification and characterization of β-1-4,-glucosidase from Clostridium papyrosolvens
    • Sharmila, T., Sreeramulu, G., and Nand, K. 1998. Purification and characterization of β-1-4,-glucosidase from Clostridium papyrosolvens. Biotechnol. Appl. Biochem. 27: 175-179.
    • (1998) Biotechnol. Appl. Biochem. , vol.27 , pp. 175-179
    • Sharmila, T.1    Sreeramulu, G.2    Nand, K.3
  • 101
    • 0028877739 scopus 로고
    • Cloning and characterization of a gene encoding a cell-bound, extracellular β-glucosidase in the yeast Candida wickerhamii
    • Skory, C.D. and Freer, S.N. 1995. Cloning and characterization of a gene encoding a cell-bound, extracellular β-glucosidase in the yeast Candida wickerhamii. Appl. Environ. Microbiol. 61: 518-525.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 518-525
    • Skory, C.D.1    Freer, S.N.2
  • 102
    • 0028300262 scopus 로고
    • Molecular cloning of thermostable β-glucosidase gene from a thermophilic anaerobe NA10 and its high expression in Escherichia coli
    • Sota, H., Arunwanich, P., Kurita, O., Vozumi, N., Honda, H., Iijma, S., and Kobayashi, T. 1994. Molecular cloning of thermostable β-glucosidase gene from a thermophilic anaerobe NA10 and its high expression in Escherichia coli. J. Ferment. Bioeng. 77: 199-201.
    • (1994) J. Ferment. Bioeng. , vol.77 , pp. 199-201
    • Sota, H.1    Arunwanich, P.2    Kurita, O.3    Vozumi, N.4    Honda, H.5    Iijma, S.6    Kobayashi, T.7
  • 104
    • 0032960527 scopus 로고    scopus 로고
    • A recombinant cellulolytic Escherichia coli: Cloning of the cellulase gene and characterization of a bifunctional cellulase
    • Srivastava, K.K., Verma, P.K., and Srivastava, R. 1999. A recombinant cellulolytic Escherichia coli: Cloning of the cellulase gene and characterization of a bifunctional cellulase. Biotechnol. Lett. 21: 293-297.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 293-297
    • Srivastava, K.K.1    Verma, P.K.2    Srivastava, R.3
  • 105
    • 0026545045 scopus 로고
    • Structure of a β-glucosidase gene from Ruminococcus albus and properties of the translated product
    • Takano, M., Moriyama, R., and Ohmiya, K. 1992. Structure of a β-glucosidase gene from Ruminococcus albus and properties of the translated product. J. Ferment. Bioeng. 73: 79-88.
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 79-88
    • Takano, M.1    Moriyama, R.2    Ohmiya, K.3
  • 106
    • 0032937042 scopus 로고    scopus 로고
    • Molecular cloning and expression of the novel fungal β-glucosidase genes from Humicola grisea and Trichoderma reesei
    • Takashima, S., Nakamura, A., Hidaka, M., Masaki, H., and Uozumi, T. 1999. Molecular cloning and expression of the novel fungal β-glucosidase genes from Humicola grisea and Trichoderma reesei. J. Biochem. 125: 728-736.
    • (1999) J. Biochem. , vol.125 , pp. 728-736
    • Takashima, S.1    Nakamura, A.2    Hidaka, M.3    Masaki, H.4    Uozumi, T.5
  • 107
    • 0027479060 scopus 로고
    • Crystallization and preliminary crystallographic analyis of the cyanogenic β-glucosidase from white clover Trifolium repens L.
    • Tolley, S.P., Barett, T.E., Suresh, C.G., and Hughes, M.A. 1993. Crystallization and preliminary crystallographic analyis of the cyanogenic β-glucosidase from white clover Trifolium repens L. J. Mol. Biol. 229: 791-793.
    • (1993) J. Mol. Biol. , vol.229 , pp. 791-793
    • Tolley, S.P.1    Barett, T.E.2    Suresh, C.G.3    Hughes, M.A.4
  • 108
    • 0028949304 scopus 로고
    • Efficient chemoselective synthesis of 3, 4', dihydroxypropiophenone 3-O-β-D-glucoside by thermophilic β-glycosidase from Sulfolobus solfataricus
    • Tricone, A. and Pagnotta, E. 1995. Efficient chemoselective synthesis of 3, 4', dihydroxypropiophenone 3-O-β-D-glucoside by thermophilic β-glycosidase from Sulfolobus solfataricus. Biotechnol. Lett. 17: 45-48.
    • (1995) Biotechnol. Lett. , vol.17 , pp. 45-48
    • Tricone, A.1    Pagnotta, E.2
  • 109
    • 0026731191 scopus 로고
    • Region-directed mutagenesis of residues surrounding the active site nucleophile in β-glucosidase from Agrobacterium faecalis
    • Trimbur, D.E., Warren, R.A.J., and Withers, S.G. 1992. Region-directed mutagenesis of residues surrounding the active site nucleophile in β-glucosidase from Agrobacterium faecalis. J. Biol. Chem. 267: 10248-51.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10248-10251
    • Trimbur, D.E.1    Warren, R.A.J.2    Withers, S.G.3
  • 110
    • 0017746987 scopus 로고
    • The active site of β-glucosidase from Botryodiplodia theobroame: Effects of pH and dioxan on enzyme catalysed reactions
    • Umezurike, G.M. 1977. The active site of β-glucosidase from Botryodiplodia theobroame: Effects of pH and dioxan on enzyme catalysed reactions. Biochem. J. 167: 831-833.
    • (1977) Biochem. J. , vol.167 , pp. 831-833
    • Umezurike, G.M.1
  • 112
    • 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. 1999. Three dimensional structure of a barley β-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure Fold. Des. 7: 179-190.
    • (1999) Structure Fold. Des. , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 113
    • 0031172560 scopus 로고    scopus 로고
    • Solvent effect on enzyme catalysed synthesis of β-D glucosides using the reverse hydrolysis method: Application to the preparative-scale synthesis of 2-hydroxybenzyl and octyl-β-D-glucopyranosides
    • Vic, G., Thomas, D., and Crout, DHG. 1997. Solvent effect on enzyme catalysed synthesis of β-D glucosides using the reverse hydrolysis method: Application to the preparative-scale synthesis of 2-hydroxybenzyl and octyl-β-D-glucopyranosides. Enz. Microb. Technol. 20: 597-603.
    • (1997) Enz. Microb. Technol. , vol.20 , pp. 597-603
    • Vic, G.1    Thomas, D.2    Crout, D.H.G.3
  • 115
    • 0028876332 scopus 로고
    • Characterization of celB gene encoding for β-glucosidase from the hyperthermophilic archeon Pyrococcus furiosus and its expression and site directed mutation in Escherichia coli
    • Voorhorst, W.G.B., Eggen, R.I.L., Lensink, E.J, and Vos, W.M.D.E. 1995. Characterization of celB gene encoding for β-glucosidase from the hyperthermophilic archeon Pyrococcus furiosus and its expression and site directed mutation in Escherichia coli. J. Bacteriol. 177: 7105-7111.
    • (1995) J. Bacteriol. , vol.177 , pp. 7105-7111
    • Voorhorst, W.G.B.1    Eggen, R.I.L.2    Lensink, E.J.3    Vos, W.M.D.E.4
  • 116
    • 0028899664 scopus 로고
    • Cloning and characterization of the bgxa gene from Erwinia chrysanthemi D1 that encodes a β-glucosidase/xylosidase enzyme
    • Vroemen, S., Heldens, J., Boyd, C., Henrissat, B., and Keen, N.T. 1995. Cloning and characterization of the bgxa gene from Erwinia chrysanthemi D1 that encodes a β-glucosidase/xylosidase enzyme. Mol. Gen. Genet. 246: 465-477.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 465-477
    • Vroemen, S.1    Heldens, J.2    Boyd, C.3    Henrissat, B.4    Keen, N.T.5
  • 119
    • 0035314098 scopus 로고    scopus 로고
    • Mechanisms of glycosyl transferases and hydrolases
    • Withers, S.G. 2001. Mechanisms of glycosyl transferases anal hydrolases. Carbohydrate Polymers 44: 325-337.
    • (2001) Carbohydrate Polymers , vol.44 , pp. 325-337
    • Withers, S.G.1
  • 120
    • 0001410590 scopus 로고
    • Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase
    • Withers, S.G. and Street, I.P. 1988. Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase. J. Am. Chem. Soc. 110: 8551-8553.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8551-8553
    • Withers, S.G.1    Street, I.P.2
  • 121
    • 2242474088 scopus 로고
    • β-Glucosidase: Mechanism and inhibition
    • Lewis, N.G., Ed. American Chemical Society, Washington, DC
    • Withers, S.G. and Street, I.P. 1989. β-Glucosidase: Mechanism and inhibition, in Plant Cell Wall Polymers: Biogenesis and Biodegradation, Lewis, N.G., Ed. American Chemical Society, Washington, DC, 597-607.
    • (1989) Plant Cell Wall Polymers: Biogenesis and Biodegradation , pp. 597-607
    • Withers, S.G.1    Street, I.P.2
  • 122
    • 0001463551 scopus 로고
    • Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase
    • Withers, S.G., Warren, R.A.J., Street, I.P., Rupitz, K., Kempton, J.B., and Aebersold, R. 1990. Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase. J. Am. Chem. Soc. 112: 5887-5889.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5887-5889
    • Withers, S.G.1    Warren, R.A.J.2    Street, I.P.3    Rupitz, K.4    Kempton, J.B.5    Aebersold, R.6
  • 123
    • 0026443120 scopus 로고
    • Cloning, characterization, and nucleotide sequence of a gene encoding Microspora bispora BglB, a thermostable β-glucosidase expressed in Escherichia coli
    • Wright, R.M., Yablonsky M. D., Shalita, Z. P., Goyal, A.K., and Eveleigh, D. E. 1992. Cloning, characterization, and nucleotide sequence of a gene encoding Microspora bispora BglB, a thermostable β-glucosidase expressed in Escherichia coli. Appl. Environ. Microbiol. 58: 3455-3465.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3455-3465
    • Wright, R.M.1    Yablonsky, M.D.2    Shalita, Z.P.3    Goyal, A.K.4    Eveleigh, D.E.5
  • 124
    • 0028809783 scopus 로고
    • 1 4 β-glucosidase with cellodextrinase and cyanoglycosidase activities
    • 1 4 β-glucosidase with cellodextrinase and cyanoglycosidase activities. J. Bacteriol. 177: 5884-5890.
    • (1995) J. Bacteriol. , vol.177 , pp. 5884-5890
    • Wulff-Strobel, C.R.1    Wilson, D.B.2
  • 125
    • 0031820066 scopus 로고    scopus 로고
    • Synthesis of cello-oligosaccharides from cellobiose with β-glucosidase II from Aspergillus niger
    • Yan, T.R. and Liau, J.C.1998a. Synthesis of cello-oligosaccharides from cellobiose with β-glucosidase II from Aspergillus niger. Biotechnol. Lett. 20: 591-594.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 591-594
    • Yan, T.R.1    Liau, J.C.2
  • 126
    • 0031866994 scopus 로고    scopus 로고
    • Synthesis of alkyl β-D-glucosides from cellobiose with Aspergillus niger β-glucosidase II
    • Yan, T.R. and Liau, J.C. 1998b. Synthesis of alkyl β-D-glucosides from cellobiose with Aspergillus niger β-glucosidase II. Biotechnol. Lett. 20: 653-657.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 653-657
    • Yan, T.R.1    Liau, J.C.2
  • 127
    • 0032487739 scopus 로고    scopus 로고
    • A novel approach to biotransformations in aqueous-organic-two-phase systems: Enzymatic synthesis of alkyl-β-[D]-glucosides using microencapsulated β-glucosidase
    • Yi, Q., Sarney, D.B., Khan J.A., and Vulfson, E.N. 1998. A novel approach to biotransformations in aqueous-organic-two-phase systems: Enzymatic synthesis of alkyl-β-[D]-glucosides using microencapsulated β-glucosidase. Biotechnol. Bioeng. 60: 385-390.
    • (1998) Biotechnol. Bioeng. , vol.60 , pp. 385-390
    • Yi, Q.1    Sarney, D.B.2    Khan, J.A.3    Vulfson, E.N.4
  • 128
    • 0034217534 scopus 로고    scopus 로고
    • β-Glucosidase of leaves and roots of the common beet Beta vulgaris
    • Zakharova, N.S. and Petrova, T.V. 2000. β-Glucosidase of leaves and roots of the common beet Beta vulgaris. Prikl. Biokhim. Mikrobiol. 36: 458-61.
    • (2000) Prikl. Biokhim. Mikrobiol. , vol.36 , pp. 458-461
    • Zakharova, N.S.1    Petrova, T.V.2
  • 129
    • 0001663436 scopus 로고    scopus 로고
    • Mechanisms of glycosyl transfer
    • Barton, D., Nakanishi, K. and Poulter, C. D. (Eds.), Elsevier, Chap. 12
    • Zechel, D. and Withers, S. G. 1999. Mechanisms of glycosyl transfer. In: Barton, D., Nakanishi, K. and Poulter, C. D. (Eds.), Comprehensive Natural Products Chemistry, vol. 5, Elsevier, Chap. 12, 279-314.
    • (1999) Comprehensive Natural Products Chemistry , vol.5 , pp. 279-314
    • Zechel, D.1    Withers, S.G.2
  • 130
    • 0030076919 scopus 로고    scopus 로고
    • A simple model for predicting the response of chicks to dietary enzyme supplementation
    • Zhang, Z., Marquardt, R.R., Wang, G., Guenter, W., Crow, G.H., Han, Z., and Bedford, M.R. 1996. A simple model for predicting the response of chicks to dietary enzyme supplementation. J. Anim. Sci. 74: 394-402.
    • (1996) J. Anim. Sci. , vol.74 , pp. 394-402
    • Zhang, Z.1    Marquardt, R.R.2    Wang, G.3    Guenter, W.4    Crow, G.H.5    Han, Z.6    Bedford, M.R.7
  • 131
    • 0035193637 scopus 로고    scopus 로고
    • Insights into the functional architecture of the catalytic centre of a maize β-glucosidase Zm-p 60.1
    • Zouhar, J., Vevodova, J., Marek, J., Damborsky, J., Su, X.D., and Brzobohaty, B. 2001. Insights into the functional architecture of the catalytic centre of a maize β-glucosidase Zm-p 60.1. Plant Physiol. 127: 973-985.
    • (2001) Plant Physiol. , vol.127 , pp. 973-985
    • Zouhar, J.1    Vevodova, J.2    Marek, J.3    Damborsky, J.4    Su, X.D.5    Brzobohaty, B.6
  • 132
    • 0030680965 scopus 로고    scopus 로고
    • Thermotoga neopolitana bglB gene, upstream of lamA, encodes a highly thermostable β-glucosidase that is a laminaribiase
    • Zverlow, V.V., Volkov, I.Y., Velikodvorskaya, T.V., and Schwarz, W.H. 1997. Thermotoga neopolitana bglB gene, upstream of lamA, encodes a highly thermostable β-glucosidase that is a laminaribiase. Microbiology 143: 3537-42.
    • (1997) Microbiology , vol.143 , pp. 3537-3542
    • Zverlow, V.V.1    Volkov, I.Y.2    Velikodvorskaya, T.V.3    Schwarz, W.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.