메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages 1324-1338

Carbohydrate synthesis by disaccharide phosphorylases: Reactions, catalytic mechanisms and application in the glycosciences

Author keywords

Application; Enzyme engineering; Glycoside synthesis; Glycosyl transfer; Inverting and retaining mechanism

Indexed keywords

ANOMERIC CONFIGURATION; CARBOHYDRATE METABOLISM; CARBOHYDRATE SYNTHESIS; CATALYTIC MECHANISMS; CELLOBIOSE; CHITOBIOSE; COSMETIC INGREDIENTS; DISACCHARIDE DONOR; DISPLACEMENT MECHANISMS; DONOR AND ACCEPTOR; DONOR SUBSTRATES; ENZYMATIC PRODUCTION; ENZYME ENGINEERING; GLYCOSIDE HYDROLASES; GLYCOSIDE SYNTHESIS; GLYCOSYL; GLYCOSYLTRANSFERASES; INVERTING AND RETAINING MECHANISM; PROTEIN ENGINEERING; REACTION CATALYZED; REACTION COORDINATES; STEREOCHEMICAL CONTROL; SUBSTRATE SPECIFICITY; TREHALOSE PHOSPHORYLASE;

EID: 78650090993     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201000217     Document Type: Review
Times cited : (80)

References (100)
  • 2
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst.
    • Zechel, D. L., Withers, S. G., Glycosidase mechanisms: Anatomy of a finely tuned catalyst. Acc. Chem. Res. 2000, 33, 11-18.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 3
    • 9144219793 scopus 로고    scopus 로고
    • Mechanistic analogies amongst carbohydrate modifying enzymes.
    • Lairson, L. L., Withers, S. G., Mechanistic analogies amongst carbohydrate modifying enzymes. Chem. Commun. 2004, 20, 2243-2248.
    • (2004) Chem. Commun. , vol.20 , pp. 2243-2248
    • Lairson, L.L.1    Withers, S.G.2
  • 4
    • 0019890796 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance studies of the effect of oxygen upon glycolysis in yeast.
    • den Hollander, J. A., Ugurbil, K., Brown, T. R., Shulman, R. G., Phosphorus-31 nuclear magnetic resonance studies of the effect of oxygen upon glycolysis in yeast. Biochemistry 1981, 20, 5871-5880.
    • (1981) Biochemistry , vol.20 , pp. 5871-5880
    • den Hollander, J.A.1    Ugurbil, K.2    Brown, T.R.3    Shulman, R.G.4
  • 6
    • 0031909833 scopus 로고    scopus 로고
    • Intracellular glucose concentration in derepressed yeast cells consuming glucose is high enough to reduce the glucose transport rate by 50%.
    • Teusink, B., Diderich, J. A., Westerhoff, H. V., van Dam, K. et al., Intracellular glucose concentration in derepressed yeast cells consuming glucose is high enough to reduce the glucose transport rate by 50%. J. Bacteriol. 1998, 180, 556-562.
    • (1998) J. Bacteriol. , vol.180 , pp. 556-562
    • Teusink, B.1    Diderich, J.A.2    Westerhoff, H.V.3    van Dam, K.4
  • 7
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics.
    • Cantarel, B. L., Coutinho, P. M., Rancurel, C., Bernard, T. et al., The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics. Nucleic Acids Res. 2009, 37, 233-238.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 233-238
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4
  • 8
    • 65449168413 scopus 로고    scopus 로고
    • The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: A large deformation of a TIM barrel scaffold.
    • Hidaka, M., Nishimoto, M., Kitaoka, M., Wakagi, T. et al., The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: A large deformation of a TIM barrel scaffold. J. Biol. Chem. 2009, 284, 7273-7283.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7273-7283
    • Hidaka, M.1    Nishimoto, M.2    Kitaoka, M.3    Wakagi, T.4
  • 9
    • 45049088085 scopus 로고    scopus 로고
    • Mechanistic differences among retaining disaccharide phosphorylases: Insights from kinetic analysis of active site mutants of sucrose phosphorylase and α,α-trehalose phosphorylase.
    • Goedl, C., Schwarz, A., Mueller, M., Brecker, L. et al., Mechanistic differences among retaining disaccharide phosphorylases: Insights from kinetic analysis of active site mutants of sucrose phosphorylase and α, α-trehalose phosphorylase. Carbohydr. Res. 2008, 343, 2032-2040.
    • (2008) Carbohydr. Res. , vol.343 , pp. 2032-2040
    • Goedl, C.1    Schwarz, A.2    Mueller, M.3    Brecker, L.4
  • 10
    • 0025373122 scopus 로고
    • Substrate-induced activation of maltose phosphorylase: Interaction with the anomeric hydroxyl group of α-maltose and α-D-glucose controls the enzyme's glycosyltransferase activity.
    • Tsumuraya, Y., Brewer, C. F., Hehre, E. J., Substrate-induced activation of maltose phosphorylase: Interaction with the anomeric hydroxyl group of α-maltose and α-D-glucose controls the enzyme's glycosyltransferase activity. Arch. Biochem. Biophys. 1990, 281, 58-65.
    • (1990) Arch. Biochem. Biophys. , vol.281 , pp. 58-65
    • Tsumuraya, Y.1    Brewer, C.F.2    Hehre, E.J.3
  • 11
    • 0034329594 scopus 로고    scopus 로고
    • Role of non-covalent enzyme-substrate interactions in the reaction catalyzed by cellobiose phosphorylase from Cellulomonas uda.
    • Nidetzky, B., Eis, C., Albert, M., Role of non-covalent enzyme-substrate interactions in the reaction catalyzed by cellobiose phosphorylase from Cellulomonas uda. Biochem. J. 2000, 351, 649-659.
    • (2000) Biochem. J. , vol.351 , pp. 649-659
    • Nidetzky, B.1    Eis, C.2    Albert, M.3
  • 12
    • 0034885657 scopus 로고    scopus 로고
    • Crystal structure of maltose phosphorylase from Lactobacillus brevis: Unexpected evolutionary relationship with glucoamylases.
    • Egloff, M. P., Uppenberg, J., Haalck, L., van Tilbeurgh, H., Crystal structure of maltose phosphorylase from Lactobacillus brevis: Unexpected evolutionary relationship with glucoamylases. Structure 2001, 9, 689-697.
    • (2001) Structure , vol.9 , pp. 689-697
    • Egloff, M.P.1    Uppenberg, J.2    Haalck, L.3    van Tilbeurgh, H.4
  • 13
    • 33747201719 scopus 로고    scopus 로고
    • Structural dissection of the reaction mechanism of cellobiose phosphorylase.
    • Hidaka, M., Kitaoka, M., Hayashi, K., Wakagi, T. et al., Structural dissection of the reaction mechanism of cellobiose phosphorylase. Biochem. J. 2006, 398, 37-43.
    • (2006) Biochem. J. , vol.398 , pp. 37-43
    • Hidaka, M.1    Kitaoka, M.2    Hayashi, K.3    Wakagi, T.4
  • 14
    • 0015522378 scopus 로고
    • Mechanism of action of sucrose phosphorylase. 3. The reaction with water and other alcohols.
    • Mieyal, J. J., Simon, M., Abeles, R. H., Mechanism of action of sucrose phosphorylase. 3. The reaction with water and other alcohols. J. Biol. Chem. 1972, 247, 532-542.
    • (1972) J. Biol. Chem. , vol.247 , pp. 532-542
    • Mieyal, J.J.1    Simon, M.2    Abeles, R.H.3
  • 15
    • 33746882419 scopus 로고    scopus 로고
    • Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases.
    • Goedl, C., Griessler, R., Schwarz, A., Nidetzky, B., Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases. Biochem. J. 2006, 397, 491-500.
    • (2006) Biochem. J. , vol.397 , pp. 491-500
    • Goedl, C.1    Griessler, R.2    Schwarz, A.3    Nidetzky, B.4
  • 16
    • 34748824093 scopus 로고    scopus 로고
    • Probing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334→Gly mutant enzymes.
    • Schwarz, A., Brecker, L., Nidetzky, B., Probing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334→Gly mutant enzymes. FEBS J. 2007, 274, 5105-5115.
    • (2007) FEBS J. , vol.274 , pp. 5105-5115
    • Schwarz, A.1    Brecker, L.2    Nidetzky, B.3
  • 17
    • 16644388860 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of cellobiose phosphorylase from Cellvibrio gilvus.
    • Hidaka, M., Kitaoka, M., Hayashi, K., Wakagi, T. et al., Crystallization and preliminary X-ray analysis of cellobiose phosphorylase from Cellvibrio gilvus. Acta Crystallogr. D 2004, 60, 1877-1878.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1877-1878
    • Hidaka, M.1    Kitaoka, M.2    Hayashi, K.3    Wakagi, T.4
  • 19
    • 0037436378 scopus 로고    scopus 로고
    • Crystal structure and evolution of a prokaryotic glucoamylase.
    • Aleshin, A. E., Feng, P. H., Honzatko, R. B., Reilly, P. J., Crystal structure and evolution of a prokaryotic glucoamylase. J. Mol. Biol. 2003, 327, 61-73.
    • (2003) J. Mol. Biol. , vol.327 , pp. 61-73
    • Aleshin, A.E.1    Feng, P.H.2    Honzatko, R.B.3    Reilly, P.J.4
  • 20
    • 77749242842 scopus 로고    scopus 로고
    • Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda.
    • Van Hoorebeke, A., Stout, J., Kyndt, J., De Groeve, M. et al., Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda. Acta Crystallogr. F 2010, 66, 346-351.
    • (2010) Acta Crystallogr. F , vol.66 , pp. 346-351
    • Van Hoorebeke, A.1    Stout, J.2    Kyndt, J.3    De Groeve, M.4
  • 21
    • 33745358234 scopus 로고    scopus 로고
    • Asp-196→Ala mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate.
    • Schwarz, A., Nidetzky, B., Asp-196→Ala mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate. FEBS Lett. 2006, 580, 3905-3910.
    • (2006) FEBS Lett. , vol.580 , pp. 3905-3910
    • Schwarz, A.1    Nidetzky, B.2
  • 22
    • 77956925456 scopus 로고    scopus 로고
    • Mieyal, J. J., Abeles, R. H., Disaccharides Phosphorylases, in: Boyer, P. D. (Ed.), The Enzymes, Academic Press, New York 1972 515-532.
    • Mieyal, J. J., Abeles, R. H., Disaccharides Phosphorylases, in: Boyer, P. D. (Ed.), The Enzymes, Academic Press, New York 1972, pp. 515-532.
  • 24
    • 70350538953 scopus 로고    scopus 로고
    • Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate.
    • Goedl, C., Nidetzky, B., Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate. ChemBioChem 2009, 10, 2333-2337.
    • (2009) ChemBioChem , vol.10 , pp. 2333-2337
    • Goedl, C.1    Nidetzky, B.2
  • 25
    • 77950839840 scopus 로고    scopus 로고
    • Crystallization and X-ray diffraction studies of inverting trehalose phosphorylase from Thermoanaerobacter sp.
    • Van Hoorebeke, A., Stout, J., Van der Meeren, R., Kyndt, J. et al., Crystallization and X-ray diffraction studies of inverting trehalose phosphorylase from Thermoanaerobacter sp. Acta Crystallogr. F 2010, 66, 442-447.
    • (2010) Acta Crystallogr. F , vol.66 , pp. 442-447
    • Van Hoorebeke, A.1    Stout, J.2    Van der Meeren, R.3    Kyndt, J.4
  • 26
    • 47049105152 scopus 로고    scopus 로고
    • Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: Substrate-assisted catalysis.
    • Vetting, M. W., Frantom, P. A., Blanchard, J. S., Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: Substrate-assisted catalysis. J. Biol. Chem. 2008, 283, 15834-15844.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15834-15844
    • Vetting, M.W.1    Frantom, P.A.2    Blanchard, J.S.3
  • 27
    • 33750974777 scopus 로고    scopus 로고
    • Insights into the synthesis of lipopolysaccharides and antibiotics through structures of two retaining glycosyltransferases from family GT-4.
    • Martinez-Fleites, C., Proctor, M., Roberts, S., Bolam, D. N. et al., Insights into the synthesis of lipopolysaccharides and antibiotics through structures of two retaining glycosyltransferases from family GT-4. Chem. Biol. 2006, 13, 1143-1152.
    • (2006) Chem. Biol. , vol.13 , pp. 1143-1152
    • Martinez-Fleites, C.1    Proctor, M.2    Roberts, S.3    Bolam, D.N.4
  • 28
    • 34547127671 scopus 로고    scopus 로고
    • Molecular recognition and interfacial catalysis by the essential phosphatidylinositol mannosyltransferase PimA from mycobacteria.
    • Guerin, M. E., Kordulakova, J., Schaeffer, F., Svetlikova, Z. et al., Molecular recognition and interfacial catalysis by the essential phosphatidylinositol mannosyltransferase PimA from mycobacteria. J. Biol. Chem. 2007, 282, 20705-20714.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20705-20714
    • Guerin, M.E.1    Kordulakova, J.2    Schaeffer, F.3    Svetlikova, Z.4
  • 29
    • 48549086905 scopus 로고    scopus 로고
    • The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode.
    • Chua, T. K., Bujnicki, J. M., Tan, T. C., Huynh, F. et al., The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode. Plant Cell 2008, 20, 1059-1072.
    • (2008) Plant Cell , vol.20 , pp. 1059-1072
    • Chua, T.K.1    Bujnicki, J.M.2    Tan, T.C.3    Huynh, F.4
  • 30
    • 77349090654 scopus 로고    scopus 로고
    • Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus.
    • Steiner, K., Hagelueken, G., Messner, P., Schaffer, C. et al., Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus. J. Mol. Biol. 2010, 397, 436-447.
    • (2010) J. Mol. Biol. , vol.397 , pp. 436-447
    • Steiner, K.1    Hagelueken, G.2    Messner, P.3    Schaffer, C.4
  • 31
    • 57349141414 scopus 로고    scopus 로고
    • Crystal structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558.
    • Ruane, K. M., Davies, G. J., Martinez-Fleites, C., Crystal structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. Proteins 2008, 73, 784-787.
    • (2008) Proteins , vol.73 , pp. 784-787
    • Ruane, K.M.1    Davies, G.J.2    Martinez-Fleites, C.3
  • 32
    • 38949126913 scopus 로고    scopus 로고
    • The phosphate site of trehalose phosphorylase from Schizophyllum commune probed by site-directed mutagenesis and chemical rescue studies.
    • Goedl, C., Nidetzky, B., The phosphate site of trehalose phosphorylase from Schizophyllum commune probed by site-directed mutagenesis and chemical rescue studies. FEBS J. 2008, 275, 903-913.
    • (2008) FEBS J. , vol.275 , pp. 903-913
    • Goedl, C.1    Nidetzky, B.2
  • 33
    • 0032437716 scopus 로고    scopus 로고
    • The stereochemical course of the reaction mechanism of trehalose phosphorylase from Schizophyllum commune.
    • Eis, C., Albert, M., Dax, K., Nidetzky, B., The stereochemical course of the reaction mechanism of trehalose phosphorylase from Schizophyllum commune. FEBS Lett. 1998, 440, 440-443.
    • (1998) FEBS Lett. , vol.440 , pp. 440-443
    • Eis, C.1    Albert, M.2    Dax, K.3    Nidetzky, B.4
  • 34
    • 0013638101 scopus 로고    scopus 로고
    • Vandamme, E. J., Van Loo, J., Machtelinckx, L., De Laporte, A., Microbial sucrose phosphorylase: Fermentation process properties, and biotechnical applications, in: Laskin, A. I. (Ed.), Adv. Appl. Microbiol., Academic Press, Orlando 1987 163-201.
    • Vandamme, E. J., Van Loo, J., Machtelinckx, L., De Laporte, A., Microbial sucrose phosphorylase: Fermentation process properties, and biotechnical applications, in: Laskin, A. I. (Ed.), Adv. Appl. Microbiol., Academic Press, Orlando 1987, pp. 163-201.
  • 35
    • 0001263593 scopus 로고
    • Transglucosylation catalyzed by sucrose phosphorylase from Leuconostoc mesenteroides and production of glucosyl-xylitol.
    • Kitao, S., Sekine, H., Transglucosylation catalyzed by sucrose phosphorylase from Leuconostoc mesenteroides and production of glucosyl-xylitol. Biosci. Biotechnol. Biochem. 1992, 56, 2011-2014.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 2011-2014
    • Kitao, S.1    Sekine, H.2
  • 36
    • 4043133300 scopus 로고    scopus 로고
    • Physico-chemical and transglucosylation properties of recombinant sucrose phosphorylase from Bifidobacterium adolescentis DSM20083.
    • van den Broek, L. A. M., van Boxtel, E. L., Kievit, R. P., Verhoef, R. et al., Physico-chemical and transglucosylation properties of recombinant sucrose phosphorylase from Bifidobacterium adolescentis DSM20083. Appl. Microbiol. Biotechnol. 2004, 65, 219-227.
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 219-227
    • van den Broek, L.A.M.1    van Boxtel, E.L.2    Kievit, R.P.3    Verhoef, R.4
  • 37
    • 33947188005 scopus 로고    scopus 로고
    • Recombinant sucrose phosphorylase from Leuconostoc mesenteroides: Characterization, kinetic studies of transglucosylation, and application of immobilized enzyme for production of α-D-glucose 1-phosphate.
    • Goedl, C., Schwarz, A., Minani, A., Nidetzky, B., Recombinant sucrose phosphorylase from Leuconostoc mesenteroides: Characterization, kinetic studies of transglucosylation, and application of immobilized enzyme for production of α-D-glucose 1-phosphate. J. Biotechnol. 2007, 129, 77-86.
    • (2007) J. Biotechnol. , vol.129 , pp. 77-86
    • Goedl, C.1    Schwarz, A.2    Minani, A.3    Nidetzky, B.4
  • 38
    • 78049312647 scopus 로고    scopus 로고
    • Regio- and stereoselective glucosylation of diols by sucrose phosphorylase using sucrose or glucose 1-phosphate as glucosyl donor.
    • Renirie, R., Pukin, A., van Lagen, B., Franssen, M. C., Regio- and stereoselective glucosylation of diols by sucrose phosphorylase using sucrose or glucose 1-phosphate as glucosyl donor. J. Mol. Catal. B Enzym. 2010, 67, 219-224.
    • (2010) J. Mol. Catal. B Enzym. , vol.67 , pp. 219-224
    • Renirie, R.1    Pukin, A.2    van Lagen, B.3    Franssen, M.C.4
  • 39
    • 0033565384 scopus 로고    scopus 로고
    • Characterization of trehalose phosphorylase from Schizophyllum commune.
    • Eis, C., Nidetzky, B., Characterization of trehalose phosphorylase from Schizophyllum commune. Biochem. J. 1999, 341, 385-393.
    • (1999) Biochem. J. , vol.341 , pp. 385-393
    • Eis, C.1    Nidetzky, B.2
  • 40
    • 0025017865 scopus 로고
    • The role of pyridoxal 5'-phosphate in glycogen phosphorylase catalysis.
    • Palm, D., Klein, H. W., Schinzel, R., Buehner, M. et al., The role of pyridoxal 5'-phosphate in glycogen phosphorylase catalysis. Biochemistry 1990, 29, 1099-1107.
    • (1990) Biochemistry , vol.29 , pp. 1099-1107
    • Palm, D.1    Klein, H.W.2    Schinzel, R.3    Buehner, M.4
  • 41
    • 0035875365 scopus 로고    scopus 로고
    • Fungal trehalose phosphorylase: Kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune.
    • Eis, C., Watkins, M., Prohaska, T., Nidetzky, B., Fungal trehalose phosphorylase: Kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune. Biochem. J. 2001, 356, 757-767.
    • (2001) Biochem. J. , vol.356 , pp. 757-767
    • Eis, C.1    Watkins, M.2    Prohaska, T.3    Nidetzky, B.4
  • 42
    • 0029560369 scopus 로고
    • Stability of parenteral nutrition admixtures containing organic phosphates.
    • Ronchera-Oms, C. L., Jimenez, N. V., Peidro, J., Stability of parenteral nutrition admixtures containing organic phosphates. Clin. Nutr. 1995, 14, 373-380.
    • (1995) Clin. Nutr. , vol.14 , pp. 373-380
    • Ronchera-Oms, C.L.1    Jimenez, N.V.2    Peidro, J.3
  • 43
    • 2442502648 scopus 로고    scopus 로고
    • Cellobiose phosphorylase from Cellulomonas uda: Gene cloning and expression in Escherichia coli, and application of the recombinant enzyme in a 'glycosynthase-type' reaction.
    • Nidetzky, B., Griessler, R., Schwarz, A., Splechtna, B., Cellobiose phosphorylase from Cellulomonas uda: Gene cloning and expression in Escherichia coli, and application of the recombinant enzyme in a 'glycosynthase-type' reaction. J. Mol. Catal. B Enzym. 2004, 29, 241-248.
    • (2004) J. Mol. Catal. B Enzym. , vol.29 , pp. 241-248
    • Nidetzky, B.1    Griessler, R.2    Schwarz, A.3    Splechtna, B.4
  • 45
    • 67650620451 scopus 로고    scopus 로고
    • Recent developments in glycoside synthesis with glycosynthases and thioglycoligases.
    • Rakic, B., Withers, S. G., Recent developments in glycoside synthesis with glycosynthases and thioglycoligases. Aust. J. Chem. 2009, 62, 510-520.
    • (2009) Aust. J. Chem. , vol.62 , pp. 510-520
    • Rakic, B.1    Withers, S.G.2
  • 46
    • 78649861857 scopus 로고    scopus 로고
    • Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum. Biochimie 2010, DOI:10.1016/j.biochi.2010.1007.1013.
    • Nakai, H., Hachem, M. A., Petersen, B. O., Westphal, Y., et al., Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum. Biochimie 2010, DOI:10.1016/j.biochi.2010.1007.1013.
    • Nakai, H.1    Hachem, M.A.2    Petersen, B.O.3    Westphal, Y.4
  • 47
    • 0032053291 scopus 로고    scopus 로고
    • Acceptor specificity of cellobiose phosphorylase from Cellvibrio gilvus: Synthesis of three branched trisaccharides.
    • Percy, A., Ono, H., Hayashi, K., Acceptor specificity of cellobiose phosphorylase from Cellvibrio gilvus: Synthesis of three branched trisaccharides. Carbohydr. Res. 1998, 308, 423-429.
    • (1998) Carbohydr. Res. , vol.308 , pp. 423-429
    • Percy, A.1    Ono, H.2    Hayashi, K.3
  • 48
    • 0042201948 scopus 로고    scopus 로고
    • Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8.
    • Rajashekhara, E., Kitaoka, M., Kim, Y. K., Hayashi, K., Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8. Biosci. Biotechnol. Biochem. 2002, 66, 2578-2586.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2578-2586
    • Rajashekhara, E.1    Kitaoka, M.2    Kim, Y.K.3    Hayashi, K.4
  • 49
    • 52649110731 scopus 로고    scopus 로고
    • A new method of synthesis of alkyl α-glycosides using sucrose as sugar donor.
    • Kino, K., Satake, R., Morimatsu, T., Kuratsu, S. et al., A new method of synthesis of alkyl α-glycosides using sucrose as sugar donor. Biosci. Biotechnol. Biochem. 2008, 72, 2415-2417.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 2415-2417
    • Kino, K.1    Satake, R.2    Morimatsu, T.3    Kuratsu, S.4
  • 50
    • 34347338778 scopus 로고    scopus 로고
    • Enzymatic synthesis of α-anomer-selective D-glucosides using maltose phosphorylase.
    • Kino, K., Shimizu, Y., Kuratsu, S., Kirimura, K., Enzymatic synthesis of α-anomer-selective D-glucosides using maltose phosphorylase. Biosci. Biotechnol. Biochem. 2007, 71, 1598-1600.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 1598-1600
    • Kino, K.1    Shimizu, Y.2    Kuratsu, S.3    Kirimura, K.4
  • 51
    • 71949124513 scopus 로고    scopus 로고
    • The maltodextrin transport system and metabolism in Lactobacillus acidophilus NCFM and production of novel α-glucosides through reverse phosphorolysis by maltose phosphorylase.
    • Nakai, H., Baumann, M. J., Petersen, B. O., Westphal, Y. et al., The maltodextrin transport system and metabolism in Lactobacillus acidophilus NCFM and production of novel α-glucosides through reverse phosphorolysis by maltose phosphorylase. FEBS J. 2009, 276, 7353-7365.
    • (2009) FEBS J. , vol.276 , pp. 7353-7365
    • Nakai, H.1    Baumann, M.J.2    Petersen, B.O.3    Westphal, Y.4
  • 52
    • 33746669461 scopus 로고    scopus 로고
    • Acceptor specificity of trehalose phosphorylase from Thermoanaerobacter brockii: Production of novel nonreducing trisaccharide, 6-O-α-D-galactopyranosyl trehalose.
    • Maruta, K., Watanabe, H., Nishimoto, T., Kubota, M. et al., Acceptor specificity of trehalose phosphorylase from Thermoanaerobacter brockii: Production of novel nonreducing trisaccharide, 6-O-α-D-galactopyranosyl trehalose. J. Biosci. Bioeng. 2006, 101, 385-390.
    • (2006) J. Biosci. Bioeng. , vol.101 , pp. 385-390
    • Maruta, K.1    Watanabe, H.2    Nishimoto, T.3    Kubota, M.4
  • 53
    • 0034847621 scopus 로고    scopus 로고
    • Enzymatic synthesis of novel oligosaccharides from L-sorbose, maltose, and sucrose using kojibiose phosphorylase.
    • Chaen, H., Nishimoto, T., Nakada, T., Fukuda, S. et al., Enzymatic synthesis of novel oligosaccharides from L-sorbose, maltose, and sucrose using kojibiose phosphorylase. J. Biosci. Bioeng. 2001, 92, 173-176.
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 173-176
    • Chaen, H.1    Nishimoto, T.2    Nakada, T.3    Fukuda, S.4
  • 54
    • 0031008546 scopus 로고    scopus 로고
    • Further syntheses employing phosphorylase.
    • Evers, B., Thiem, J., Further syntheses employing phosphorylase. Bioorg. Med. Chem. 1997, 5, 857-863.
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 857-863
    • Evers, B.1    Thiem, J.2
  • 55
    • 0020488546 scopus 로고
    • General acid-base catalysis of α-glucan phosphorylase: Stereospecific glucosyl transfer from D-glucal is a pyridoxal 5'-phosphate and orthophosphate (arsenate) dependent reaction.
    • Klein, H. W., Palm, D., Helmreich, E. J., General acid-base catalysis of α-glucan phosphorylase: Stereospecific glucosyl transfer from D-glucal is a pyridoxal 5'-phosphate and orthophosphate (arsenate) dependent reaction. Biochemistry 1982, 21, 6675-6684.
    • (1982) Biochemistry , vol.21 , pp. 6675-6684
    • Klein, H.W.1    Palm, D.2    Helmreich, E.J.3
  • 56
    • 0032437716 scopus 로고    scopus 로고
    • The stereochemical course of the reaction mechanism of trehalose phosphorylase from Schizophyllum commune.
    • Eis, C., Albert, M., Dax, K., Nidetzky, B., The stereochemical course of the reaction mechanism of trehalose phosphorylase from Schizophyllum commune. FEBS Lett. 1998, 440, 440-443.
    • (1998) FEBS Lett. , vol.440 , pp. 440-443
    • Eis, C.1    Albert, M.2    Dax, K.3    Nidetzky, B.4
  • 57
    • 0020595852 scopus 로고
    • α-Glucan phosphorylases catalyze the glucosyl transfer from α-D-glucosyl flouride to oligosaccharides.
    • Palm, D., Blumenauer, G., Klein, H. W., Blanc-Muesser, M., α-Glucan phosphorylases catalyze the glucosyl transfer from α-D-glucosyl flouride to oligosaccharides. Biochem. Biophys. Res. Commun. 1983, 111, 530-536.
    • (1983) Biochem. Biophys. Res. Commun. , vol.111 , pp. 530-536
    • Palm, D.1    Blumenauer, G.2    Klein, H.W.3    Blanc-Muesser, M.4
  • 58
    • 0035893762 scopus 로고    scopus 로고
    • α-Retaining glucosyl transfer catalyzed by trehalose phosphorylase from Schizophyllum commune: Mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors.
    • Nidetzky, B., Eis, C., α-Retaining glucosyl transfer catalyzed by trehalose phosphorylase from Schizophyllum commune: Mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors. Biochem. J. 2001, 360, 727-736.
    • (2001) Biochem. J. , vol.360 , pp. 727-736
    • Nidetzky, B.1    Eis, C.2
  • 59
    • 74549196321 scopus 로고    scopus 로고
    • Sucrose phosphorylase: A powerful transglucosylation catalyst for synthesis of α-D-glucosides as industrial fine chemicals.
    • Goedl, C., Sawangwan, T., Wildberger, P., Nidetzky, B., Sucrose phosphorylase: A powerful transglucosylation catalyst for synthesis of α-D-glucosides as industrial fine chemicals. Biocatal. Biotransform. 2010, 28, 10-21.
    • (2010) Biocatal. Biotransform. , vol.28 , pp. 10-21
    • Goedl, C.1    Sawangwan, T.2    Wildberger, P.3    Nidetzky, B.4
  • 60
    • 57749102704 scopus 로고    scopus 로고
    • A high-yielding biocatalytic process for the production of 2-O-(α-D-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient.
    • Goedl, C., Sawangwan, T., Mueller, M., Schwarz, A. et al., A high-yielding biocatalytic process for the production of 2-O-(α-D-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient. Angew. Chem. Int. Ed. 2008, 47, 10086-10089.
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 10086-10089
    • Goedl, C.1    Sawangwan, T.2    Mueller, M.3    Schwarz, A.4
  • 61
    • 70349808079 scopus 로고    scopus 로고
    • Single-step enzymatic synthesis of (R)-2-O-α-D-glucopyranosyl glycerate, a compatible solute from micro-organisms that functions as a protein stabiliser.
    • Sawangwan, T., Goedl, C., Nidetzky, B., Single-step enzymatic synthesis of (R)-2-O-α-D-glucopyranosyl glycerate, a compatible solute from micro-organisms that functions as a protein stabiliser. Org. Biomol. Chem. 2009, 7, 4267-4270.
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 4267-4270
    • Sawangwan, T.1    Goedl, C.2    Nidetzky, B.3
  • 62
    • 77955664256 scopus 로고    scopus 로고
    • Regioselective O-glucosylation by sucrose phosphorylase: A promising route for functional diversification of a range of 1,2-propanediols.
    • Luley-Goedl, C., Sawangwan, T., Brecker, L., Wildberger, P. et al., Regioselective O-glucosylation by sucrose phosphorylase: A promising route for functional diversification of a range of 1, 2-propanediols. Carbohydr. Res. 2010, 345, 1736-1740.
    • (2010) Carbohydr. Res. , vol.345 , pp. 1736-1740
    • Luley-Goedl, C.1    Sawangwan, T.2    Brecker, L.3    Wildberger, P.4
  • 63
    • 0004689436 scopus 로고
    • The enzymic utilization of sucrose in the synthesis of amylose and derivatives of amylose, using phosphorylases.
    • Waldmann, H., Gygax, D., Bednarski, M. D., Shangraw, W. R. et al., The enzymic utilization of sucrose in the synthesis of amylose and derivatives of amylose, using phosphorylases. Carbohydr. Res. 1986, 157, 4-7.
    • (1986) Carbohydr. Res. , vol.157 , pp. 4-7
    • Waldmann, H.1    Gygax, D.2    Bednarski, M.D.3    Shangraw, W.R.4
  • 64
    • 78650123099 scopus 로고    scopus 로고
    • Biodegradable articles obtained from enzymatically synthesized amylose. WO patent 2002006507
    • Kitamura, S., Shiraishi, N., Yoshioka, M., Kudo, K., et al., Biodegradable articles obtained from enzymatically synthesized amylose. WO patent 2002006507 (2002) pp. 30.
    • (2002) , pp. 30
    • Kitamura, S.1    Shiraishi, N.2    Yoshioka, M.3    Kudo, K.4
  • 65
    • 33947104492 scopus 로고    scopus 로고
    • Trehalose phosphorylase from Pleurotus ostreatus: Characterization and stabilization by covalent modification, and application for the synthesis of α,α-trehalose.
    • Schwarz, A., Goedl, C., Minani, A., Nidetzky, B., Trehalose phosphorylase from Pleurotus ostreatus: Characterization and stabilization by covalent modification, and application for the synthesis of α, α-trehalose. J. Biotechnol. 2007, 129, 140-150.
    • (2007) J. Biotechnol. , vol.129 , pp. 140-150
    • Schwarz, A.1    Goedl, C.2    Minani, A.3    Nidetzky, B.4
  • 67
    • 78650149289 scopus 로고    scopus 로고
    • Taniguchi, H., Sasaki, T., Kitaoka, M., Method for preparing cellobiose. EP patent 423768 (1991)
    • Taniguchi, H., Sasaki, T., Kitaoka, M., Method for preparing cellobiose. EP patent 423768 (1991), p. 9.
  • 68
    • 0034253282 scopus 로고    scopus 로고
    • Enzymatic synthesis of novel disaccharides using disaccharide phosphorylases.
    • Aisaka, K., Masuda-Kato, T., Chikamune, T., Kamitori, K. et al., Enzymatic synthesis of novel disaccharides using disaccharide phosphorylases. J. Biosci. Bioeng. 2000, 90, 208-213.
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 208-213
    • Aisaka, K.1    Masuda-Kato, T.2    Chikamune, T.3    Kamitori, K.4
  • 69
    • 28744444455 scopus 로고    scopus 로고
    • Hyper expression of kojibiose phosphorylase gene and trehalose phosphorylase gene from Thermoanaerobacter brockii ATCC35047 in Bacillus subtilis and selaginose synthesis utilizing two phosphorylases.
    • Yamamoto, T., Mukai, K., Maruta, K., Watanabe, H. et al., Hyper expression of kojibiose phosphorylase gene and trehalose phosphorylase gene from Thermoanaerobacter brockii ATCC35047 in Bacillus subtilis and selaginose synthesis utilizing two phosphorylases. J. Biosci. Bioeng. 2005, 100, 343-346.
    • (2005) J. Biosci. Bioeng. , vol.100 , pp. 343-346
    • Yamamoto, T.1    Mukai, K.2    Maruta, K.3    Watanabe, H.4
  • 70
    • 0002953261 scopus 로고    scopus 로고
    • Production of trehalose from starch by maltose phosphorylase and trehalose phosphorylase from a strain of
    • Yoshida, M., Nakamura, N., Horikoshi, K., Production of trehalose from starch by maltose phosphorylase and trehalose phosphorylase from a strain of Plesiomonas. Starch/Stärke 1997, 49, 21-26.
    • (1997) Plesiomonas. Starch/Stärke , vol.49 , pp. 21-26
    • Yoshida, M.1    Nakamura, N.2    Horikoshi, K.3
  • 72
    • 0001508705 scopus 로고
    • Conversion of sucrose into cellobiose using sucrose phosphorylase, xylose isomerase, and cellobiose phosphorylase.
    • Kitaoka, M., Sasaki, T., Taniguchi, H., Conversion of sucrose into cellobiose using sucrose phosphorylase, xylose isomerase, and cellobiose phosphorylase. Denpun Kagaku 1992, 39, 281-283.
    • (1992) Denpun Kagaku , vol.39 , pp. 281-283
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3
  • 74
    • 33747315816 scopus 로고    scopus 로고
    • α-Glucan phosphorylase and its use in carbohydrate engineering.
    • Yanase, M., Takaha, T., Kuriki, T., α-Glucan phosphorylase and its use in carbohydrate engineering. J. Sci. Food Agric. 2006, 86, 1631-1635.
    • (2006) J. Sci. Food Agric. , vol.86 , pp. 1631-1635
    • Yanase, M.1    Takaha, T.2    Kuriki, T.3
  • 75
    • 71749119169 scopus 로고    scopus 로고
    • Synthesis of cellobiose from starch by the successive actions of two phosphorylases.
    • Suzuki, M., Kaneda, K., Nakai, Y., Kitaoka, M. et al., Synthesis of cellobiose from starch by the successive actions of two phosphorylases. Nat. Biotechnol. 2009, 26, 137-142.
    • (2009) Nat. Biotechnol. , vol.26 , pp. 137-142
    • Suzuki, M.1    Kaneda, K.2    Nakai, Y.3    Kitaoka, M.4
  • 76
    • 0029901440 scopus 로고    scopus 로고
    • Maltodextrin phosphorylase from Escherichia coli: Production and application for the synthesis of α-glucose-1-phosphate.
    • Nidetzky, B., Weinhausel, A., Haltrich, D., Kulbe, K. D. et al., Maltodextrin phosphorylase from Escherichia coli: Production and application for the synthesis of α-glucose-1-phosphate. Ann. N. Y. Acad. Sci. 1996, 782, 208-218.
    • (1996) Ann. N. Y. Acad. Sci. , vol.782 , pp. 208-218
    • Nidetzky, B.1    Weinhausel, A.2    Haltrich, D.3    Kulbe, K.D.4
  • 77
    • 77956689488 scopus 로고    scopus 로고
    • Enzymatic production of α-D-glucose-1-phosphate from trehalose.
    • Van der Borght, J., Desmet, T., Soetaert, W., Enzymatic production of α-D-glucose-1-phosphate from trehalose. Biotechnol. J. 2010, 5, 986-993.
    • (2010) Biotechnol. J. , vol.5 , pp. 986-993
    • Van der Borght, J.1    Desmet, T.2    Soetaert, W.3
  • 78
    • 77953133672 scopus 로고    scopus 로고
    • Efficient one-pot enzymatic synthesis of α-(1α4)-glucosidic disaccharides through a coupled reaction catalyzed by Lactobacillus acidophilus NCFM maltose phosphorylase.
    • Nakai, H., Dilokpimol, A., Hachem, M. A., Svensson, B., Efficient one-pot enzymatic synthesis of α-(1α4)-glucosidic disaccharides through a coupled reaction catalyzed by Lactobacillus acidophilus NCFM maltose phosphorylase. Carbohydr. Res. 2010, 345, 1061-1064.
    • (2010) Carbohydr. Res. , vol.345 , pp. 1061-1064
    • Nakai, H.1    Dilokpimol, A.2    Hachem, M.A.3    Svensson, B.4
  • 79
    • 76149098836 scopus 로고    scopus 로고
    • Distribution of in vitro fermentation ability of lacto-N-biose I, a major building block of human milk oligosaccharides, in bifidobacterial strains.
    • Xiao, J. Z., Takahashi, S., Nishimoto, M., Odamaki, T. et al., Distribution of in vitro fermentation ability of lacto-N-biose I, a major building block of human milk oligosaccharides, in bifidobacterial strains. Appl. Environ. Microbiol. 2010, 76, 54-59.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 54-59
    • Xiao, J.Z.1    Takahashi, S.2    Nishimoto, M.3    Odamaki, T.4
  • 80
    • 35548975958 scopus 로고    scopus 로고
    • Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk.
    • Nishimoto, M., Kitaoka, M., Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk. Biosci. Biotechnol. Biochem. 2007, 71, 2101-2104.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 2101-2104
    • Nishimoto, M.1    Kitaoka, M.2
  • 81
    • 71549147182 scopus 로고    scopus 로고
    • One-pot enzymatic production of α-D-galactopyranosyl-(1α3)-2-acetamido-2-deoxy-D-galactose (galacto-N-biose) from sucrose and 2-acetamido-2-deoxy-D-galactose (N-acetylgalactosamine).
    • Nishimoto, M., Kitaoka, M., One-pot enzymatic production of α-D-galactopyranosyl-(1α3)-2-acetamido-2-deoxy-D-galactose (galacto-N-biose) from sucrose and 2-acetamido-2-deoxy-D-galactose (N-acetylgalactosamine). Carbohydr. Res. 2009, 344, 2573-2576.
    • (2009) Carbohydr. Res. , vol.344 , pp. 2573-2576
    • Nishimoto, M.1    Kitaoka, M.2
  • 82
    • 7444221687 scopus 로고    scopus 로고
    • Stabilization of model membranes during drying by compatible solutes involved in the stress tolerance of plants and microorganisms.
    • Hincha, D. K., Hagemann, M., Stabilization of model membranes during drying by compatible solutes involved in the stress tolerance of plants and microorganisms. Biochem. J. 2004, 383, 277-283.
    • (2004) Biochem. J. , vol.383 , pp. 277-283
    • Hincha, D.K.1    Hagemann, M.2
  • 83
    • 78650132305 scopus 로고    scopus 로고
    • D-Glucopyranosyl glycerol derivatives as antiallergic agents, health foods, and cosmetics. JP patent 2007137862
    • Yoshida, K., Takenaka, A., Nitta, T., Iki, M., α-D-Glucopyranosyl glycerol derivatives as antiallergic agents, health foods, and cosmetics. JP patent 2007137862 (2007) pp. 15.
    • (2007) , pp. 15
    • Yoshida, K.1    Takenaka, A.2    Nitta, T.3    Iki, M.4
  • 84
    • 78650088513 scopus 로고    scopus 로고
    • Cosmetic preparations containing glucosyl glycerides and one or more acrylamidomethyl propylsulphonic acid polymers. WO patent 2006122669
    • Breitenbach, U., Kallmayer, V., Raschke, T., Scherner, C., et al., Cosmetic preparations containing glucosyl glycerides and one or more acrylamidomethyl propylsulphonic acid polymers. WO patent 2006122669 (2006) pp. 25.
    • (2006) , pp. 25
    • Breitenbach, U.1    Kallmayer, V.2    Raschke, T.3    Scherner, C.4
  • 85
    • 78650131826 scopus 로고    scopus 로고
    • Cosmetic preparations with an effective amount of glycosylglycerides as skin moisturizers. EP patent 770378
    • Thiem, J., Scheel, O., Schneider, G., Cosmetic preparations with an effective amount of glycosylglycerides as skin moisturizers. EP patent 770378 (1997) pp. 16.
    • (1997) , pp. 16
    • Thiem, J.1    Scheel, O.2    Schneider, G.3
  • 86
    • 0034280575 scopus 로고    scopus 로고
    • Synthesis of α-D-glucosylglycerol by α-glucosidase and some of its characteristics.
    • Takenaka, F., Uchiyama, H., Synthesis of α-D-glucosylglycerol by α-glucosidase and some of its characteristics. Biosci. Biotechnol. Biochem. 2000, 64, 1821-1826.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1821-1826
    • Takenaka, F.1    Uchiyama, H.2
  • 87
    • 78650150752 scopus 로고    scopus 로고
    • Antitumor agents containing α-D-glucopyranosylglycerols and food and cosmetics containing them. JP patent 2007262023
    • Nitta, T., Takenaka, A., Iki, M., Matsumura, E., et al., Antitumor agents containing α-D-glucopyranosylglycerols and food and cosmetics containing them. JP patent 2007262023 (2007) pp. 13.
    • (2007) , pp. 13
    • Nitta, T.1    Takenaka, A.2    Iki, M.3    Matsumura, E.4
  • 88
    • 0034522550 scopus 로고    scopus 로고
    • Glycoglycerolipid analogues active as anti-tumor-promoters: The influence of the anomeric configuration.
    • Colombo, D., Compostella, F., Ronchetti, F., Scala, A. et al., Glycoglycerolipid analogues active as anti-tumor-promoters: The influence of the anomeric configuration. Eur. J. Med. Chem. 2000, 35, 1109-1113.
    • (2000) Eur. J. Med. Chem. , vol.35 , pp. 1109-1113
    • Colombo, D.1    Compostella, F.2    Ronchetti, F.3    Scala, A.4
  • 89
    • 78650103235 scopus 로고    scopus 로고
    • Goedl, C., Sawangwan, T., Nidetzky, B., Mueller, M., Preparation of 2-O-glyceryl-α-D-glucopyranoside from a glucosyl donor and a glucosyl acceptor. WO patent 2008034158 (2008)
    • Goedl, C., Sawangwan, T., Nidetzky, B., Mueller, M., Preparation of 2-O-glyceryl-α-D-glucopyranoside from a glucosyl donor and a glucosyl acceptor. WO patent 2008034158 (2008) pp. 25.
  • 90
    • 78650121631 scopus 로고    scopus 로고
    • JanDekkerInternational, The spirit of youth, in: Official Show Preview of the In-Cosmetics, Munich, Germany, 2009.
    • JanDekkerInternational, The spirit of youth, in: Official Show Preview of the In-Cosmetics, Munich, Germany, 2009.
  • 91
    • 67651158859 scopus 로고    scopus 로고
    • Creating lactose phosphorylase enzymes by directed evolution of cellobiose phosphorylase.
    • De Groeve, M. R., De Baere, M., Hoflack, L., Desmet, T. et al., Creating lactose phosphorylase enzymes by directed evolution of cellobiose phosphorylase. Protein Eng. Des. Sel. 2009, 22, 393-399.
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 393-399
    • De Groeve, M.R.1    De Baere, M.2    Hoflack, L.3    Desmet, T.4
  • 92
    • 73949098109 scopus 로고    scopus 로고
    • Enzymatic production of α-D-galactose 1-phosphate by lactose phosphorolysis.
    • De Groeve, M. R., Depreitere, V., Desmet, T., Soetaert, W., Enzymatic production of α-D-galactose 1-phosphate by lactose phosphorolysis. Biotechnol. Lett. 2009, 31, 1873-1877.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1873-1877
    • De Groeve, M.R.1    Depreitere, V.2    Desmet, T.3    Soetaert, W.4
  • 93
    • 77951094229 scopus 로고    scopus 로고
    • Development and application of a screening assay for glycoside phosphorylases.
    • De Groeve, M. R., Tran, G. H., Van Hoorebeke, A., Stout, J. et al., Development and application of a screening assay for glycoside phosphorylases. Anal. Biochem. 2010, 401, 162-167.
    • (2010) Anal. Biochem. , vol.401 , pp. 162-167
    • De Groeve, M.R.1    Tran, G.H.2    Van Hoorebeke, A.3    Stout, J.4
  • 94
    • 78650138613 scopus 로고    scopus 로고
    • Construction of cellobiose phosphorylase variants with broadened acceptor specificity towards anomerically substituted glucosides.
    • De Groeve, M. R., Remmery, L., Van Hoorebeke, A., Stout, J. et al., Construction of cellobiose phosphorylase variants with broadened acceptor specificity towards anomerically substituted glucosides. Biotechnol. Bioeng. 2010, 107, 413-420.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 413-420
    • De Groeve, M.R.1    Remmery, L.2    Van Hoorebeke, A.3    Stout, J.4
  • 95
    • 77956570506 scopus 로고    scopus 로고
    • Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase.
    • Nakai, H., Petersen, B. O., Westphal, Y., Dilokpimol, A. et al., Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase. Protein Eng. Des. Sel. 2010, 23, 781-787.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 781-787
    • Nakai, H.1    Petersen, B.O.2    Westphal, Y.3    Dilokpimol, A.4
  • 96
    • 33747265618 scopus 로고    scopus 로고
    • Enhancing the thermal stability of sucrose phosphorylase from Streptococcus mutans by random mutagenesis.
    • Fujii, K., Iiboshi, M., Yanase, M., Takaha, T. et al., Enhancing the thermal stability of sucrose phosphorylase from Streptococcus mutans by random mutagenesis. J. Appl. Glycosci. 2006, 53, 91-97.
    • (2006) J. Appl. Glycosci. , vol.53 , pp. 91-97
    • Fujii, K.1    Iiboshi, M.2    Yanase, M.3    Takaha, T.4
  • 97
    • 77957367702 scopus 로고    scopus 로고
    • Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization.
    • Cerdobbel, A., Desmet, T., De Winter, K., Maertens, J. et al., Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization. J. Biotechnol. 2010, 150, 125-130.
    • (2010) J. Biotechnol. , vol.150 , pp. 125-130
    • Cerdobbel, A.1    Desmet, T.2    De Winter, K.3    Maertens, J.4
  • 98
    • 78349258236 scopus 로고    scopus 로고
    • Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial applications.
    • Cerdobbel, A., De Winter, K., Desmet, T., Soetaert, W., Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial applications. Biotechnol. J. 2010, 5, 1192-1197.
    • (2010) Biotechnol. J. , vol.5 , pp. 1192-1197
    • Cerdobbel, A.1    De Winter, K.2    Desmet, T.3    Soetaert, W.4
  • 99
    • 33750299417 scopus 로고
    • Immobilized sucrose phosphorylase from Leuconostoc mesenteroides.
    • Pimentel, M. C. B., Ferreira, M. S. S., Immobilized sucrose phosphorylase from Leuconostoc mesenteroides. Appl. Biochem. Biotechnol. 1991, 27, 37-43.
    • (1991) Appl. Biochem. Biotechnol. , vol.27 , pp. 37-43
    • Pimentel, M.C.B.1    Ferreira, M.S.S.2
  • 100
    • 78650135325 scopus 로고    scopus 로고
    • Development of protein engineering method to render sucrose phosphorylase thermal stability and use of thermostable enzyme in glucose polymer production. WO patent 2005024008
    • Fujii, K., Iiboshi, M., Yanase, M., Takata, H., et al., Development of protein engineering method to render sucrose phosphorylase thermal stability and use of thermostable enzyme in glucose polymer production. WO patent 2005024008 (2005) p. 120.
    • (2005) , pp. 120
    • Fujii, K.1    Iiboshi, M.2    Yanase, M.3    Takata, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.