메뉴 건너뛰기




Volumn , Issue , 2005, Pages 1229-1256

Enzymatic synthesis of oligosaccharides: Progress and recent trends

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84884248507     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (153)
  • 1
    • 0035937502 scopus 로고    scopus 로고
    • Cinderella's coach is ready
    • Hurtley, S., R. Service, P. Szuromi. Cinderella's coach is ready. Science 291:2337-2337, 2001.
    • (2001) Science , vol.291 , pp. 2337-2337
    • Hurtley, S.1    Service, R.2    Szuromi, P.3
  • 2
    • 0000084638 scopus 로고    scopus 로고
    • Carbohydrate drugs: An ongoing challenge
    • McAuliffe, J.C., O. Hindsgaul. Carbohydrate drugs: an ongoing challenge. Chem. Ind. 5:170-174, 1997.
    • (1997) Chem. Ind , vol.5 , pp. 170-174
    • McAuliffe, J.C.1    Hindsgaul, O.2
  • 3
    • 0027339137 scopus 로고
    • Carbohydrates in cell recognition
    • Sharon, N., H. Lis. Carbohydrates in cell recognition. Sci. Am. 268:82-89, 1993.
    • (1993) Sci. Am , vol.268 , pp. 82-89
    • Sharon, N.1    Lis, H.2
  • 5
    • 0001851183 scopus 로고
    • Oligosaccharides
    • 2nd ed., Vol. IIA. Pigman, W., D. Horton, eds., New York: Academic Press
    • Pazur, J.H. Oligosaccharides. In: The Carbohydrates: Chemistry and Biochemistry, 2nd ed., Vol. IIA. Pigman, W., D. Horton, eds., New York: Academic Press, 1970, pp 69-137.
    • (1970) The Carbohydrates: Chemistry and Biochemistry , pp. 69-137
    • Pazur, J.H.1
  • 6
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All the theories are correct
    • Varki, A. Biological roles of oligosaccharides: all the theories are correct. Glycobiology 3:97-130, 1993.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 7
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek, R.A. Glycobiology: toward understanding the function of sugars. Chem. Rev. 96:683-720, 1996.
    • (1996) Chem. Rev , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 8
    • 0025260978 scopus 로고
    • Adhesins as lectins: Specificity and role in infection
    • Ofek, I., N. Sharon. Adhesins as lectins: specificity and role in infection. Curr. Top. Microbiol. Immunol. 151:91-113, 1990.
    • (1990) Curr. Top. Microbiol. Immunol , vol.151 , pp. 91-113
    • Ofek, I.1    Sharon, N.2
  • 9
    • 0029881352 scopus 로고    scopus 로고
    • Oligosaccharides anti-infective agents
    • Zopf, D., S. Roth. Oligosaccharides anti-infective agents. Lancet 347:1017-1021, 1996.
    • (1996) Lancet , vol.347 , pp. 1017-1021
    • Zopf, D.1    Roth, S.2
  • 10
    • 0031872407 scopus 로고    scopus 로고
    • Meaning and therapeutic potential of microbial recognition of host glyco-conjugates
    • Karlsson, K.-A. Meaning and therapeutic potential of microbial recognition of host glyco-conjugates. Mol. Microbiol. 29:1-11, 1998.
    • (1998) Mol. Microbiol , vol.29 , pp. 1-11
    • Karlsson, K.-A.1
  • 11
    • 0036311402 scopus 로고    scopus 로고
    • Glycoscience: Oligosaccharides as drugs, functional foods, and receptors in the gut
    • Playne, M.J., Glycoscience: oligosaccharides as drugs, functional foods, and receptors in the gut. Aust. Biotechnol. 12:35-37, 2002.
    • (2002) Aust. Biotechnol , vol.12 , pp. 35-37
    • Playne, M.J.1
  • 13
    • 0036149240 scopus 로고    scopus 로고
    • Synthesis of "mixed type" oligosaccharide mimetics based on a carbohydrate scaffold
    • Patel, A., T.K. Lindhorst. Synthesis of "mixed type" oligosaccharide mimetics based on a carbohydrate scaffold. Eur. J. Org. Chem. 1:79-86, 2002.
    • (2002) Eur. J. Org. Chem , vol.1 , pp. 79-86
    • Patel, A.1    Lindhorst, T.K.2
  • 14
    • 0030295006 scopus 로고    scopus 로고
    • Production, properties and application of food-grade oligo-saccharides
    • Crittenden, R.G., M.J. Playne. Production, properties and application of food-grade oligo-saccharides. Trends Food Sci. Tech. 7:353-361, 1996.
    • (1996) Trends Food Sci. Tech , vol.7 , pp. 353-361
    • Crittenden, R.G.1    Playne, M.J.2
  • 15
    • 0036664864 scopus 로고    scopus 로고
    • Present status and future of functional oligosaccharide development in Japan
    • Nakakuki, T. Present status and future of functional oligosaccharide development in Japan. Pure Appl. Chem. 74:1245-1251, 2002.
    • (2002) Pure Appl. Chem , vol.74 , pp. 1245-1251
    • Nakakuki, T.1
  • 16
    • 0024094991 scopus 로고
    • Enzymatic synthesis of oligosaccharides
    • Nilsson, K.G.I. Enzymatic synthesis of oligosaccharides. Trends Biotech. 6:256-264, 1988.
    • (1988) Trends Biotech , vol.6 , pp. 256-264
    • Nilsson, K.G.I.1
  • 17
    • 0030058793 scopus 로고    scopus 로고
    • Strategies in oligosaccharide synthesis
    • Boons, G.J. Strategies in oligosaccharide synthesis. Tetrahedron 52:1095-1121, 1996.
    • (1996) Tetrahedron , vol.52 , pp. 1095-1121
    • Boons, G.J.1
  • 18
    • 0034698451 scopus 로고    scopus 로고
    • Recent developments in oligosaccharide synthesis
    • Davis, B.G. Recent developments in oligosaccharide synthesis. J. Chem. Soc. Perkin Trans. 1(14):2137-2160, 2000.
    • (2000) J. Chem. Soc. Perkin Trans , vol.1 , Issue.14 , pp. 2137-2160
    • Davis, B.G.1
  • 19
    • 0343528450 scopus 로고    scopus 로고
    • Towards the 21st century: The emerging importance of oligosaccharide synthesis
    • Ekelöf, K., P.J. Garegg, L. Olsson, S. Oscarson. Towards the 21st century: the emerging importance of oligosaccharide synthesis. Pure Appl. Chem. 69:1847-1852, 1997.
    • (1997) Pure Appl. Chem , vol.69 , pp. 1847-1852
    • Ekelöf, K.1    Garegg, P.J.2    Olsson, L.3    Oscarson, S.4
  • 20
    • 0030892662 scopus 로고    scopus 로고
    • A new strategy for oligosaccharide assembly exploiting cyclohexane-1,2-diacetal methodology: An efficient synthesis of a high mannose type nonasaccharide
    • Grice, P., S.V. Ley, J. Pietruszka, H.M.I. Osborn, H.W.M. Priepke, S.L. Warriner. A new strategy for oligosaccharide assembly exploiting cyclohexane-1,2-diacetal methodology: an efficient synthesis of a high mannose type nonasaccharide. Chem. Eur. J. 3:431-440, 1997.
    • (1997) Chem. Eur. J , vol.3 , pp. 431-440
    • Grice, P.1    Ley, S.V.2    Pietruszka, J.3    Osborn, H.M.I.4    Priepke, H.W.M.5    Warriner, S.L.6
  • 22
    • 0035820048 scopus 로고    scopus 로고
    • Pursuit of optimal carbohydrate-based anticancer vaccines: Preparation of a multiantigenic unimolecular glycopeptide containing the Tn, MBr1, and Lewis (y) antigens
    • Allen, J.R., C.R. Harris, S.J. Danishefsky. Pursuit of optimal carbohydrate-based anticancer vaccines: preparation of a multiantigenic unimolecular glycopeptide containing the Tn, MBr1, and Lewis (y) antigens. J. Am. Chem. Soc. 123:1890-1897, 2001.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 1890-1897
    • Allen, J.R.1    Harris, C.R.2    Danishefsky, S.J.3
  • 23
    • 0037007836 scopus 로고    scopus 로고
    • Synthesis of biologically potent A-1,2-linked disaccharide derivatives via regioselective one-pot protection-glycosylation
    • Wang, C.-C., J.-C. Lee, S.-Y. Luo, H.-F. Fan, C.-L. Pai, W.-C. Yang, L.-D. Lu, S.-C. Hung. Synthesis of biologically potent A-1,2-linked disaccharide derivatives via regioselective one-pot protection-glycosylation. Angew Chem. Int. Ed. 41:2360-2362, 2002.
    • (2002) Angew Chem. Int. Ed , vol.41 , pp. 2360-2362
    • Wang, C.-C.1    Lee, J.-C.2    Luo, S.-Y.3    Fan, H.-F.4    Pai, C.-L.5    Yang, W.-C.6    Lu, L.-D.7    Hung, S.-C.8
  • 24
    • 0028886945 scopus 로고
    • Rapid chemical synthesis of sugar-nucleotides in a form suitable for enzymatic oligosaccharide synthesis
    • Arlt, M., O. Hidsgaul. Rapid chemical synthesis of sugar-nucleotides in a form suitable for enzymatic oligosaccharide synthesis. J. Org. Chem. 60:14-15, 1995.
    • (1995) J. Org. Chem , vol.60 , pp. 14-15
    • Arlt, M.1    Hidsgaul, O.2
  • 25
    • 0035443894 scopus 로고    scopus 로고
    • New approaches to the chemical synthesis of bioactive oli-gosaccharides
    • Bartolozzi, A., P.H. Seeberger. New approaches to the chemical synthesis of bioactive oli-gosaccharides. Curr. Opin. Struct. Biol. 11:587-592, 2001.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 587-592
    • Bartolozzi, A.1    Seeberger, P.H.2
  • 26
    • 0034697139 scopus 로고    scopus 로고
    • Anomeric reactivity-based one-pot oligosaccharide synthesis: A rapid route to oligosaccharide libraries
    • Ye, X.-S., C.-H. Wong. Anomeric reactivity-based one-pot oligosaccharide synthesis: a rapid route to oligosaccharide libraries. J. Org. Chem. 65:2410-2431, 2000.
    • (2000) J. Org. Chem , vol.65 , pp. 2410-2431
    • Ye, X.-S.1    Wong, C.-H.2
  • 27
    • 0033657768 scopus 로고    scopus 로고
    • Complex carbohydrate synthesis tools for glycobiologists: Enzyme-based approach and programmable one-pot strategies
    • Koeller, K.M., C.-H. Wong. Complex carbohydrate synthesis tools for glycobiologists: enzyme-based approach and programmable one-pot strategies. Glycobiology 10:1157-1169, 2000.
    • (2000) Glycobiology , vol.10 , pp. 1157-1169
    • Koeller, K.M.1    Wong, C.-H.2
  • 28
    • 0031395418 scopus 로고    scopus 로고
    • The chemoenzymatic synthesis of the core trisaccharide of N-linked oligosaccharides using a recombinant B -mannosyltransferase
    • Watt, G.M., L. Revers, M.C. Webberley, I.B.H. Wilson, S.L. Flitsch. The chemoenzymatic synthesis of the core trisaccharide of N-linked oligosaccharides using a recombinant B -mannosyltransferase. Carbohydr. Res. 305:533-541, 1997.
    • (1997) Carbohydr. Res , vol.305 , pp. 533-541
    • Watt, G.M.1    Revers, L.2    Webberley, M.C.3    Wilson, I.B.H.4    Flitsch, S.L.5
  • 29
    • 84982635826 scopus 로고
    • Applications of enzymes in synthetic carbohydrate chemistry
    • Theim, J. Applications of enzymes in synthetic carbohydrate chemistry. FEMS Microbiol. Rev. 16:193-211, 1995.
    • (1995) FEMS Microbiol. Rev , vol.16 , pp. 193-211
    • Theim, J.1
  • 30
    • 0000991554 scopus 로고    scopus 로고
    • Glycosyltransferase-catalysed synthesis of non-natural oligosaccharides
    • Öhrlein, R. Glycosyltransferase-catalysed synthesis of non-natural oligosaccharides. Top. Curr. Chem. 200:227-254, 1999.
    • (1999) Top. Curr. Chem , vol.200 , pp. 227-254
    • Öhrlein, R.1
  • 32
    • 0032708956 scopus 로고    scopus 로고
    • Biocatalytic synthesis of oligosaccharides
    • Palcic, M.M. Biocatalytic synthesis of oligosaccharides. Curr. Opin. Biotechnol. 10:616-624, 1999.
    • (1999) Curr. Opin. Biotechnol , vol.10 , pp. 616-624
    • Palcic, M.M.1
  • 34
    • 0035354761 scopus 로고    scopus 로고
    • Heterologous over-expression of alpha-1,6-fucosyltransferase from Rhizobium sp.: Application to the synthesis of the trisaccharide beta-D-GlcNAc(1 -> 4)-(alpha-L-Fuc-(1 -> 6))-D-GlcNAc, study of the acceptor specificity and evaluation of polyhydroxylated indolizidines as inhibitors
    • Bastida, A., A. Fernandez-Mayoralas, R.G. Arrayas, F. Iradier, J.C. Carretero, E. Garcia-Junceda. Heterologous over-expression of alpha-1,6-fucosyltransferase from Rhizobium sp.: application to the synthesis of the trisaccharide beta-D-GlcNAc(1 -> 4)-(alpha-L-Fuc-(1 -> 6))-D-GlcNAc, study of the acceptor specificity and evaluation of polyhydroxylated indolizidines as inhibitors. Chem. Eur. J. 7:2390-2397, 2001.
    • (2001) Chem. Eur. J , vol.7 , pp. 2390-2397
    • Bastida, A.1    Fernandez-Mayoralas, A.2    Arrayas, R.G.3    Iradier, F.4    Carretero, J.C.5    Garcia-Junceda, E.6
  • 35
    • 0020009823 scopus 로고
    • Cloning genes for bacterial glycosyltransferases
    • Creeger, E.S., L.I. Rothfield. Cloning genes for bacterial glycosyltransferases. Methods Enzymol. 83:326-331, 1982.
    • (1982) Methods Enzymol , vol.83 , pp. 326-331
    • Creeger, E.S.1    Rothfield, L.I.2
  • 36
    • 0023182876 scopus 로고
    • Characterization of glucosyltrans-ferase expressed from a Streptococcus sobrinus gene cloned in
    • Russel, R.R.B., M.L. Gilpin, H. Mukasa, G. Dougan. Characterization of glucosyltrans-ferase expressed from a Streptococcus sobrinus gene cloned in Escherichia coli. J. Gen. Microbiol. 133:935-944, 1987.
    • (1987) Escherichia coli. J. Gen. Microbiol , vol.133 , pp. 935-944
    • Russel, R.R.B.1    Gilpin, M.L.2    Mukasa, H.3    Dougan, G.4
  • 37
    • 0023623637 scopus 로고
    • Primary structure of beta-galctosidase alpha-2,6-sialyltransferase- conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor
    • Weinstein, J., E.U. Lee, K. McEntee, P.H. Lai, J.C. Paulson. Primary structure of beta-galctosidase alpha-2,6-sialyltransferase- conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor. J. Biol. Chem. 262:17735-17743, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 17735-17743
    • Weinstein, J.1    Lee, E.U.2    McEntee, K.3    Lai, P.H.4    Paulson, J.C.5
  • 38
    • 0026666837 scopus 로고
    • Primary structure of Gal-beta-1,3(4)GlcNAc alpha-2,3-sialyltransferase determined by mass-spectrometry sequence-analysis and molecular-cloning-evidence for a protein motif in the sialyltransferase gene family
    • Wen, D.X., B.D. Livingston, K.F. Medzihradszky, S. Kelm, A.L. Burlingame, J.C. Paulson. Primary structure of Gal-beta-1,3(4)GlcNAc alpha-2,3-sialyltransferase determined by mass-spectrometry sequence-analysis and molecular-cloning-evidence for a protein motif in the sialyltransferase gene family. J. Biol. Chem. 267:21011-21019, 1992.
    • (1992) J. Biol. Chem , vol.267 , pp. 21011-21019
    • Wen, D.X.1    Livingston, B.D.2    Medzihradszky, K.F.3    Kelm, S.4    Burlingame, A.L.5    Paulson, J.C.6
  • 39
    • 0024593480 scopus 로고
    • Stable expression of blood group-H determinants and GDP-L-fucose-beta-D-galactosidase 2-alpha-L-fucosyltransferase in mouse cells after transfection with human DNA
    • Ernst, L.K., V.P. Rajan, R.D. Larsen, M.M. Ruff, J.B. Lowe. Stable expression of blood group-H determinants and GDP-L-fucose-beta-D-galactosidase 2-alpha-L-fucosyltransferase in mouse cells after transfection with human DNA. J. Biol. Chem. 264:3436-3447, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 3436-3447
    • Ernst, L.K.1    Rajan, V.P.2    Larsen, R.D.3    Ruff, M.M.4    Lowe, J.B.5
  • 40
    • 0001236540 scopus 로고
    • Enzymes in oligosaccha-ride synthesis: Active domain overproduction, specificity study, and synthetic use of an A-1,2-mannosyltransferase with regeneration of GDP-Man
    • Wang, P., G.-J. Shen, Y.-F. Wang, Y. Ichikawa, C.-H. Wong. Enzymes in oligosaccha-ride synthesis: active domain overproduction, specificity study, and synthetic use of an A-1,2-mannosyltransferase with regeneration of GDP-Man. J. Org. Chem. 58:3985-3990, 1993.
    • (1993) J. Org. Chem , vol.58 , pp. 3985-3990
    • Wang, P.1    Shen, G.-J.2    Wang, Y.-F.3    Ichikawa, Y.4    Wong, C.-H.5
  • 41
    • 0033025655 scopus 로고    scopus 로고
    • Development of recombinant, immobilised beta-1,4-mannosyltransferase for use as an efficient tool in the chemo-enzymatic synthesis of N-linked oligosaccharides
    • Revers, L., R.M. Bill, I.B.H. Wilson, G.M. Watt, S.L. Flitsch. Development of recombinant, immobilised beta-1,4-mannosyltransferase for use as an efficient tool in the chemo-enzymatic synthesis of N-linked oligosaccharides. Biochim. Biophys. Acta Gen. Subjects 1428:88-98, 1999.
    • (1999) Biochim. Biophys. Acta Gen. Subjects , vol.1428 , pp. 88-98
    • Revers, L.1    Bill, R.M.2    Wilson, I.B.H.3    Watt, G.M.4    Flitsch, S.L.5
  • 43
    • 0030036056 scopus 로고    scopus 로고
    • Recombinant soluble beta-1,4-galactosyltransferases expressed in Saccharomyces cerevi-siae: Purification, characterization and comparison with human enzyme
    • Malissard, M., L. Borsig, S. DiMarco, M.G. Grutter, U. Kragl, C. Wandrey, E.G. Berger. Recombinant soluble beta-1,4-galactosyltransferases expressed in Saccharomyces cerevi-siae: purification, characterization and comparison with human enzyme. Eur. J. Biochem. 239:340-348, 1996.
    • (1996) Eur. J. Biochem , vol.239 , pp. 340-348
    • Malissard, M.1    Borsig, L.2    DiMarco, S.3    Grutter, M.G.4    Kragl, U.5    Wandrey, C.6    Berger, E.G.7
  • 44
    • 0037016720 scopus 로고    scopus 로고
    • Cloning and expression of human core beta 1,3- galactosyltransferase
    • Ju, T.Z., K. Brewer, A. D'Souza, R.D. Cummings, W.M. Canfield. Cloning and expression of human core beta 1,3- galactosyltransferase. J. Biol. Chem. 277:178-186, 2002.
    • (2002) J. Biol. Chem , vol.277 , pp. 178-186
    • Ju, T.Z.1    Brewer, K.2    D'Souza, A.3    Cummings, R.D.4    Canfield, W.M.5
  • 45
    • 0037033072 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel UDP-Gal: GaINAc alpha peptide beta 1,3-galactosyltransferase (ClGal-T2), an enzyme synthesizing a core 1 structure of O-glycan
    • Kudo, T., T. Iwai, T. Kubota, H. Iwasaki, Y. Takayma, T. Hiruma, N. Inaba, Y. Zhang, M. Gotoh, A. Togayachi, H. Narimatsu. Molecular cloning and characterization of a novel UDP-Gal: GaINAc alpha peptide beta 1,3-galactosyltransferase (ClGal-T2), an enzyme synthesizing a core 1 structure of O-glycan. J. Biol. Chem. 277:47724-47731, 2002.
    • (2002) J. Biol. Chem , vol.277 , pp. 47724-47731
    • Kudo, T.1    Iwai, T.2    Kubota, T.3    Iwasaki, H.4    Takayma, Y.5    Hiruma, T.6    Inaba, N.7    Zhang, Y.8    Gotoh, M.9    Togayachi, A.10    Narimatsu, H.11
  • 46
    • 0026655074 scopus 로고
    • Enzyme-catalyzed oligosaccharide synthesis
    • Ichikawa, Y., G.C. Look, C.-H. Wong. Enzyme-catalyzed oligosaccharide synthesis. Anal. Biochem. 202:215-238, 1992.
    • (1992) Anal. Biochem , vol.202 , pp. 215-238
    • Ichikawa, Y.1    Look, G.C.2    Wong, C.-H.3
  • 47
    • 0031993483 scopus 로고    scopus 로고
    • Glycosidases and glycosyl transferases in glycoside and oligosac-charide synthesis
    • Crout, D.H.G., G. Vic. Glycosidases and glycosyl transferases in glycoside and oligosac-charide synthesis. Curr. Opin. Chem. Biol. 2:98-111, 1998.
    • (1998) Curr. Opin. Chem. Biol , vol.2 , pp. 98-111
    • Crout, D.H.G.1    Vic, G.2
  • 48
    • 1642593650 scopus 로고
    • Enzyme-catalysed synthesis of N-acetyllac-tosamine with in situ regeneration of uridine 5\-diphosphate glucose and uridine 5\- diphosphate galactose
    • Wong, C.-H., S.L. Haynie, G.M. Whitesides. Enzyme-catalysed synthesis of N-acetyllac-tosamine with in situ regeneration of uridine 5\-diphosphate glucose and uridine 5\- diphosphate galactose. J. Org. Chem. 47:5416-5418, 1982.
    • (1982) J. Org. Chem , vol.47 , pp. 5416-5418
    • Wong, C.-H.1    Haynie, S.L.2    Whitesides, G.M.3
  • 49
    • 0001462336 scopus 로고
    • A highly efficient multienzyme system for the one-step synthesis of a sialyl trisaccharide-insitu generation of sialic-acid and N-acetyl-lactosamine coupled with regeneration of UDP-Glucose, UDP-Galactose, and CMP-Sialic acid
    • Ichikawa, Y., J.L.C. Liu, G.J. Shen, C.H. Wong. A highly efficient multienzyme system for the one-step synthesis of a sialyl trisaccharide-insitu generation of sialic-acid and N-acetyl-lactosamine coupled with regeneration of UDP-Glucose, UDP-Galactose, and CMP-Sialic acid. J. Am. Chem. Soc. 113:6300-6302, 1991.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 6300-6302
    • Ichikawa, Y.1    Liu, J.L.C.2    Shen, G.J.3    Wong, C.H.4
  • 50
    • 0026739706 scopus 로고
    • Regeneration of sugar-nucleotide for enzymatic oligosac-charide synthesis: Use of Gal-1-phosphate uridyltransferase in the regeneration of UDP-galac-tose, UDP-2-deoxygalactose, and UDP-galactosamine
    • Wong, C.-H., R. Wang, Y. Ichikawa. Regeneration of sugar-nucleotide for enzymatic oligosac-charide synthesis: use of Gal-1-phosphate uridyltransferase in the regeneration of UDP-galac-tose, UDP-2-deoxygalactose, and UDP-galactosamine. J. Org. Chem. 57:4343-1344, 1992.
    • (1992) J. Org. Chem , vol.57 , pp. 1344-4343
    • Wong, C.-H.1    Wang, R.2    Ichikawa, Y.3
  • 51
    • 0032821706 scopus 로고    scopus 로고
    • Enzymatic synthesis of nucleotide sugars
    • Bulter, T., L. Elling. Enzymatic synthesis of nucleotide sugars. Glycoconjugate J. 16:147-159, 1999.
    • (1999) Glycoconjugate J , vol.16 , pp. 147-159
    • Bulter, T.1    Elling, L.2
  • 52
    • 0343750679 scopus 로고    scopus 로고
    • Enzymatic synthesis of UDP-galactose on a gram scale
    • Bulter, T., L. Elling. Enzymatic synthesis of UDP-galactose on a gram scale. J. Mol. Catal. B Enzym. 8:281-284, 2000.
    • (2000) J. Mol. Catal. B Enzym , vol.8 , pp. 281-284
    • Bulter, T.1    Elling, L.2
  • 53
    • 0022886959 scopus 로고
    • Synthesis of the trisaccharide Neu-5-Ac-Alpha(2-)6)Gal-Beta (1-)4)GlcNAc by the use of immobilized enzymes
    • Thiem, J., W. Treder. Synthesis of the trisaccharide Neu-5-Ac-Alpha(2-)6)Gal-Beta (1-)4)GlcNAc by the use of immobilized enzymes. Angew. Chem. Int. Ed. Engl. 25:1096-1097, 1986.
    • (1986) Angew. Chem. Int. Ed. Engl , vol.25 , pp. 1096-1097
    • Thiem, J.1    Treder, W.2
  • 54
    • 0030991639 scopus 로고    scopus 로고
    • Porcine liver (2->3)-alpha-sialyltransferase: Substrate specificity studies and application of the immobilized enzyme to the synthesis of various sialylated oligosaccharide sequences
    • Lubineau, A., K. BassetCarpentier, C. Auge. Porcine liver (2->3)-alpha-sialyltransferase: substrate specificity studies and application of the immobilized enzyme to the synthesis of various sialylated oligosaccharide sequences. Carbohydr. Res. 300:161-167, 1997.
    • (1997) Carbohydr. Res , vol.300 , pp. 161-167
    • Lubineau, A.1    BassetCarpentier, K.2    Auge, C.3
  • 55
    • 0035823741 scopus 로고    scopus 로고
    • Highly efficient oligosaccharide synthesis on water-soluble polymeric primers by recombinant glycosyl-transferases immobilized on solid supports
    • Nishiguchi, S., K. Yamada, Y. Fuji, S. Shibatani, A. Toda, S.-I. Nishimura. Highly efficient oligosaccharide synthesis on water-soluble polymeric primers by recombinant glycosyl-transferases immobilized on solid supports. Chem. Commun. 19:1944-1945, 2001.
    • (2001) Chem. Commun , vol.19 , pp. 1944-1945
    • Nishiguchi, S.1    Yamada, K.2    Fuji, Y.3    Shibatani, S.4    Toda, A.5    Nishimura, S.-I.6
  • 56
    • 0028011302 scopus 로고
    • Recombinant whole cells as catalysts for the enzymatic synthesis of oligosaccharides and glycopeptides
    • Herrmann, G.F., P. Wang, G.-J. Shen, C.-H. Wong. Recombinant whole cells as catalysts for the enzymatic synthesis of oligosaccharides and glycopeptides. Angew. Chem. Int. Ed. Engl. 33:1241-1242, 1994.
    • (1994) Angew. Chem. Int. Ed. Engl , vol.33 , pp. 1241-1242
    • Herrmann, G.F.1    Wang, P.2    Shen, G.-J.3    Wong, C.-H.4
  • 57
    • 0346037163 scopus 로고    scopus 로고
    • Superbeads: Immobilization in "sweet" chemistry
    • Nahalka, J., Z. Liu, X. Chen, P.G. Wang. Superbeads: immobilization in "sweet" chemistry. Chem. Eur. J. 9:372-377, 2003.
    • (2003) Chem. Eur. J , vol.9 , pp. 372-377
    • Nahalka, J.1    Liu, Z.2    Chen, X.3    Wang, P.G.4
  • 58
    • 0031754396 scopus 로고    scopus 로고
    • Large-scale production of UDP-galactose and globotriose by coupling metabolically engineered bacteria
    • Koizumi, S., T. Endo, K. Tabata, A. Ozaki. Large-scale production of UDP-galactose and globotriose by coupling metabolically engineered bacteria. Nat. Biotechnol. 16:847-850, 1998.
    • (1998) Nat. Biotechnol , vol.16 , pp. 847-850
    • Koizumi, S.1    Endo, T.2    Tabata, K.3    Ozaki, A.4
  • 59
    • 0033032743 scopus 로고    scopus 로고
    • Large-scale production of N-acetyl-lactosamine through bacterial coupling
    • Endo, T., S. Koizumi, K. Tabata, S. Kakita, A. Ozaki. Large-scale production of N-acetyl-lactosamine through bacterial coupling. Carbohydr. Res. 316:179-183, 1999.
    • (1999) Carbohydr. Res , vol.316 , pp. 179-183
    • Endo, T.1    Koizumi, S.2    Tabata, K.3    Kakita, S.4    Ozaki, A.5
  • 60
    • 0034069205 scopus 로고    scopus 로고
    • Large-scale production of CMP-NeuAc and sialylated oligosaccharides through bacterial coupling
    • Endo, T., S. Koizumi, K. Tabata, A. Ozaki. Large-scale production of CMP-NeuAc and sialylated oligosaccharides through bacterial coupling. Appl. Microbiol. Biotechnol. 53:257-261, 2000.
    • (2000) Appl. Microbiol. Biotechnol , vol.53 , pp. 257-261
    • Endo, T.1    Koizumi, S.2    Tabata, K.3    Ozaki, A.4
  • 61
    • 0035961368 scopus 로고    scopus 로고
    • Large-scale production of the carbohydrate portion of the sialyl-Tn epitope, alpha-Neup5Ac-(2 -> 6)-D-GalpNAc, through bacterial coupling
    • Endo, T., S. Koizumi, K. Tabata, S. Kakita, A. Ozaki. Large-scale production of the carbohydrate portion of the sialyl-Tn epitope, alpha-Neup5Ac-(2 -> 6)-D-GalpNAc, through bacterial coupling. Carbohydrate Res. 330:439-443, 2001.
    • (2001) Carbohydrate Res , vol.330 , pp. 439-443
    • Endo, T.1    Koizumi, S.2    Tabata, K.3    Kakita, S.4    Ozaki, A.5
  • 62
    • 0037016633 scopus 로고    scopus 로고
    • Reassembled biosynthetic pathway for large-scale carbohydrate synthesis: Alpha-Gal epitope producing "superbug"
    • Chen, X., Z.Y. Liu, J.B. Zhang, W. Zhang, P. Kowal, P.G. Wang. Reassembled biosynthetic pathway for large-scale carbohydrate synthesis: alpha-Gal epitope producing "superbug". Chem. Biochem. 3:47-53, 2002.
    • (2002) Chem. Biochem , vol.3 , pp. 47-53
    • Chen, X.1    Liu, Z.Y.2    Zhang, J.B.3    Zhang, W.4    Kowal, P.5    Wang, P.G.6
  • 63
    • 0036019911 scopus 로고    scopus 로고
    • A new fermentation process allows large-scale production of human-milk oligosaccharides by metabolically engineered bacteria
    • Priem, B., M. Gilbert, W.W. Wakarchuk, A. Heyraud, E. Samain. A new fermentation process allows large-scale production of human-milk oligosaccharides by metabolically engineered bacteria. Glycobiology 12:235-240, 2002.
    • (2002) Glycobiology , vol.12 , pp. 235-240
    • Priem, B.1    Gilbert, M.2    Wakarchuk, W.W.3    Heyraud, A.4    Samain, E.5
  • 64
    • 0035819944 scopus 로고    scopus 로고
    • Sugar nucleotide regeneration beads (Superbeads): A versatile tool for the practical synthesis of oligosaccharides
    • Chen, X., J. Fang, J. Zhang, Z. Liu, J. Shao, P. Kowal, P. Andreana, P.G. Wang. Sugar nucleotide regeneration beads (Superbeads): a versatile tool for the practical synthesis of oligosaccharides. J. Am. Chem. Soc. 123:2081-2082, 2001.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 2081-2082
    • Chen, X.1    Fang, J.2    Zhang, J.3    Liu, Z.4    Shao, J.5    Kowal, P.6    Andreana, P.7    Wang, P.G.8
  • 65
    • 0037007176 scopus 로고    scopus 로고
    • Combined biosynthetic pathway for de novo production of UDP-galactose: Catalysis with multiple enzymes immobilized on agarose beads
    • Liu, Z.Y., J.B. Zhang, X. Chen, P.G. Wang. Combined biosynthetic pathway for de novo production of UDP-galactose: catalysis with multiple enzymes immobilized on agarose beads. Chem. Biochem. 3:348-355, 2002.
    • (2002) Chem. Biochem , vol.3 , pp. 348-355
    • Liu, Z.Y.1    Zhang, J.B.2    Chen, X.3    Wang, P.G.4
  • 66
    • 0035713715 scopus 로고    scopus 로고
    • Large-scale synthesis of carbohydrates for pharmaceutical development
    • Zhang, J., B. Wu, Z. Liu, P. Kowal, X. Chen, J. Shao, P.G. Wang. Large-scale synthesis of carbohydrates for pharmaceutical development. Curr. Org. Chem. 5:1169-1176, 2001.
    • (2001) Curr. Org. Chem , vol.5 , pp. 1169-1176
    • Zhang, J.1    Wu, B.2    Liu, Z.3    Kowal, P.4    Chen, X.5    Shao, J.6    Wang, P.G.7
  • 68
    • 0033305545 scopus 로고    scopus 로고
    • 1998 Hoffman La Roche Award Lecture: Understanding and exploiting glyco-sidases
    • Withers, S.G. 1998 Hoffman La Roche Award Lecture: understanding and exploiting glyco-sidases. Can. J. Chem. 77:1-11, 1999.
    • (1999) Can. J. Chem , vol.77 , pp. 1-11
    • Withers, S.G.1
  • 70
    • 0035314098 scopus 로고    scopus 로고
    • Mechanisms of glycosyl transferases and hydrolases
    • Withers, S.G. Mechanisms of glycosyl transferases and hydrolases. Carbohydr. Polym. 44:325-337, 2001.
    • (2001) Carbohydr. Polym , vol.44 , pp. 325-337
    • Withers, S.G.1
  • 73
    • 0029666454 scopus 로고    scopus 로고
    • The pK(a) of the general acid/base carboxyl group of a glycosidase cycle during catalysis: A C-13-NMR study of Bacillus circulans xylanase
    • McIntosh, L.P., G. Hand, P.E. Johnson, M.D. Joshi, M. Korner, L.A. Plesniak, L. Ziser, W.W. Wakarchuk, S.G. Withers. The pK(a) of the general acid/base carboxyl group of a glycosidase cycle during catalysis: A C-13-NMR study of Bacillus circulans xylanase. Biochemistry 35:9958-9966, 1996.
    • (1996) Biochemistry , vol.35 , pp. 9958-9966
    • McIntosh, L.P.1    Hand, G.2    Johnson, P.E.3    Joshi, M.D.4    Korner, M.5    Plesniak, L.A.6    Ziser, L.7    Wakarchuk, W.W.8    Withers, S.G.9
  • 76
    • 0036015502 scopus 로고    scopus 로고
    • Control of regioselectivity in the enzymatic syntheses of oligo-saccharides using glycosides
    • Ajisaka, K., Y. Yamamoto. Control of regioselectivity in the enzymatic syntheses of oligo-saccharides using glycosides. Trends Glycosci. Glycotechnol. 14:1-11, 2002.
    • (2002) Trends Glycosci. Glycotechnol , vol.14 , pp. 1-11
    • Ajisaka, K.1    Yamamoto, Y.2
  • 77
    • 0001150534 scopus 로고
    • Use of an activated carbon column for the synthesis of disaccharides by use of a reverse hydrolysis activity of beta-galactosidase
    • Ajisaka, K., H. Nishida, H. Fujimoto. Use of an activated carbon column for the synthesis of disaccharides by use of a reverse hydrolysis activity of beta-galactosidase. Biotechnol. Lett. 9:387-392, 1987.
    • (1987) Biotechnol. Lett , vol.9 , pp. 387-392
    • Ajisaka, K.1    Nishida, H.2    Fujimoto, H.3
  • 78
    • 0021106296 scopus 로고
    • Carbohydrate specificity of the surface lectins of Escherichia coli, Klebsiella pneumoniae, and
    • Firon, N., I. Ofek, N. Sharon. Carbohydrate specificity of the surface lectins of Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium. Carbohydr. Res. 120:235-249, 1983.
    • (1983) Salmonella typhimurium. Carbohydr. Res , vol.120 , pp. 235-249
    • Firon, N.1    Ofek, I.2    Sharon, N.3
  • 79
    • 0023191455 scopus 로고
    • Bacterial lectins, cell-cell recognition and infectious disease
    • Sharon, N. Bacterial lectins, cell-cell recognition and infectious disease. FEBS Lett. 217:145-157, 1987.
    • (1987) FEBS Lett , vol.217 , pp. 145-157
    • Sharon, N.1
  • 80
    • 0030863415 scopus 로고    scopus 로고
    • Specificity of the high-man-nose recognition site between Enterobacter cloacae pili adhesin and HT-29 cell membranes
    • Pan, Y.T., B. Xu, K. Rice, S. Smith, R. Jackson, A.D. Elbein. Specificity of the high-man-nose recognition site between Enterobacter cloacae pili adhesin and HT-29 cell membranes. Infect. Immun. 65:4199-4206, 1997.
    • (1997) Infect. Immun , vol.65 , pp. 4199-4206
    • Pan, Y.T.1    Xu, B.2    Rice, K.3    Smith, S.4    Jackson, R.5    Elbein, A.D.6
  • 82
    • 0026541995 scopus 로고
    • A-mannosidase-catalysed synthesis of novel manno-,lyxo-,and heteromanno-oligosaccharides: A comparison of kineti-cally and thermodynamically mediated approaches
    • Rastall, R.A., N.H. Rees, R. Wait, M.W. Adlard, C. Bucke. A-mannosidase-catalysed synthesis of novel manno-,lyxo-,and heteromanno-oligosaccharides: a comparison of kineti-cally and thermodynamically mediated approaches. Enzyme Microb. Technol. 14:53-57, 1992.
    • (1992) Enzyme Microb. Technol , vol.14 , pp. 53-57
    • Rastall, R.A.1    Rees, N.H.2    Wait, R.3    Adlard, M.W.4    Bucke, C.5
  • 83
    • 0032170622 scopus 로고    scopus 로고
    • Enzymatic synthesis of manno- and heteromanno-oligosac-charides using A-mannosidases: A comparative study of linkage-specific and non-linkage-specific enzymes
    • Suwasono, S., R.A. Rastall. Enzymatic synthesis of manno- and heteromanno-oligosac-charides using A-mannosidases: a comparative study of linkage-specific and non-linkage-specific enzymes. J. Chem. Technol. Biotechnol. 73:37-42, 1998.
    • (1998) J. Chem. Technol. Biotechnol , vol.73 , pp. 37-42
    • Suwasono, S.1    Rastall, R.A.2
  • 84
    • 0033994529 scopus 로고    scopus 로고
    • Glycosidase-catalysed synthesis of manno-bioses by the reverse hydrolysis activity of alpha-mannosidase: Partial purification of alpha-mannosidases from almond meal, limpets and
    • Singh, S., M. Scigelova, D.H.G. Crout. Glycosidase-catalysed synthesis of manno-bioses by the reverse hydrolysis activity of alpha-mannosidase: partial purification of alpha-mannosidases from almond meal, limpets and Aspergillus niger. Tetrahedron Asymmetry 11:223-229, 2000.
    • (2000) Aspergillus niger. Tetrahedron Asymmetry , vol.11 , pp. 223-229
    • Singh, S.1    Scigelova, M.2    Crout, D.H.G.3
  • 86
    • 0030018665 scopus 로고    scopus 로고
    • A highly regioselective synthesis of mannobiose and mannot-riose by reverse hydrolysis using specific 1,2-A-mannosidase from
    • Suwasono, S., R.A. Rastall. A highly regioselective synthesis of mannobiose and mannot-riose by reverse hydrolysis using specific 1,2-A-mannosidase from Aspergillus phoenicis. Biotechnol. Lett. 18:851-856, 1996.
    • (1996) Aspergillus phoenicis. Biotechnol. Lett , vol.18 , pp. 851-856
    • Suwasono, S.1    Rastall, R.A.2
  • 87
    • 1242270629 scopus 로고    scopus 로고
    • Regioselective synthesis of mannobiose and mannotriose by reverse hydrolysis using a novel 1,6-A-D-mannosidase from
    • Athanasopoulos, V.l., K. Niranjan, R.A. Rastall. Regioselective synthesis of mannobiose and mannotriose by reverse hydrolysis using a novel 1,6-A-D-mannosidase from Aspergillus phoenicis. J. Mol. Catal. B Enzym. 27:215-219, 2004.
    • (2004) Aspergillus phoenicis. J. Mol. Catal. B Enzym , vol.27 , pp. 215-219
    • Athanasopoulos, V.I.1    Niranjan, K.2    Rastall, R.A.3
  • 88
    • 0025737855 scopus 로고
    • Synthesis of hetero-oligosaccharides by glucoamy-lase in reverse
    • Rastall, R.A., M.W. Adlard, C. Bucke. Synthesis of hetero-oligosaccharides by glucoamy-lase in reverse. Biotechnol. Lett. 13:501-504, 1991.
    • (1991) Biotechnol. Lett , vol.13 , pp. 501-504
    • Rastall, R.A.1    Adlard, M.W.2    Bucke, C.3
  • 89
    • 0026689642 scopus 로고
    • Synthesis of oligosaccharides by reversal of a fungal B-glucanase
    • Rastall, R.A., S.F. Pikett, M.W. Adlard, C. Bucke. Synthesis of oligosaccharides by reversal of a fungal B-glucanase. Biotechnol. Lett. 14:373-378, 1992.
    • (1992) Biotechnol. Lett , vol.14 , pp. 373-378
    • Rastall, R.A.1    Pikett, S.F.2    Adlard, M.W.3    Bucke, C.4
  • 90
    • 0031555005 scopus 로고    scopus 로고
    • Kinetics and equilibria of condensation reactions between monosaccharide pairs catalyzed by Aspergillus niger glucoamylase
    • Pestlin, S., D. Prinz, J.N. Starr, P.J. Reilly. Kinetics and equilibria of condensation reactions between monosaccharide pairs catalyzed by Aspergillus niger glucoamylase. Biotechnol. Bioeng. 56:9-22, 1997.
    • (1997) Biotechnol. Bioeng , vol.56 , pp. 9-22
    • Pestlin, S.1    Prinz, D.2    Starr, J.N.3    Reilly, P.J.4
  • 91
    • 0032203817 scopus 로고    scopus 로고
    • Cellulases for oligosaccharide synthesis: A preliminary study
    • Gama, F.M., M. Mota. Cellulases for oligosaccharide synthesis: a preliminary study. Carbohydr. Polym. 37:279-281, 1998.
    • (1998) Carbohydr. Polym , vol.37 , pp. 279-281
    • Gama, F.M.1    Mota, M.2
  • 92
    • 0034605567 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by reversed catalysis using A-amylase from Bacillus licheniformis
    • Chitradon, L., P. Mahakhan, C. Bucke. Oligosaccharide synthesis by reversed catalysis using A-amylase from Bacillus licheniformis. J. Mol. Catal. B Enzym. 10:273-280, 2000.
    • (2000) J. Mol. Catal. B Enzym , vol.10 , pp. 273-280
    • Chitradon, L.1    Mahakhan, P.2    Bucke, C.3
  • 94
    • 0036097465 scopus 로고    scopus 로고
    • Enzymatic synthesis of thioglucosides using almond B-glucosidse
    • Meulenbeld, G.H., B.M. Roode, S. Hartmans. Enzymatic synthesis of thioglucosides using almond B-glucosidse. Biocatal. Biotrans. 20:251-256, 2002.
    • (2002) Biocatal. Biotrans , vol.20 , pp. 251-256
    • Meulenbeld, G.H.1    Roode, B.M.2    Hartmans, S.3
  • 95
    • 0028951034 scopus 로고
    • Enzymatic synthesis of oligosaccharies
    • Monsan, P., F. Paul. Enzymatic synthesis of oligosaccharies. FEMS Microb. Rev. 16:187-192, 1995.
    • (1995) FEMS Microb. Rev , vol.16 , pp. 187-192
    • Monsan, P.1    Paul, F.2
  • 96
    • 0034703443 scopus 로고    scopus 로고
    • Enzymatic synthesis of fucose-containing disaccharides employing the partially purified A-L-fucosidase from
    • Farkas, E., J. Thiem, K. Ajisaka. Enzymatic synthesis of fucose-containing disaccharides employing the partially purified A-L-fucosidase from Penicillium multicolor. Carbohydr. Res. 328:293-299, 2000.
    • (2000) Penicillium multicolor. Carbohydr. Res , vol.328 , pp. 293-299
    • Farkas, E.1    Thiem, J.2    Ajisaka, K.3
  • 97
    • 0033199969 scopus 로고    scopus 로고
    • B-galactooligosaccharide synthesis with B-galactosidases from Sulfolobus solfataricus, Aspergillus oryzae, and
    • Reuter, S., A.R. Nygaard, W. Zimmermann. B-galactooligosaccharide synthesis with B-galactosidases from Sulfolobus solfataricus, Aspergillus oryzae, and Escherichia coli. Enzyme Microb. Technol. 25:509-516, 1999.
    • (1999) Escherichia coli. Enzyme Microb. Technol , vol.25 , pp. 509-516
    • Reuter, S.1    Nygaard, A.R.2    Zimmermann, W.3
  • 98
    • 0034135690 scopus 로고    scopus 로고
    • Effect of temperature and enzyme origin on the enzymatic synthesis of oligosaccharides
    • Boon, M.A., A.E.M. Janssen, K. van't Riet. Effect of temperature and enzyme origin on the enzymatic synthesis of oligosaccharides. Enzyme Microb. Technol. 26:271-281, 2000.
    • (2000) Enzyme Microb. Technol , vol.26 , pp. 271-281
    • Boon, M.A.1    Janssen, A.E.M.2    van't Riet, K.3
  • 99
    • 0036184323 scopus 로고    scopus 로고
    • High yield and high selectivity of reactions in the frozen state: The acceptor reaction of dextransucrase
    • Daum, B., K. Buchholz. High yield and high selectivity of reactions in the frozen state: the acceptor reaction of dextransucrase. Biocatal. Biotrans. 20:15-21, 2002.
    • (2002) Biocatal. Biotrans , vol.20 , pp. 15-21
    • Daum, B.1    Buchholz, K.2
  • 100
    • 0036732504 scopus 로고    scopus 로고
    • The temperature influences the ratio of glucosidase and galac-tosidase activities of B-glycosidases
    • Hansson, T., P. Adlercreutz. The temperature influences the ratio of glucosidase and galac-tosidase activities of B-glycosidases. Biotechnol. Lett. 24:1465-1471, 2002.
    • (2002) Biotechnol. Lett , vol.24 , pp. 1465-1471
    • Hansson, T.1    Adlercreutz, P.2
  • 101
    • 0037420306 scopus 로고    scopus 로고
    • Maillard reactions and increased enzyme inactivation during oligosaccharide synthesis by a hyperthermophilic glycosidase
    • Bruins, M.E., E.W. Van Hellemond, A.E.M. Janssen, R.M. Boom. Maillard reactions and increased enzyme inactivation during oligosaccharide synthesis by a hyperthermophilic glycosidase. Biotechnol. Bioeng. 81:546-552, 2003.
    • (2003) Biotechnol. Bioeng , vol.81 , pp. 546-552
    • Bruins, M.E.1    Van Hellemond, E.W.2    Janssen, A.E.M.3    Boom, R.M.4
  • 102
    • 0037413442 scopus 로고    scopus 로고
    • Enzyme inactivation due to Maillard reactions during oligosaccharide synthesis by a hyperthermophilic glyclosidase: Influence of enzyme immobilization
    • Bruins, M.E., A.J.H. Thewessen, A.E.M. Janssen, R.M. Boom. Enzyme inactivation due to Maillard reactions during oligosaccharide synthesis by a hyperthermophilic glyclosidase: influence of enzyme immobilization. J. Mol. Catal. B Enzym. 21:31-34, 2003.
    • (2003) J. Mol. Catal. B Enzym , vol.21 , pp. 31-34
    • Bruins, M.E.1    Thewessen, A.J.H.2    Janssen, A.E.M.3    Boom, R.M.4
  • 103
    • 3343015826 scopus 로고    scopus 로고
    • Enzyme glycation influences product yields during oligosaccharide synthesis by reverse hydrolysis
    • Maitin, V., R.A. Rastall. Enzyme glycation influences product yields during oligosaccharide synthesis by reverse hydrolysis. J. Mol. Catal. B Enzym. 30:195-202, 2004.
    • (2004) J. Mol. Catal. B Enzym , vol.30 , pp. 195-202
    • Maitin, V.1    Rastall, R.A.2
  • 104
    • 0034616232 scopus 로고    scopus 로고
    • Regioselective synthesis of p-nitrophenyl glycosides of B-D-galactopyranosyl-disaccharides by transglycosylation with B-D-galactosidases
    • Zeng, X., R. Yoshino, T. Murata, K. Ajisaka, T. Usui. Regioselective synthesis of p-nitrophenyl glycosides of B-D-galactopyranosyl-disaccharides by transglycosylation with B-D-galactosidases. Carbohydr. Res. 325:120-131, 2000.
    • (2000) Carbohydr. Res , vol.325 , pp. 120-131
    • Zeng, X.1    Yoshino, R.2    Murata, T.3    Ajisaka, K.4    Usui, T.5
  • 105
    • 0035377358 scopus 로고    scopus 로고
    • Synthesis and fermentation properties of novel galacto-oligosaccharides by B-galactosidases from Bifidobacterium species
    • Rabiu, B.A., A.J. Jay, G.R. Gibson, R.A. Rastall. Synthesis and fermentation properties of novel galacto-oligosaccharides by B-galactosidases from Bifidobacterium species. Appl. Environ. Microbiol. 67:2526-2530, 2001.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 2526-2530
    • Rabiu, B.A.1    Jay, A.J.2    Gibson, G.R.3    Rastall, R.A.4
  • 106
    • 1542359002 scopus 로고    scopus 로고
    • Synthesis of FimH receptor-active manno-oligosaccharides by reverse hydrolysis using A-mannosidases from Penicillium citrinum, Aspergillus phoenicis and almond
    • Maitin, V., V. Athanasopoulos, R.A. Rastall. Synthesis of FimH receptor-active manno-oligosaccharides by reverse hydrolysis using A-mannosidases from Penicillium citrinum, Aspergillus phoenicis and almond. Appl. Microbiol. Biotechnol. 63:666-671, 2004.
    • (2004) Appl. Microbiol. Biotechnol , vol.63 , pp. 666-671
    • Maitin, V.1    Athanasopoulos, V.2    Rastall, R.A.3
  • 107
    • 0030780520 scopus 로고    scopus 로고
    • The effects of organic solvents on the synthesis of galactose disaccha-rides using B-galactosidases
    • Finch, P., J.H. Yoon. The effects of organic solvents on the synthesis of galactose disaccha-rides using B-galactosidases. Carbohydr. Res. 303:339-345, 1997.
    • (1997) Carbohydr. Res , vol.303 , pp. 339-345
    • Finch, P.1    Yoon, J.H.2
  • 108
    • 0026899850 scopus 로고
    • Effect of organic solvents on stability of two glycosidases and on glucoamylase-catalysed oligosaccharide synthesis
    • Laroute, V., R.-M. Willemot. Effect of organic solvents on stability of two glycosidases and on glucoamylase-catalysed oligosaccharide synthesis. Enzyme Microb. Technol. 14:528-534, 1992.
    • (1992) Enzyme Microb. Technol , vol.14 , pp. 528-534
    • Laroute, V.1    Willemot, R.-M.2
  • 109
    • 0028260340 scopus 로고
    • Disaccharide production by glucoamylase in aqueous ether mixtures
    • Cantarella, L., Z.L. Nikolov, P.J. Reilly. Disaccharide production by glucoamylase in aqueous ether mixtures. Enzyme Microb. Technol. 16:383-387, 1994.
    • (1994) Enzyme Microb. Technol , vol.16 , pp. 383-387
    • Cantarella, L.1    Nikolov, Z.L.2    Reilly, P.J.3
  • 110
    • 0035715016 scopus 로고    scopus 로고
    • Optimization of galactooligosaccharide production from lactose using B-glycosidases from hyperthermophiles
    • Hansson, T., P. Adlercreutz. Optimization of galactooligosaccharide production from lactose using B-glycosidases from hyperthermophiles. Food Biotechnol. 15:79-97, 2001.
    • (2001) Food Biotechnol , vol.15 , pp. 79-97
    • Hansson, T.1    Adlercreutz, P.2
  • 112
    • 0035814182 scopus 로고    scopus 로고
    • Synthesis of galacto-oligosaccharides in AOT/isooctane reverse micelles by B-galactosidase
    • Chen, S.-X., D.-Z. Wei, Z.-H. Hu. Synthesis of galacto-oligosaccharides in AOT/isooctane reverse micelles by B-galactosidase. J. Mol. Catal. B Enzym. 16:109-114, 2001.
    • (2001) J. Mol. Catal. B Enzym , vol.16 , pp. 109-114
    • Chen, S.-X.1    Wei, D.-Z.2    Hu, Z.-H.3
  • 114
    • 17344386610 scopus 로고    scopus 로고
    • Towards regioselective synthesis of oligosaccharides by the use of A-glucosidases with different substrate specificity
    • Malá, Š., H. Dvoráková, R. Hrabal, B. Králová. Towards regioselective synthesis of oligosaccharides by the use of A-glucosidases with different substrate specificity. Carbohydr. Res. 322:209-218, 1999.
    • (1999) Carbohydr. Res , vol.322 , pp. 209-218
    • Malá, S.1    Dvoráková, H.2    Hrabal, R.3    Králová, B.4
  • 115
    • 0028871272 scopus 로고
    • Oligosaccharides synthesis by free and immobilized B-galactosidases from Thermus aquaticus YT-1
    • Berger, J.L., B.H. Lee, C. Lacroix. Oligosaccharides synthesis by free and immobilized B-galactosidases from Thermus aquaticus YT-1. Biotechnol. Lett. 17:1077-1080, 1995.
    • (1995) Biotechnol. Lett , vol.17 , pp. 1077-1080
    • Berger, J.L.1    Lee, B.H.2    Lacroix, C.3
  • 116
    • 0032211708 scopus 로고    scopus 로고
    • Continuous production of galacto-oligosaccharides from lactose by Bullera singularis B-galactosidase immobilized in chitosan beads
    • H.-J. Shin, J.-M. Park, J.-W. Yang. Continuous production of galacto-oligosaccharides from lactose by Bullera singularis B-galactosidase immobilized in chitosan beads. Process Biochem. 33:787-792, 1998.
    • (1998) Process Biochem , vol.33 , pp. 787-792
    • Shin, H.-J.1    Park, J.-M.2    Yang, J.-W.3
  • 117
    • 0031804544 scopus 로고    scopus 로고
    • Production of galactooligosaccharides by B-galactosidase immobilized on glutaraldehyde-treated chitosan beads
    • Sheu, D.-C., S.-Y. Li, K.-J. Duan, C.W. Chen. Production of galactooligosaccharides by B-galactosidase immobilized on glutaraldehyde-treated chitosan beads. Biotechnol. Techniques 12:273-276, 1998.
    • (1998) Biotechnol. Techniques , vol.12 , pp. 273-276
    • Sheu, D.-C.1    Li, S.-Y.2    Duan, K.-J.3    Chen, C.W.4
  • 118
    • 0037021799 scopus 로고    scopus 로고
    • Production of galacto-oligosaccharides from lactose by Aspergillus oryzae B-galactosidase immobilized on cotton cloth
    • Albayrak, N., S.-T. Yang. Production of galacto-oligosaccharides from lactose by Aspergillus oryzae B-galactosidase immobilized on cotton cloth. Biotechnol. Bioeng. 77:8-19, 2002.
    • (2002) Biotechnol. Bioeng , vol.77 , pp. 8-19
    • Albayrak, N.1    Yang, S.-T.2
  • 119
    • 0027334862 scopus 로고
    • Gluco-oligosaccharide synthesis by free and immobilized B-glucosidase
    • Ravet, C., D. Thomas, M.D. Legoy. Gluco-oligosaccharide synthesis by free and immobilized B-glucosidase. Biotechnol. Bioeng. 42:303-308, 1993.
    • (1993) Biotechnol. Bioeng , vol.42 , pp. 303-308
    • Ravet, C.1    Thomas, D.2    Legoy, M.D.3
  • 120
    • 0031964290 scopus 로고    scopus 로고
    • Synthesis of oligosaccharides using immobilized 1,2-A-mam-nosidase from Aspergillus phoenicis: Immobilization dependent modulation of product spectrum
    • Suwasono, S., R.A. Rastall. Synthesis of oligosaccharides using immobilized 1,2-A-mam-nosidase from Aspergillus phoenicis: immobilization dependent modulation of product spectrum. Biotechnol. Lett. 20:15-17, 1998.
    • (1998) Biotechnol. Lett , vol.20 , pp. 15-17
    • Suwasono, S.1    Rastall, R.A.2
  • 122
    • 0036658176 scopus 로고    scopus 로고
    • Biosynthetic activity of recombinant Escherichia coli- expressed Pichia etchellsii B-glucosidase II
    • Bhatia, Y., S. Mishra, V.S. Bisaria. Biosynthetic activity of recombinant Escherichia coli- expressed Pichia etchellsii B-glucosidase II. Appl. Biochem. Biotechnol. 102,103:367-379, 2002.
    • (2002) Appl. Biochem. Biotechnol , vol.102 , Issue.103 , pp. 367-379
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 123
    • 0032503519 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosi-dases for oligosaccharide synthesis
    • Mackenzie, L.F., Q. Wang, R.A.J. Warren, S.G. Withers. Glycosynthases: mutant glycosi-dases for oligosaccharide synthesis. J. Am. Chem. Soc. 120:5583-5584, 1998.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 5583-5584
    • Mackenzie, L.F.1    Wang, Q.2    Warren, R.A.J.3    Withers, S.G.4
  • 124
    • 0035931580 scopus 로고    scopus 로고
    • Glycosynthases: New enzymes for oligosaccharide synthesis
    • Moracci, M., A. Trincone, M. Rossi. Glycosynthases: new enzymes for oligosaccharide synthesis. J. Mol. Catal. B Enzym. 155-163, 2001.
    • (2001) J. Mol. Catal. B Enzym , pp. 155-163
    • Moracci, M.1    Trincone, A.2    Rossi, M.3
  • 125
    • 0036015487 scopus 로고    scopus 로고
    • Glycosynthases: New tools for oligosaccharide synthesis
    • Jakeman, D.L., S.G. Withers. Glycosynthases: new tools for oligosaccharide synthesis. Trends Glycosci. Glycotechnol. 14:13-25, 2002.
    • (2002) Trends Glycosci. Glycotechnol , vol.14 , pp. 13-25
    • Jakeman, D.L.1    Withers, S.G.2
  • 126
    • 0036303152 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosidases for glycoside synthesis
    • Williams, S.J., S.G. Withers. Glycosynthases: mutant glycosidases for glycoside synthesis. Aust. J. Chem. 55:3-12, 2002.
    • (2002) Aust. J. Chem , vol.55 , pp. 3-12
    • Williams, S.J.1    Withers, S.G.2
  • 127
    • 0028191018 scopus 로고
    • Changing enzymatic reaction mechanisms by mutagenesis: Conversion of a retaining glucosidase to an inverting enzyme
    • Wang, Q., R.W. Graham, D. Trimbur, R.A.J. Warren, S.G. Withers. Changing enzymatic reaction mechanisms by mutagenesis: conversion of a retaining glucosidase to an inverting enzyme. J. Am. Chem. Soc. 116:11594-11595, 1994.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 11594-11595
    • Wang, Q.1    Graham, R.W.2    Trimbur, D.3    Warren, R.A.J.4    Withers, S.G.5
  • 129
    • 0033954715 scopus 로고    scopus 로고
    • The E358S mutant of Agrobacterium sp. B-glucosidase is a greatly improved glycosynthase
    • Mayer, C., D.L. Zechel, S.P. Reid, R.A.J. Warren, S.G. Withers. The E358S mutant of Agrobacterium sp. B-glucosidase is a greatly improved glycosynthase. FEBS Lett. 466:40-44, 2000.
    • (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
  • 131
    • 0035813818 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by coupled endo-glycosynthases of different specificity: A straightforward preparation of two mixed-linkage hexasaccharide substrates of 1,3/1,4- B-glucanases
    • Faijes, M., J.K. Fairweather, D. Hugues, A. Planas. Oligosaccharide synthesis by coupled endo-glycosynthases of different specificity: a straightforward preparation of two mixed-linkage hexasaccharide substrates of 1,3/1,4- B-glucanases. Chem. Eur. J. 7:4651-4655, 2001.
    • (2001) Chem. Eur. J , vol.7 , pp. 4651-4655
    • Faijes, M.1    Fairweather, J.K.2    Hugues, D.3    Planas, A.4
  • 132
    • 0036436302 scopus 로고    scopus 로고
    • On expanding the repertoire of glycosynthases: Mutant B-galactosidases forming B-(1,6)-linkages
    • Jakeman, D.L., S.G. Withers. On expanding the repertoire of glycosynthases: mutant B-galactosidases forming B-(1,6)-linkages. Can. J. Chem. 80:866-870, 2002.
    • (2002) Can. J. Chem , vol.80 , pp. 866-870
    • Jakeman, D.L.1    Withers, S.G.2
  • 137
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner, O., F.H. Arnold. Directed evolution of enzyme catalysts. Trends Biotech. 15:523-530, 1997.
    • (1997) Trends Biotech , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 138
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W.P.C. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA 91:10747-10751, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 139
    • 0030754926 scopus 로고    scopus 로고
    • Optimization of DNA shuffling for high-fidelity recombination
    • Zhao, H., F.H. Arnold. Optimization of DNA shuffling for high-fidelity recombination. Nucleic Acids Res. 25:1307-1308, 1997.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1307-1308
    • Zhao, H.1    Arnold, F.H.2
  • 140
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., L. Giver, Z. Shao, J.A. Affholter, F.H. Arnold. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat. Biotechnol. 16:258-261, 1998.
    • (1998) Nat. Biotechnol , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5
  • 143
    • 0031874849 scopus 로고    scopus 로고
    • Improved properties of FLP recombinase evolved by cycling mutagenesis
    • Buchholz, F., P.-O. Angrand, A.F. Stewart. Improved properties of FLP recombinase evolved by cycling mutagenesis. Nat. Biotechnol. 16:657-662, 1998.
    • (1998) Nat. Biotechnol , vol.16 , pp. 657-662
    • Buchholz, F.1    Angrand, P.-O.2    Stewart, A.F.3
  • 144
    • 0033567665 scopus 로고    scopus 로고
    • Recombination and chimeragenesis by in vitro hetero-duplex formation and in vivo repair
    • Volkov, A.A., Z. Shao, F.H. Arnold. Recombination and chimeragenesis by in vitro hetero-duplex formation and in vivo repair. Nucleic Acids Res. 27, e18:1-6, 1999.
    • (1999) Nucleic Acids Res , vol.27 , Issue.E18 , pp. 1-6
    • Volkov, A.A.1    Shao, Z.2    Arnold, F.H.3
  • 145
    • 0002273141 scopus 로고    scopus 로고
    • Engineering a revolution
    • Affholter, J., F. Arnold. Engineering a revolution. Chem. Br. 35:48-51, 1999.
    • (1999) Chem. Br , vol.35 , pp. 48-51
    • Affholter, J.1    Arnold, F.2
  • 146
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang, J.-H., G. Dawes, W.P.C. Stemmer. Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA 94:4504-4509, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.-H.1    Dawes, G.2    Stemmer, W.P.C.3
  • 149
    • 0002626566 scopus 로고    scopus 로고
    • Unnatural selection: Molecular sex for fun and profit
    • Arnold, F.H. Unnatural selection: molecular sex for fun and profit. Eng. Sci. 1/2:41-50, 1999.
    • (1999) Eng. Sci , vol.1-2 , pp. 41-50
    • Arnold, F.H.1
  • 150
    • 0034999624 scopus 로고    scopus 로고
    • Directed evolution of new glycosynthases from Agrobacterium B-glucosidase: A general screen to detect enzymes for oligosaccharide synthesis
    • Mayer, C., D.L. Jakeman, M. Mah, G. Karjala, L. Gal, R.A.J. Warren, S.G. Withers. Directed evolution of new glycosynthases from Agrobacterium B-glucosidase: a general screen to detect enzymes for oligosaccharide synthesis. Chem. Biol. 8:437-443, 2001.
    • (2001) Chem. Biol , vol.8 , pp. 437-443
    • Mayer, C.1    Jakeman, D.L.2    Mah, M.3    Karjala, G.4    Gal, L.5    Warren, R.A.J.6    Withers, S.G.7
  • 151
    • 33748907883 scopus 로고    scopus 로고
    • Glycosidase-catalysed oligosac-charide synthesis of di-, tri- and tetra-saccharides using the N-acetylhexosaminidase from Aspergillus oryzae and B-galactosidase from
    • Singh, S., M. Michaela Scigelova, G. Vic, D.H.G. Crout. Glycosidase-catalysed oligosac-charide synthesis of di-, tri- and tetra-saccharides using the N-acetylhexosaminidase from Aspergillus oryzae and B-galactosidase from Bacillus circulans. J. Chem. Soc. Perkin Trans. 1(16):1921-1926, 1996.
    • (1996) Bacillus circulans. J. Chem. Soc. Perkin Trans , vol.1 , Issue.16 , pp. 1921-1926
    • Singh, S.1    Michaela Scigelova, M.2    Vic, G.3    Crout, D.H.G.4
  • 152
    • 0032727926 scopus 로고    scopus 로고
    • Enzymatic synthesis of galactose-containing disaccharides employing B-galactosidase from
    • Farkas, E., J. Thiem. Enzymatic synthesis of galactose-containing disaccharides employing B-galactosidase from Bacillus circulans. Eur. J. Org. Chem. 11:3073-3077, 1999.
    • (1999) Bacillus circulans. Eur. J. Org. Chem , vol.11 , pp. 3073-3077
    • Farkas, E.1    Thiem, J.2
  • 153
    • 0031505852 scopus 로고    scopus 로고
    • Glycozymes: Tools for oligosaccharide synthesis and targets for drug development
    • Ichikawa, Y. Glycozymes: tools for oligosaccharide synthesis and targets for drug development. Trends Glycosci. Glycotechnol. 9:S47-S59, 1997.
    • (1997) Trends Glycosci. Glycotechnol , vol.9 , pp. S47-S59
    • Ichikawa, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.