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Volumn 62, Issue 40, 2014, Pages 9615-9631

Methods for improving enzymatic trans-glycosylation for synthesis of human milk oligosaccharide biomimetics

Author keywords

biomimetic glycans; human milk oligosaccharides; sialidase; trans glycosylation; l fucosidase; galactosidase

Indexed keywords

GALACTOSIDASES; GLYCANS; HUMAN MILK OLIGOSACCHARIDES; SIALIDASES; TRANS-GLYCOSYLATION;

EID: 84907930217     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf502619p     Document Type: Review
Times cited : (83)

References (116)
  • 1
    • 79954416532 scopus 로고    scopus 로고
    • A comparative study of the regioselectivity of the β-galactosidases from Kluyveromyces lactis and Bacillus circulans in the enzymatic synthesis of N -acetyl-lactosamine in aqueous media
    • Bridiau, N.; Maugard, T. A comparative study of the regioselectivity of the β-galactosidases from Kluyveromyces lactis and Bacillus circulans in the enzymatic synthesis of N -acetyl-lactosamine in aqueous media Biotechnol. Prog. 2011, 27, 386-394
    • (2011) Biotechnol. Prog. , vol.27 , pp. 386-394
    • Bridiau, N.1    Maugard, T.2
  • 3
    • 84862816742 scopus 로고    scopus 로고
    • Synthesis of galactosyl sucralose by β-galactosidase from Lactobacillus bulgaricus L3
    • Lu, L.; Xu, S.; Jin, L.; Zhang, D.; Li, Y.; Xiao, M. Synthesis of galactosyl sucralose by β-galactosidase from Lactobacillus bulgaricus L3 Food Chem. 2012, 134, 269-275
    • (2012) Food Chem. , vol.134 , pp. 269-275
    • Lu, L.1    Xu, S.2    Jin, L.3    Zhang, D.4    Li, Y.5    Xiao, M.6
  • 5
    • 84878566892 scopus 로고    scopus 로고
    • Synthesis of fucosyl- N -acetylglucosamine disaccharides by transfucosylation using α- L -fucosidases from Lactobacillus casei
    • Rodríguez-Díaz, J.; Carbajo, R. J.; Pineda-Lucena, A.; Monedero, V.; Yebra, M. J. Synthesis of fucosyl- N -acetylglucosamine disaccharides by transfucosylation using α- l -fucosidases from Lactobacillus casei Appl. Environ. Microbiol. 2013, 79, 3847-3850
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 3847-3850
    • Rodríguez-Díaz, J.1    Carbajo, R.J.2    Pineda-Lucena, A.3    Monedero, V.4    Yebra, M.J.5
  • 8
    • 0028672815 scopus 로고
    • Regeneration of sugar nucleotide for enzymatic oligosaccharide synthesis
    • Ichikawa, Y.; Wang, R.; Wong, C.-H. Regeneration of sugar nucleotide for enzymatic oligosaccharide synthesis Methods Enzymol. 1994, 247, 107-127
    • (1994) Methods Enzymol. , vol.247 , pp. 107-127
    • Ichikawa, Y.1    Wang, R.2    Wong, C.-H.3
  • 9
    • 41549135510 scopus 로고    scopus 로고
    • Genetic engineering of Escherichia coli for the economical production of sialylated oligosaccharides
    • Fierfort, N.; Samain, E. Genetic engineering of Escherichia coli for the economical production of sialylated oligosaccharides J. Biotechnol. 2008, 134, 261-265
    • (2008) J. Biotechnol. , vol.134 , pp. 261-265
    • Fierfort, N.1    Samain, E.2
  • 10
    • 77955771975 scopus 로고    scopus 로고
    • Efficient synthesis of 6'-sialyllactose, 6,6'-disialyllactose, and 6'-KDO-lactose by metabolically engineered E. Coli expressing a multifunctional sialyltransferase from the Photobacterium sp. JT-ISH-224
    • Drouillard, S.; Mine, T.; Kajiwara, H.; Yamamoto, T.; Samain, E. Efficient synthesis of 6'-sialyllactose, 6,6'-disialyllactose, and 6'-KDO-lactose by metabolically engineered E. coli expressing a multifunctional sialyltransferase from the Photobacterium sp. JT-ISH-224 Carbohydr. Res. 2010, 345, 1394-1399
    • (2010) Carbohydr. Res. , vol.345 , pp. 1394-1399
    • Drouillard, S.1    Mine, T.2    Kajiwara, H.3    Yamamoto, T.4    Samain, E.5
  • 11
    • 84864465909 scopus 로고    scopus 로고
    • Human milk oligosaccharides: Every baby needs a sugar mama
    • Bode, L. Human milk oligosaccharides: every baby needs a sugar mama Glycobiology 2012, 22, 1147-1162
    • (2012) Glycobiology , vol.22 , pp. 1147-1162
    • Bode, L.1
  • 12
    • 0036332863 scopus 로고    scopus 로고
    • Synthesis of tumor-associated glycopeptides antigens
    • Brocke, C.; Kunz, H. Synthesis of tumor-associated glycopeptides antigens Bioorg. Med. Chem. 2002, 10, 3085-3112
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3085-3112
    • Brocke, C.1    Kunz, H.2
  • 13
    • 0032832941 scopus 로고    scopus 로고
    • Enzymatic synthesis of α- L -fucosyl- N -acetyllactosamines and 3'- O -α- l -fucosyllactose utilizing α- L -fucosidases
    • Murata, T.; Morimoto, S.; Zeng, X.; Watanabe, S.; Usui, T. Enzymatic synthesis of α- l -fucosyl- N -acetyllactosamines and 3'- O -α- l -fucosyllactose utilizing α- l -fucosidases Carbohydr. Res. 1999, 320, 192-199
    • (1999) Carbohydr. Res. , vol.320 , pp. 192-199
    • Murata, T.1    Morimoto, S.2    Zeng, X.3    Watanabe, S.4    Usui, T.5
  • 14
    • 0030590838 scopus 로고    scopus 로고
    • Complete synthesis of 3'-sialyl- N -acetyllactosamine by regioselective transglycosylation
    • Vetere, A.; Paoletti, S. Complete synthesis of 3'-sialyl- N -acetyllactosamine by regioselective transglycosylation FEBS Lett. 1996, 399, 203-206
    • (1996) FEBS Lett. , vol.399 , pp. 203-206
    • Vetere, A.1    Paoletti, S.2
  • 15
    • 0033975998 scopus 로고    scopus 로고
    • Regiospecific glycosidase-assisted synthesis of lacto- N -biose i (Galβ1-3GlcNAc) and 3'-sialyl-lacto- N -biose i (NeuAcα2-3Galβ1-3GlcNAc)
    • Vetere, A.; Miletich, M.; Bosco, M.; Paoletti, S. Regiospecific glycosidase-assisted synthesis of lacto- N -biose I (Galβ1-3GlcNAc) and 3'-sialyl-lacto- N -biose I (NeuAcα2-3Galβ1-3GlcNAc) Eur. J. Biochem. 2000, 267, 942-949
    • (2000) Eur. J. Biochem. , vol.267 , pp. 942-949
    • Vetere, A.1    Miletich, M.2    Bosco, M.3    Paoletti, S.4
  • 16
    • 76749088556 scopus 로고    scopus 로고
    • Recent advances refining galactooligosaccharide production from lactose
    • Gosling, A.; Stevens, G. W.; Barber, A. R.; Kentish, S. E.; Gras, S. L. Recent advances refining galactooligosaccharide production from lactose Food Chem. 2010, 121, 307-318
    • (2010) Food Chem. , vol.121 , pp. 307-318
    • Gosling, A.1    Stevens, G.W.2    Barber, A.R.3    Kentish, S.E.4    Gras, S.L.5
  • 17
    • 0026655074 scopus 로고
    • Enzyme-catalyzed oligosaccharide synthesis
    • Ichikawa, Y.; Look, G. C.; Wong, C.-H. Enzyme-catalyzed oligosaccharide synthesis Anal. Biochem. 1992, 202, 215-238
    • (1992) Anal. Biochem. , vol.202 , pp. 215-238
    • Ichikawa, Y.1    Look, G.C.2    Wong, C.-H.3
  • 18
    • 0022630151 scopus 로고
    • Mechanism and yields in enzyme catalysed equilibrium and kinetically controlled synthesis of β-lactam antibiotics, peptides and other condensation products
    • Kasche, V. Mechanism and yields in enzyme catalysed equilibrium and kinetically controlled synthesis of β-lactam antibiotics, peptides and other condensation products Enzyme Microb. Technol. 1986, 8, 4-16
    • (1986) Enzyme Microb. Technol. , vol.8 , pp. 4-16
    • Kasche, V.1
  • 19
    • 0034618243 scopus 로고    scopus 로고
    • The efficient enzymatic synthesis of N -acetyllactosamine in an organic co-solvent
    • Yoon, J. H.; Rhee, J. S. The efficient enzymatic synthesis of N -acetyllactosamine in an organic co-solvent Carbohydr. Res. 2000, 327, 377-383
    • (2000) Carbohydr. Res. , vol.327 , pp. 377-383
    • Yoon, J.H.1    Rhee, J.S.2
  • 20
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland, D. Stereochemistry and the mechanism of enzymatic reactions Biol. Rev. 1953, 28, 416-436
    • (1953) Biol. Rev. , vol.28 , pp. 416-436
    • Koshland, D.1
  • 22
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates and products. I. Nomenclature and rate equations
    • Cleland, W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates and products. I. Nomenclature and rate equations Biochim. Biophys. Acta 1963, 67, 104-137
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 23
    • 0016774185 scopus 로고
    • A probable oxocarbonium ion in the reaction mechanism of small intestinal sucrase and isomaltase
    • Cogoli, A.; Semenza, G. A probable oxocarbonium ion in the reaction mechanism of small intestinal sucrase and isomaltase J. Biol. Chem. 1975, 250, 7802-7809
    • (1975) J. Biol. Chem. , vol.250 , pp. 7802-7809
    • Cogoli, A.1    Semenza, G.2
  • 24
    • 0342814062 scopus 로고
    • α-Glucosidase from grape berries: Partial purification and characterization
    • Peruffo, A. D. B.; Renosto, F.; Pallavicini, C. α-Glucosidase from grape berries: partial purification and characterization Planta 1978, 142, 195-201
    • (1978) Planta , vol.142 , pp. 195-201
    • Peruffo, A.D.B.1    Renosto, F.2    Pallavicini, C.3
  • 25
    • 0036203356 scopus 로고    scopus 로고
    • Kinetic model for synthesis of fructosyl-stevioside using suspended β-fructofuranosidase
    • Suzuki, K.; Fukumura, T.; Shibasaki-Kitakawa, N.; Yonemoto, T. Kinetic model for synthesis of fructosyl-stevioside using suspended β-fructofuranosidase Biochem. Eng. J. 2002, 10, 207-215
    • (2002) Biochem. Eng. J. , vol.10 , pp. 207-215
    • Suzuki, K.1    Fukumura, T.2    Shibasaki-Kitakawa, N.3    Yonemoto, T.4
  • 26
    • 40849118185 scopus 로고    scopus 로고
    • Kinetic and mechanistic analysis of Trypanosoma cruzi trans-sialidase reveals a classical ping-pong mechanism with acid/base catalysis
    • Damager, I.; Buchini, S.; Amaya, M. F.; Buschiazzo, A.; Alzari, P.; Frasch, A. C.; Watts, A.; Withers, S. G. Kinetic and mechanistic analysis of Trypanosoma cruzi trans-sialidase reveals a classical ping-pong mechanism with acid/base catalysis Biochemistry 2008, 47, 3507-3512
    • (2008) Biochemistry , vol.47 , pp. 3507-3512
    • Damager, I.1    Buchini, S.2    Amaya, M.F.3    Buschiazzo, A.4    Alzari, P.5    Frasch, A.C.6    Watts, A.7    Withers, S.G.8
  • 29
    • 2942741170 scopus 로고    scopus 로고
    • α- l -Fucosidases: Exoglycosidases with unusual transglycosylation properties
    • Berteau, O.; Bielicki, J.; Kilonda, A.; Machy, D.; Anson, D. S.; Kenne, L. α- l -Fucosidases: exoglycosidases with unusual transglycosylation properties Biochemistry 2004, 43, 7881-7891
    • (2004) Biochemistry , vol.43 , pp. 7881-7891
    • Berteau, O.1    Bielicki, J.2    Kilonda, A.3    Machy, D.4    Anson, D.S.5    Kenne, L.6
  • 30
    • 0035813475 scopus 로고    scopus 로고
    • Influence of water activity on the competition between β-glycosidase catalysed transglycosylation and hydrolysis in aqueous hexanol
    • Hansson, T.; Andersson, M.; Wehtje, E.; Adlercreutz, P. Influence of water activity on the competition between β-glycosidase catalysed transglycosylation and hydrolysis in aqueous hexanol Enzyme Microb. Technol. 2001, 29, 527-534
    • (2001) Enzyme Microb. Technol. , vol.29 , pp. 527-534
    • Hansson, T.1    Andersson, M.2    Wehtje, E.3    Adlercreutz, P.4
  • 31
    • 33845397675 scopus 로고    scopus 로고
    • Influence of ionic liquid cosolvent on transgalactosylation reactions catalyzed by thermostable β-glycosylhydrolase CelB from Pyrococcus furiosus
    • Lang, M.; Kamrat, T.; Nidetzky, B. Influence of ionic liquid cosolvent on transgalactosylation reactions catalyzed by thermostable β-glycosylhydrolase CelB from Pyrococcus furiosus Biotechnol. Bioeng. 2006, 95, 1093-1100
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 1093-1100
    • Lang, M.1    Kamrat, T.2    Nidetzky, B.3
  • 32
    • 84982635826 scopus 로고
    • Applications of enzymes in synthetic carbohydrate chemistry
    • Thiem, J. Applications of enzymes in synthetic carbohydrate chemistry FEMS Microbiol. Rev. 1995, 16, 193-211
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 193-211
    • Thiem, J.1
  • 33
    • 33745746213 scopus 로고    scopus 로고
    • Glycosyl hydrolases and glycosyltransferases in the synthesis of oligosaccharides
    • Trincone, A.; Giordano, A. Glycosyl hydrolases and glycosyltransferases in the synthesis of oligosaccharides Curr. Org. Chem. 2006, 10, 1163-1193
    • (2006) Curr. Org. Chem. , vol.10 , pp. 1163-1193
    • Trincone, A.1    Giordano, A.2
  • 35
    • 0028761239 scopus 로고
    • Regioselective transglycosylation in the synthesis of oligosaccharides: Comparison of β-galactosidases and sialidases of various origins
    • Ajisaka, K.; Fujimoto, H.; Isomura, M. Regioselective transglycosylation in the synthesis of oligosaccharides: comparison of β-galactosidases and sialidases of various origins Carbohydr. Res. 1994, 259, 103-115
    • (1994) Carbohydr. Res. , vol.259 , pp. 103-115
    • Ajisaka, K.1    Fujimoto, H.2    Isomura, M.3
  • 36
    • 0037249715 scopus 로고    scopus 로고
    • Regioselective synthesis of galactosylated tri- and tetrasaccharides by use of β-galactosidase from Bacillus circulans
    • Farkas, E.; Schmidt, U.; Thiem, J.; Kowalczyk, J.; Kunz, M.; Vogel, M. Regioselective synthesis of galactosylated tri- and tetrasaccharides by use of β-galactosidase from Bacillus circulans Synthesis 2003, 5, 699-706
    • (2003) Synthesis , vol.5 , pp. 699-706
    • Farkas, E.1    Schmidt, U.2    Thiem, J.3    Kowalczyk, J.4    Kunz, M.5    Vogel, M.6
  • 37
    • 33748234464 scopus 로고
    • Chemoenzymatic syntheses of sialyloligosaccharides with immobilized sialidase
    • Thiem, J.; Sauerbrei, B. Chemoenzymatic syntheses of sialyloligosaccharides with immobilized sialidase Angew. Chem., Int. Ed. Engl. 1991, 30, 1503-1505
    • (1991) Angew. Chem., Int. Ed. Engl. , vol.30 , pp. 1503-1505
    • Thiem, J.1    Sauerbrei, B.2
  • 38
    • 0027314040 scopus 로고
    • Enzymatic characterization of β- D -galactoside α2,3- trans -sialidase from Trypanosoma cruzi
    • Scudder, P.; Doom, J. P.; Chuenkova, M.; Manger, I. D.; Pereira, M. E. A. Enzymatic characterization of β- d -galactoside α2,3- trans -sialidase from Trypanosoma cruzi J. Biol. Chem. 1993, 268, 9886-9891
    • (1993) J. Biol. Chem. , vol.268 , pp. 9886-9891
    • Scudder, P.1    Doom, J.P.2    Chuenkova, M.3    Manger, I.D.4    Pereira, M.E.A.5
  • 39
    • 0034670518 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of sialyl oligosaccharides with sialidases employing transglycosylation methodology
    • Schmidt, D.; Sauerbrei, B.; Thiem, J. Chemoenzymatic synthesis of sialyl oligosaccharides with sialidases employing transglycosylation methodology J. Org. Chem. 2000, 65, 8518-8526
    • (2000) J. Org. Chem. , vol.65 , pp. 8518-8526
    • Schmidt, D.1    Sauerbrei, B.2    Thiem, J.3
  • 40
    • 84891802531 scopus 로고    scopus 로고
    • Optimizing the biocatalytic productivity of an engineered sialidase from Trypanosoma rangeli for 3'-sialyllactose production
    • Zeuner, B.; Luo, J.; Nyffenegger, C.; Aumala, V.; Mikkelsen, J. D.; Meyer, A. S. Optimizing the biocatalytic productivity of an engineered sialidase from Trypanosoma rangeli for 3'-sialyllactose production Enzyme Microb. Technol. 2014, 55, 85-93
    • (2014) Enzyme Microb. Technol. , vol.55 , pp. 85-93
    • Zeuner, B.1    Luo, J.2    Nyffenegger, C.3    Aumala, V.4    Mikkelsen, J.D.5    Meyer, A.S.6
  • 41
    • 84899922442 scopus 로고    scopus 로고
    • Improvement of trans -sialylation versus hydrolysis activity of an engineered sialidase from Trypanosoma rangeli by use of co-solvents
    • Zeuner, B.; Riisager, A.; Mikkelsen, J. D.; Meyer, A. S. Improvement of trans -sialylation versus hydrolysis activity of an engineered sialidase from Trypanosoma rangeli by use of co-solvents Biotechnol. Lett. 2014, 36, 1315-1320
    • (2014) Biotechnol. Lett. , vol.36 , pp. 1315-1320
    • Zeuner, B.1    Riisager, A.2    Mikkelsen, J.D.3    Meyer, A.S.4
  • 43
    • 84890846001 scopus 로고    scopus 로고
    • A Pasteurella multocida sialyltransferase displaying dual trans-sialidase activities for production of 3'-sialyl and 6'-sialyl glycans
    • Guo, Y.; Jers, C.; Meyer, A. S.; Arnous, A.; Li, H.; Kirpekar, F.; Mikkelsen, J. D. A Pasteurella multocida sialyltransferase displaying dual trans-sialidase activities for production of 3'-sialyl and 6'-sialyl glycans J. Biotechnol. 2014, 170, 60-67
    • (2014) J. Biotechnol. , vol.170 , pp. 60-67
    • Guo, Y.1    Jers, C.2    Meyer, A.S.3    Arnous, A.4    Li, H.5    Kirpekar, F.6    Mikkelsen, J.D.7
  • 45
    • 77953622356 scopus 로고    scopus 로고
    • Quantitation of N -acetylneuraminic (sialic) acid in bovine glycomacropeptide (GMP)
    • Fernando, S. F.; Woonton, B. W. Quantitation of N -acetylneuraminic (sialic) acid in bovine glycomacropeptide (GMP) J. Food Compos. Anal. 2010, 23, 359-366
    • (2010) J. Food Compos. Anal. , vol.23 , pp. 359-366
    • Fernando, S.F.1    Woonton, B.W.2
  • 46
    • 84867798511 scopus 로고    scopus 로고
    • Direct estimation of sialic acid in milk and milk products by fluorimetry and its application in detection of sweet whey adulteration in milk
    • Neelima; Rao, P. S.; Sharma, R.; Rajput, Y. S. Direct estimation of sialic acid in milk and milk products by fluorimetry and its application in detection of sweet whey adulteration in milk J. Dairy Res. 2012, 79, 495-501
    • (2012) J. Dairy Res. , vol.79 , pp. 495-501
    • Neelima1    Rao, P.S.2    Sharma, R.3    Rajput, Y.S.4
  • 47
    • 0026887671 scopus 로고
    • Variations and distributions of O-glycosidically linked sugar chains in bovine κ-casein
    • Saito, T.; Itoh, T. Variations and distributions of O-glycosidically linked sugar chains in bovine κ-casein J. Dairy Sci. 1992, 75, 1768-1774
    • (1992) J. Dairy Sci. , vol.75 , pp. 1768-1774
    • Saito, T.1    Itoh, T.2
  • 49
    • 0042071269 scopus 로고    scopus 로고
    • Glycosidase-catalyzed synthesis of fucosyl di- and trisaccharide derivatives using α- L -fucosidase from Alcaligenes sp
    • Zeng, X.; Murata, T.; Usui, T. Glycosidase-catalyzed synthesis of fucosyl di- and trisaccharide derivatives using α- l -fucosidase from Alcaligenes sp J. Carbohydr. Chem. 2003, 22, 309-316
    • (2003) J. Carbohydr. Chem. , vol.22 , pp. 309-316
    • Zeng, X.1    Murata, T.2    Usui, T.3
  • 50
    • 0031854865 scopus 로고    scopus 로고
    • An α- L -fucosidase from Penicillium multicolor as a candidate enzyme for the synthesis of α(1→3)-linked fucosyl oligosaccharides by transglycosylation
    • Ajisaka, K.; Fujimoto, H.; Miyasato, M. An α- l -fucosidase from Penicillium multicolor as a candidate enzyme for the synthesis of α(1→3)-linked fucosyl oligosaccharides by transglycosylation Carbohydr. Res. 1998, 309, 125-129
    • (1998) Carbohydr. Res. , vol.309 , pp. 125-129
    • Ajisaka, K.1    Fujimoto, H.2    Miyasato, M.3
  • 51
    • 33846591870 scopus 로고    scopus 로고
    • Directed evolution of the α- L -fucosidase from Thermotoga maritima into an α- L -transfucosidase
    • Osanjo, G.; Dion, M.; Drone, J.; Solleux, C.; Tran, V.; Rabiller, C.; Tellier, C. Directed evolution of the α- l -fucosidase from Thermotoga maritima into an α- l -transfucosidase Biochemistry 2007, 46, 1022-1033
    • (2007) Biochemistry , vol.46 , pp. 1022-1033
    • Osanjo, G.1    Dion, M.2    Drone, J.3    Solleux, C.4    Tran, V.5    Rabiller, C.6    Tellier, C.7
  • 53
    • 0034703443 scopus 로고    scopus 로고
    • Enzymatic synthesis of fucose-containing disaccharides employing the partially purified α- L -fucosidase from Penicillium multicolor
    • Farkas, E.; Thiem, J.; Ajisaka, K. Enzymatic synthesis of fucose-containing disaccharides employing the partially purified α- l -fucosidase from Penicillium multicolor Carbohydr. Res. 2000, 328, 293-299
    • (2000) Carbohydr. Res. , vol.328 , pp. 293-299
    • Farkas, E.1    Thiem, J.2    Ajisaka, K.3
  • 54
    • 84877576453 scopus 로고    scopus 로고
    • Highly efficient enzymatic synthesis of Galβ-(1→3)-GalNAc and Galβ-(1→3)-GlcNAc in ionic liquids
    • Bayón, C.; Cortés, á.; Berenguer, J.; Hernáiz, M. J. Highly efficient enzymatic synthesis of Galβ-(1→3)-GalNAc and Galβ-(1→3)-GlcNAc in ionic liquids Tetrahedron 2013, 69, 4973-4978
    • (2013) Tetrahedron , vol.69 , pp. 4973-4978
    • Bayón, C.1    Cortés Á.2    Berenguer, J.3    Hernáiz, M.J.4
  • 55
    • 79952200265 scopus 로고    scopus 로고
    • The effects of organic solvents on the efficiency and regioselectivity of N -acetyl-lactosamine synthesis, using the β-galactosidase from Bacillus circulans in hydro-organic media
    • Bridiau, N.; Issaoui, N.; Maugard, T. The effects of organic solvents on the efficiency and regioselectivity of N -acetyl-lactosamine synthesis, using the β-galactosidase from Bacillus circulans in hydro-organic media Biotechnol. Prog. 2010, 26, 1278-1289
    • (2010) Biotechnol. Prog. , vol.26 , pp. 1278-1289
    • Bridiau, N.1    Issaoui, N.2    Maugard, T.3
  • 56
    • 0036322169 scopus 로고    scopus 로고
    • Use of ionic liquids to increase the yield and enzyme stability in the β-galactosidase catalysed synthesis of N -acetyllactosamine
    • Kaftzik, N.; Wasserscheid, P.; Kragl, U. Use of ionic liquids to increase the yield and enzyme stability in the β-galactosidase catalysed synthesis of N -acetyllactosamine Org. Process Res. Dev. 2002, 6, 553-557
    • (2002) Org. Process Res. Dev. , vol.6 , pp. 553-557
    • Kaftzik, N.1    Wasserscheid, P.2    Kragl, U.3
  • 57
    • 0001378427 scopus 로고
    • Enzymatic syntheses of N -acetyllactosamine and N -acetylallolactosamine by the use of β- D -galactosidases
    • Sakai, K.; Katsumi, R.; Ohi, H.; Usui, T.; Ishido, Y. Enzymatic syntheses of N -acetyllactosamine and N -acetylallolactosamine by the use of β- d -galactosidases J. Carbohydr. Chem. 1992, 11, 553-565
    • (1992) J. Carbohydr. Chem. , vol.11 , pp. 553-565
    • Sakai, K.1    Katsumi, R.2    Ohi, H.3    Usui, T.4    Ishido, Y.5
  • 58
    • 0036105886 scopus 로고    scopus 로고
    • Enzymatic synthesis of hexyl glycosides from lactose at low water activity and high temperature using hyperthermostable β-glycosidases
    • Hansson, T.; Adlercreutz, P. Enzymatic synthesis of hexyl glycosides from lactose at low water activity and high temperature using hyperthermostable β-glycosidases Biocatal. Biotransform. 2002, 20, 167-178
    • (2002) Biocatal. Biotransform. , vol.20 , pp. 167-178
    • Hansson, T.1    Adlercreutz, P.2
  • 59
    • 0034616232 scopus 로고    scopus 로고
    • Regioselective synthesis of p -nitrophenyl glycosides of β- D -galactopyranosyl-disaccharides by transglycosylation with β- D -galactosidases
    • Zeng, X.; Yoshino, R.; Murata, T.; Ajisaka, K.; Usui, T. Regioselective synthesis of p -nitrophenyl glycosides of β- d -galactopyranosyl-disaccharides by transglycosylation with β- d -galactosidases Carbohydr. Res. 2000, 325, 120-131
    • (2000) Carbohydr. Res. , vol.325 , pp. 120-131
    • Zeng, X.1    Yoshino, R.2    Murata, T.3    Ajisaka, K.4    Usui, T.5
  • 60
    • 0034697882 scopus 로고    scopus 로고
    • Synthesis of sialyloligosaccharides using the trans -sialidase from Trypanosoma cruzi: Novel branched and di-sialylated products from digalactoside acceptors
    • Singh, S.; Scigelova, M.; Hallberg, M. L.; Howarth, O. W.; Schenkman, S.; Crout, D. H. G. Synthesis of sialyloligosaccharides using the trans -sialidase from Trypanosoma cruzi: novel branched and di-sialylated products from digalactoside acceptors Chem. Commun. 2000, 1013-1014
    • (2000) Chem. Commun. , pp. 1013-1014
    • Singh, S.1    Scigelova, M.2    Hallberg, M.L.3    Howarth, O.W.4    Schenkman, S.5    Crout, D.H.G.6
  • 61
    • 0036842393 scopus 로고    scopus 로고
    • Production of sialyloligosaccharides by trans -sialidase catalyzed reaction using fetuin as a sialic acid donor
    • Lee, S.-G.; Shin, D.-H.; Kim, B.-G. Production of sialyloligosaccharides by trans -sialidase catalyzed reaction using fetuin as a sialic acid donor Enzyme Microb. Technol. 2002, 31, 742-746
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 742-746
    • Lee, S.-G.1    Shin, D.-H.2    Kim, B.-G.3
  • 62
    • 0027113971 scopus 로고
    • Regioselective synthesis of α- L -fucosyl-containing disaccharides by use of α- L -fucosidases of various origins
    • Ajisaka, K.; Shirakabe, M. Regioselective synthesis of α- l -fucosyl-containing disaccharides by use of α- l -fucosidases of various origins Carbohydr. Res. 1992, 224, 291-299
    • (1992) Carbohydr. Res. , vol.224 , pp. 291-299
    • Ajisaka, K.1    Shirakabe, M.2
  • 63
    • 0031578257 scopus 로고    scopus 로고
    • All-aqueous, regiospecific tranglycosylation synthesis of 3- O -α- l -fucopyranosyl-2-acetamido-2-deoxy- d -glucopyranose, a building block for the synthesis of branched oligosaccharides
    • Vetere, A.; Galateo, C.; Paoletti, S. All-aqueous, regiospecific tranglycosylation synthesis of 3- O -α- l -fucopyranosyl-2-acetamido-2-deoxy- d -glucopyranose, a building block for the synthesis of branched oligosaccharides Biochem. Biophys. Res. Commun. 1997, 234, 358-361
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 358-361
    • Vetere, A.1    Galateo, C.2    Paoletti, S.3
  • 64
    • 0033199969 scopus 로고    scopus 로고
    • β-Galactooligosaccharide synthesis with β-galactosidases from Sulfolobus solfataricus, Aspergillus oryzae, and Escherichia coli
    • Reuter, S.; Nygaard, A. R.; Zimmermann, W. β-Galactooligosaccharide synthesis with β-galactosidases from Sulfolobus solfataricus, Aspergillus oryzae, and Escherichia coli Enzyme Microb. Technol. 1999, 25, 509-516
    • (1999) Enzyme Microb. Technol. , vol.25 , pp. 509-516
    • Reuter, S.1    Nygaard, A.R.2    Zimmermann, W.3
  • 65
    • 77952426860 scopus 로고    scopus 로고
    • Synthesis of oligosaccharides with lactose and N -acetylglucosamine as substrates by using β- D -galactosidase from Bacillus circulans
    • Li, W.; Sun, Y.; Ye, H.; Zeng, X. Synthesis of oligosaccharides with lactose and N -acetylglucosamine as substrates by using β- d -galactosidase from Bacillus circulans Eur. Food Res. Technol. 2010, 231, 55-63
    • (2010) Eur. Food Res. Technol. , vol.231 , pp. 55-63
    • Li, W.1    Sun, Y.2    Ye, H.3    Zeng, X.4
  • 66
    • 84856189253 scopus 로고    scopus 로고
    • Bacillus circulans β-galactosidase catalyses the synthesis of N -acetyl-lactosamine in a hydro-organic medium via a steady-state ordered Bi Bi reaction mechanism
    • Bridiau, N.; Maugard, T. Bacillus circulans β-galactosidase catalyses the synthesis of N -acetyl-lactosamine in a hydro-organic medium via a steady-state ordered Bi Bi reaction mechanism J. Mol. Catal. B: Enzym. 2012, 77, 24-31
    • (2012) J. Mol. Catal. B: Enzym. , vol.77 , pp. 24-31
    • Bridiau, N.1    Maugard, T.2
  • 67
    • 1342324033 scopus 로고    scopus 로고
    • Synthesis of oligosaccharides as potential novel food components and upscaled enzymatic reaction employing the β-galactosidase from bovine testes
    • Schröder, S.; Schmidt, U.; Thiem, J.; Kowalczyk, J.; Kunz, M.; Vogel, M. Synthesis of oligosaccharides as potential novel food components and upscaled enzymatic reaction employing the β-galactosidase from bovine testes Tetrahedron 2004, 60, 2601-2608
    • (2004) Tetrahedron , vol.60 , pp. 2601-2608
    • Schröder, S.1    Schmidt, U.2    Thiem, J.3    Kowalczyk, J.4    Kunz, M.5    Vogel, M.6
  • 68
    • 0031201761 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding a novel β-galactosidase from Bacillus circulans
    • Ito, Y.; Sasaki, T. Cloning and characterization of the gene encoding a novel β-galactosidase from Bacillus circulans Biosci., Biotechnol., Biochem. 1997, 61, 1270-1276
    • (1997) Biosci., Biotechnol., Biochem. , vol.61 , pp. 1270-1276
    • Ito, Y.1    Sasaki, T.2
  • 69
    • 0034684068 scopus 로고    scopus 로고
    • A highly selective synthesis of N -acetyllactosamine catalyzed by immobilised β-galactosidase from Bacillus circulans
    • Hernaiz, M. J.; Crout, D. H. G. A highly selective synthesis of N -acetyllactosamine catalyzed by immobilised β-galactosidase from Bacillus circulans J. Mol. Catal. B: Enzym. 2000, 10, 403-408
    • (2000) J. Mol. Catal. B: Enzym. , vol.10 , pp. 403-408
    • Hernaiz, M.J.1    Crout, D.H.G.2
  • 70
    • 84880939975 scopus 로고    scopus 로고
    • α- l -Fucosidase from Paenibacillus thiaminolyticus: Its hydrolytic and transglycosylation abilities
    • Benešová, E.; Lipovová, P.; Dvořáková, H.; Králová, B. α- l -Fucosidase from Paenibacillus thiaminolyticus: its hydrolytic and transglycosylation abilities Glycobiology 2013, 23, 1052-1065
    • (2013) Glycobiology , vol.23 , pp. 1052-1065
    • Benešová, E.1    Lipovová, P.2    Dvořáková, H.3    Králová, B.4
  • 71
    • 0029896688 scopus 로고    scopus 로고
    • Regioselectivity of β- D -galactosyl-disaccharide formation using the β- D -galactosidase from Bacillus circulans
    • Usui, T.; Morimoto, S.; Hayakawa, Y.; Kawaguchi, M.; Murata, T.; Matahira, Y.; Nishida, Y. Regioselectivity of β- d -galactosyl-disaccharide formation using the β- d -galactosidase from Bacillus circulans Carbohydr. Res. 1996, 285, 29-39
    • (1996) Carbohydr. Res. , vol.285 , pp. 29-39
    • Usui, T.1    Morimoto, S.2    Hayakawa, Y.3    Kawaguchi, M.4    Murata, T.5    Matahira, Y.6    Nishida, Y.7
  • 72
    • 0037010874 scopus 로고    scopus 로고
    • Water activity dependence of lipase catalysis in organic media explains successful transesterification reactions
    • Ma, L.; Persson, M.; Adlercreutz, P. Water activity dependence of lipase catalysis in organic media explains successful transesterification reactions Enzyme Microb. Technol. 2002, 31, 1024-1029
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 1024-1029
    • Ma, L.1    Persson, M.2    Adlercreutz, P.3
  • 73
    • 0032575262 scopus 로고    scopus 로고
    • Activity and mobility of subtilisin in low water organic media: Hydration is more important than solvent dielectric
    • Partridge, J.; Dennison, P. R.; Moore, B. D.; Halling, P. J. Activity and mobility of subtilisin in low water organic media: hydration is more important than solvent dielectric Biochim. Biophys. Acta 1998, 1386, 79-89
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 79-89
    • Partridge, J.1    Dennison, P.R.2    Moore, B.D.3    Halling, P.J.4
  • 75
    • 84881520578 scopus 로고    scopus 로고
    • Highly efficient and regioselective enzymatic synthesis of β-(1→3) galactosides in biosolvents
    • Bayón, C.; Cortés, A.; Aires-Trapote, A.; Civera, C.; Hernáiz, M. J. Highly efficient and regioselective enzymatic synthesis of β-(1→3) galactosides in biosolvents RSC Adv. 2013, 3, 12155-12163
    • (2013) RSC Adv. , vol.3 , pp. 12155-12163
    • Bayón, C.1    Cortés, A.2    Aires-Trapote, A.3    Civera, C.4    Hernáiz, M.J.5
  • 76
    • 84871635550 scopus 로고    scopus 로고
    • Optimised N -acetyl- d -lactosamine synthesis using Thermus thermophilus β-galactosidase in bio-solvents
    • Sandoval, M.; Civera, C.; Berenguer, J.; García-Blanco, F.; Hernáiz, M. J. Optimised N -acetyl- d -lactosamine synthesis using Thermus thermophilus β-galactosidase in bio-solvents Tetrahedron 2013, 69, 1148-1152
    • (2013) Tetrahedron , vol.69 , pp. 1148-1152
    • Sandoval, M.1    Civera, C.2    Berenguer, J.3    García-Blanco, F.4    Hernáiz, M.J.5
  • 78
    • 0346366718 scopus 로고    scopus 로고
    • Enzymatic synthesis of N -acetyllactosamine in aqueous-organic reaction media
    • Franke, J.; Braun, K.; Kuhl, P. Enzymatic synthesis of N -acetyllactosamine in aqueous-organic reaction media Pharmazie 2003, 58, 857-859
    • (2003) Pharmazie , vol.58 , pp. 857-859
    • Franke, J.1    Braun, K.2    Kuhl, P.3
  • 79
    • 0025714081 scopus 로고
    • Purification of α- L -fucosidase by C -glycosylic affinity chromatography, and the enzymic synthesis of α- L -fucosyl disaccharides
    • Svensson, S. C. T.; Thiem, J. Purification of α- l -fucosidase by C -glycosylic affinity chromatography, and the enzymic synthesis of α- l -fucosyl disaccharides Carbohydr. Res. 1990, 200, 391-402
    • (1990) Carbohydr. Res. , vol.200 , pp. 391-402
    • Svensson, S.C.T.1    Thiem, J.2
  • 80
    • 84884707240 scopus 로고    scopus 로고
    • Membrane-based recovery of glucose from enzymatic hydrolysis of ionic liquid pretreated cellulose
    • Abels, C.; Thimm, K.; Wulfhorst, H.; Spiess, A. C.; Wessling, M. Membrane-based recovery of glucose from enzymatic hydrolysis of ionic liquid pretreated cellulose Bioresour. Technol. 2013, 149, 58-64
    • (2013) Bioresour. Technol. , vol.149 , pp. 58-64
    • Abels, C.1    Thimm, K.2    Wulfhorst, H.3    Spiess, A.C.4    Wessling, M.5
  • 81
    • 0000782283 scopus 로고
    • Oligosaccharide production, concentration effects in the enzymatic conversion of lactose to oligosaccharides
    • Roberts, H. R.; Pettinati, J. D. Oligosaccharide production, concentration effects in the enzymatic conversion of lactose to oligosaccharides J. Agric. Food Chem. 1957, 5, 130-134
    • (1957) J. Agric. Food Chem. , vol.5 , pp. 130-134
    • Roberts, H.R.1    Pettinati, J.D.2
  • 82
    • 0026541995 scopus 로고
    • α-Mannosidase-catalysed synthesis of novel manno-, lyxo-, and heteromanno-oligosaccharides: A comparison of kinetically and thermodynamically mediated approaches
    • Rastall, R. A.; Rees, N. H.; Wait, R.; Adlard, M. W.; Bucke, C. α-Mannosidase-catalysed synthesis of novel manno-, lyxo-, and heteromanno-oligosaccharides: a comparison of kinetically and thermodynamically mediated approaches Enzyme Microb. Technol. 1992, 14, 53-57
    • (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
    • 72549083561 scopus 로고    scopus 로고
    • Evaluation of Norrish's equation for correlating the water activity of highly concentrated solutions of sugars, polyols, and polyethylene glycols
    • Baeza, R.; Pérez, A.; Sánchez, V.; Zamora, M. C.; Chirife, J. Evaluation of Norrish's equation for correlating the water activity of highly concentrated solutions of sugars, polyols, and polyethylene glycols Food Bioprocess Technol. 2010, 3, 87-92
    • (2010) Food Bioprocess Technol. , vol.3 , pp. 87-92
    • Baeza, R.1    Pérez, A.2    Sánchez, V.3    Zamora, M.C.4    Chirife, J.5
  • 84
    • 0030780520 scopus 로고    scopus 로고
    • The effects of organic solvents on the synthesis of galactose disaccharides using β-galactosidases
    • Finch, P.; Yoon, J. H. The effects of organic solvents on the synthesis of galactose disaccharides using β-galactosidases Carbohydr. Res. 1997, 303, 339-345
    • (1997) Carbohydr. Res. , vol.303 , pp. 339-345
    • Finch, P.1    Yoon, J.H.2
  • 85
    • 84879739683 scopus 로고    scopus 로고
    • Effects of carbohydrates on the o NPG converting activity of β-galactosidases
    • Warmerdam, A.; Wang, J.; Boom, R. M.; Janssen, A. E. M. Effects of carbohydrates on the o NPG converting activity of β-galactosidases J. Agric. Food Chem. 2013, 61, 6458-6464
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 6458-6464
    • Warmerdam, A.1    Wang, J.2    Boom, R.M.3    Janssen, A.E.M.4
  • 86
    • 0030064138 scopus 로고    scopus 로고
    • High-yield synthesis of N -acetyllactosamine by regioselective transglycosylation
    • Vetere, A.; Paoletti, S. High-yield synthesis of N -acetyllactosamine by regioselective transglycosylation Biochem. Biophys. Res. Commun. 1996, 219, 6-13
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 6-13
    • Vetere, A.1    Paoletti, S.2
  • 87
    • 0034694154 scopus 로고    scopus 로고
    • Enzymatic synthesis of oligosaccharides: Product removal during a kinetically controlled reaction
    • Boon, M. A.; van't Riet, V.; Janssen, A. E. M. Enzymatic synthesis of oligosaccharides: product removal during a kinetically controlled reaction Biotechnol. Bioeng. 2000, 70, 411-420
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 411-420
    • Boon, M.A.1    Van't Riet, V.2    Janssen, A.E.M.3
  • 88
    • 0034845738 scopus 로고    scopus 로고
    • In-situ product removal to enhance the yield of biocatalytic reactions with competing equilibria: α-glucosidase catalysed synthesis of disaccharides
    • Ahmed, F.; Stein, A.; Lye, G. J. In-situ product removal to enhance the yield of biocatalytic reactions with competing equilibria: α-glucosidase catalysed synthesis of disaccharides J. Chem. Technol. Biotechnol. 2001, 76, 971-977
    • (2001) J. Chem. Technol. Biotechnol. , vol.76 , pp. 971-977
    • Ahmed, F.1    Stein, A.2    Lye, G.J.3
  • 90
    • 84865109347 scopus 로고    scopus 로고
    • Batch hydrolysis and rotating disk membrane bioreactor for the production of galacto-oligosaccharides: A comparative study
    • Sen, D.; Sarkar, A.; Das, S.; Chowdhury, R.; Bhattacharjee, C. Batch hydrolysis and rotating disk membrane bioreactor for the production of galacto-oligosaccharides: a comparative study Ind. Eng. Chem. Res. 2012, 51, 10671-10681
    • (2012) Ind. Eng. Chem. Res. , vol.51 , pp. 10671-10681
    • Sen, D.1    Sarkar, A.2    Das, S.3    Chowdhury, R.4    Bhattacharjee, C.5
  • 91
    • 84874486411 scopus 로고    scopus 로고
    • Synthesis and separation of galacto-oligosaccharides using membrane bioreactor
    • Nath, A.; Bhattacharjee, C.; Chowdhury, R. Synthesis and separation of galacto-oligosaccharides using membrane bioreactor Desalination 2013, 316, 31-41
    • (2013) Desalination , vol.316 , pp. 31-41
    • Nath, A.1    Bhattacharjee, C.2    Chowdhury, R.3
  • 92
    • 79959944989 scopus 로고    scopus 로고
    • Feasibility study of enzyme immobilization on polymeric membrane: A case study with enzymatically galacto-oligosaccharides production from lactose
    • Sen, D.; Sarkar, A.; Gosling, A.; Gras, S. L.; Stevens, G. W.; Kentish, S. E.; Bhattacharya, P. K.; Barber, A. R.; Bhattacharjee, C. Feasibility study of enzyme immobilization on polymeric membrane: a case study with enzymatically galacto-oligosaccharides production from lactose J. Membr. Sci. 2011, 378, 471-478
    • (2011) J. Membr. Sci. , vol.378 , pp. 471-478
    • Sen, D.1    Sarkar, A.2    Gosling, A.3    Gras, S.L.4    Stevens, G.W.5    Kentish, S.E.6    Bhattacharya, P.K.7    Barber, A.R.8    Bhattacharjee, C.9
  • 96
    • 73849138550 scopus 로고    scopus 로고
    • Rational design of a GH1 β-glycosidase to prevent self-condensation during the transglycosylation reaction
    • Tran, V.; Hoffmann, L.; Rabiller, C.; Tellier, C.; Dion, M. Rational design of a GH1 β-glycosidase to prevent self-condensation during the transglycosylation reaction Protein Eng., Des. Sel. 2010, 23, 43-49
    • (2010) Protein Eng., Des. Sel. , vol.23 , pp. 43-49
    • Tran, V.1    Hoffmann, L.2    Rabiller, C.3    Tellier, C.4    Dion, M.5
  • 99
    • 77952270262 scopus 로고    scopus 로고
    • Tryptophan as a molecular shovel in the glycosyl transfer activity of Trypanosoma cruzi trans-sialidase
    • Mitchell, F. L.; Miles, S. M.; Neres, J.; Bichenkova, E. V.; Bryce, R. A. Tryptophan as a molecular shovel in the glycosyl transfer activity of Trypanosoma cruzi trans-sialidase Biophys. J. 2010, 98, L38-L40
    • (2010) Biophys. J. , vol.98 , pp. 38-L40
    • Mitchell, F.L.1    Miles, S.M.2    Neres, J.3    Bichenkova, E.V.4    Bryce, R.A.5
  • 100
    • 84961980629 scopus 로고    scopus 로고
    • Free energy study of the catalytic mechanism of Trypanosoma cruzi trans -sialidase. from the Michaelis complex to the covalent intermediate
    • Pierdominici-Sottile, G.; Horenstein, N. A.; Roitberg, A. E. Free energy study of the catalytic mechanism of Trypanosoma cruzi trans -sialidase. From the Michaelis complex to the covalent intermediate Biochemistry 2011, 50, 10150-10158
    • (2011) Biochemistry , vol.50 , pp. 10150-10158
    • Pierdominici-Sottile, G.1    Horenstein, N.A.2    Roitberg, A.E.3
  • 101
    • 84893817892 scopus 로고    scopus 로고
    • Free-energy computations identify the mutations required to confer trans-sialidase activity into Trypanosoma rangeli sialidase
    • Pierdominici-Sottile, G.; Palma, J.; Roitberg, A. E. Free-energy computations identify the mutations required to confer trans-sialidase activity into Trypanosoma rangeli sialidase Proteins: Struct., Funct., Bioinf. 2014, 82, 424-435
    • (2014) Proteins: Struct., Funct., Bioinf. , vol.82 , pp. 424-435
    • Pierdominici-Sottile, G.1    Palma, J.2    Roitberg, A.E.3
  • 102
    • 0032503519 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosidases for oligosaccharide synthesis
    • Mackenzie, L. F.; Wang, Q.; Warren, R. A. J.; Withers, S. G. Glycosynthases: mutant glycosidases for oligosaccharide synthesis J. Am. Chem. Soc. 1998, 120, 5583-5584
    • (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
  • 103
    • 62549106593 scopus 로고    scopus 로고
    • Glycosidases: A key to tailored carbohydrates
    • Bojarová, P.; Křen, V. Glycosidases: a key to tailored carbohydrates Trends Biotechnol. 2009, 27, 199-209
    • (2009) Trends Biotechnol. , vol.27 , pp. 199-209
    • Bojarová, P.1    Křen, V.2
  • 104
    • 42149186349 scopus 로고    scopus 로고
    • Teaching old enzymes new tricks: Engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis
    • Shaikh, F. A.; Withers, S. G. Teaching old enzymes new tricks: engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis Biochem. Cell. Biol. 2008, 86, 169-177
    • (2008) Biochem. Cell. Biol. , vol.86 , pp. 169-177
    • Shaikh, F.A.1    Withers, S.G.2
  • 106
    • 0034631781 scopus 로고    scopus 로고
    • Glycosyl fluorides in enzymatic reactions
    • Williams, S. J.; Withers, S. G. Glycosyl fluorides in enzymatic reactions Carbohydr. Res. 2000, 327, 27-46
    • (2000) Carbohydr. Res. , vol.327 , pp. 27-46
    • Williams, S.J.1    Withers, S.G.2
  • 111
    • 0242318374 scopus 로고    scopus 로고
    • Mutagenesis of the conserved active-site tyrosine changes a retaining sialidase into an inverting sialidase
    • Watson, J. N.; Dookhun, V.; Borgford, T. J.; Bennet, A. J. Mutagenesis of the conserved active-site tyrosine changes a retaining sialidase into an inverting sialidase Biochemistry 2003, 42, 12682-12690
    • (2003) Biochemistry , vol.42 , pp. 12682-12690
    • Watson, J.N.1    Dookhun, V.2    Borgford, T.J.3    Bennet, A.J.4
  • 112
    • 21744453183 scopus 로고    scopus 로고
    • Structure and mechanism of action of an inverting mutant sialidase
    • Newstead, S.; Watson, J. N.; Knoll, T. L.; Bennet, A. J.; Taylor, G. Structure and mechanism of action of an inverting mutant sialidase Biochemistry 2005, 44, 9117-9122
    • (2005) Biochemistry , vol.44 , pp. 9117-9122
    • Newstead, S.1    Watson, J.N.2    Knoll, T.L.3    Bennet, A.J.4    Taylor, G.5
  • 113
    • 33750737735 scopus 로고    scopus 로고
    • The hydrolases and transferase activity of an inverting mutant sialidase using non-natural β-sialoside substrates
    • Watson, J. N.; Indurugalla, D.; Cheng, L. L.; Narine, A. A.; Bennet, A. J. The hydrolases and transferase activity of an inverting mutant sialidase using non-natural β-sialoside substrates Biochemistry 2006, 45, 13264-13275
    • (2006) Biochemistry , vol.45 , pp. 13264-13275
    • Watson, J.N.1    Indurugalla, D.2    Cheng, L.L.3    Narine, A.A.4    Bennet, A.J.5
  • 115
    • 85007880332 scopus 로고
    • A system for sialic acid transfer by colominic acid and a sialidase that preferentially hydrolyzes sialyl α-2,8 linkages
    • Tanaka, H.; Ito, F.; Iwasaki, T. A system for sialic acid transfer by colominic acid and a sialidase that preferentially hydrolyzes sialyl α-2,8 linkages Biosci., Biotechnol., Biochem. 1995, 59, 638-643
    • (1995) Biosci., Biotechnol., Biochem. , vol.59 , pp. 638-643
    • Tanaka, H.1    Ito, F.2    Iwasaki, T.3


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