References
- Dextrans;Industrial Gums De Belder, A.N.;Whistler, R.L.(ed.);BeMiller, J.N.(ed.)
- Carbohydr. Res. v.61 The mechanism of acceptor reactions of Leuconostoc mesenteroides B-512F dextransucrase Robyt, J.F.;Walseth, T.E. https://doi.org/10.1016/S0008-6215(00)84503-6
- Carbohydr. Res. v.121 Relative, quantitative effects of acceptors in the reaction of Leuconostoc mesenteroides B-512F dextransucrase Robyt, J.F.;Eklund, S.H. https://doi.org/10.1016/0008-6215(83)84024-5
- Leucrose, a ketodisaccharide of industrial design;Carbohydrates as Organic Raw Materials Schwengers, D.;Lichtenthaler, F.W.(ed.)
- Biotech. Bioeng. v.22 Immobilization and properties of Leuconostoc mesenteroides dextransucrase Kaboli, H.;Reilly, P.J. https://doi.org/10.1002/bit.260220513
- Biotech. Bioeng. v.23 On the production of dextran by free and immobilized dextransucrase Monsan, P.;Lopez, A. https://doi.org/10.1002/bit.260230908
- Biotech. Bioeng. v.40 Investigation of production of dextran and dextransucrase by Leuconostoc mesenteroides immobilized within porous stainless steel El-Sayed, A.M.M.;Abdul-Wahid, K.;Coughlin, R.W. https://doi.org/10.1002/bit.260400509
- Enzyme Microb. Technol. v.17 Unconventional immobilization of dextransucrase with alginate Reischwitz, A.;Reh, K.D.;Buchholz, K. https://doi.org/10.1016/0141-0229(94)00091-5
- Enzyme Microb. Technol. v.19 Productivity of immobilized dextransucrase for leucrose formation Reh, K.D.;Noll-Borchers, M.;Buchholz, K. https://doi.org/10.1016/S0141-0229(96)80003-E
- J. Appl. Polymer Sci. v.51 Hemoglobin encapsulation in chitosan/calcium alginate beads Huguet, M.L.;Groboillot, A.;Neufeld, R.J.;Poncelet, D.;Dellacherie, E. https://doi.org/10.1002/app.1994.070510810
- Process Biochem. v.31 Calcium-alginate beads coated with polycationic polymers: comparison of chitosan and DEAE-dextran Huguet, M.L.;Neufeld, R.I.;Dellacherie, E. https://doi.org/10.1016/0032-9592(95)00076-3
-
Gene
v.182
Cloning and sequencing of a gene coding for a novel dextransucrase from Leuconostoc mesenteroides NRRL B-1299 synthesizing only
${\alpha}$ (1-6) and${\alpha}$ (1-3) linkages Monchois, B.;Willemot, R.M.;Remaud-Simeon, M.;Croux, C.;Monsan, P. https://doi.org/10.1016/S0378-1119(96)00346-0 - Biosci. Biotech. Biochem. v.53 Aggregated form of dextransucrases from Leuconostoc mesenteroides NRRL B-512F and its constitutive mutant Funane, K.;Yamada, M.;Shiraiwa, M.;Takahara, H.;Yamamoto, N.;Ichishima, E.;Kobayashi, M.
- Enzyme Microb. Technol. v.23 Large-scale preparation of highly purified dextransucrase from a high-producing constitutive mutant of Leuconostoc mesenteroides B-512FMC Kitaoka, M.;Robyt, J.F. https://doi.org/10.1016/S0141-0229(98)00060-X
- Enzyme Microb. Technol. v.16 Production and selection of mutants of Leuconostoc mesenteroides constitutive for glucansucrases Kim, D.;Robyt, J.F. https://doi.org/10.1016/0141-0229(94)90086-8
- Carbohydr. Res. v.266 Mechanism of dextran activation of dextransucrase Robyt, J.F.;Kim, D.;Yu, L. https://doi.org/10.1016/0008-6215(94)00262-E
- Enzyme Microb. Technol. v.16 Properties of Leuconostoc mesenteroides B-512FMC constitutive dextransucrase Kim, D.;Robyt, J.F. https://doi.org/10.1016/0141-0229(94)90134-1
- Carbohydr. Res. v.147 Milligram to gram scale purification and characterization of dextransucrase from Leuconostoc mesenteroides NRRL B-512F Miller, A.W.;Eklund, S.H.;Robyt, J.F. https://doi.org/10.1016/0008-6215(86)85011-X
- Biochem. Biophys. Acta v.614 Characterization of the multiple forms and main component of dextransucrase from Leuconostoc mesenteroides NRRL B-512F Kobayashi, M.;Matsuda, K. https://doi.org/10.1016/0005-2744(80)90166-7
- J. Agric. Food Chem. v.45 Immobilization of thermostable maltogenic amylase from Bacillus stearothermophilus for continuous production of branched oligosaccharides Kang, G.J.;Kim, M.J.;Kim, J.W.;Park, K.H. https://doi.org/10.1021/jf970378p
-
Biomaterials
v.13
Covalent immobilization of
${\alpha}$ -amylase onto PHEMA microspheres: preparation and application to fixed bed reactor Agric, M.Y.;Hasirci, V.;Alaeddinoglu, N.G. https://doi.org/10.1016/0142-9612(92)90131-7 - Polymer v.36 Entrapment of urease in glycol containing polymeric matrices and estimation of effective diffusion coefficients of urea Dermircioglu, H.;Beyenal, H.;Tanyolac, A.;Hasirci, N. https://doi.org/10.1016/0032-3861(95)90989-F
- Adv. Carbo. Chem. Biochem. v.51 Mechanisms in the glucansucrase synthesis of polysaccharides and oligosaccharides from sucrose Robyt, J.F. https://doi.org/10.1016/S0065-2318(08)60193-6
- J. Am. Chem. Soc. v.78 The preparation, properties and structure of the disaccharide leucrose Stodola, F.H.;Sharpe, E.S.;Koepsell, H.J. https://doi.org/10.1021/ja01592a050
- Methods Enzymol. v.136 Dextran synthesis using immobilized Leuconostoc mesenteroides dextransucrase Monsan, P.;Paul, F.;Auriol, D.;Lopez, A. https://doi.org/10.1016/S0076-6879(87)36025-2
- Biotechnol. Lett. v.20 In vitro synthesis of oligosaccharides by acceptor reaction of dextransucrase from Leuconostoc mesenteroides Pereira, A.M.;Costa, F.A.;Rodrigues, M.I.;Maugeri, F. https://doi.org/10.1023/A:1005387632760
- Adv. Biochem. Eng. Biotechnol. v.64 Bioaffinity based immobilization of enzymes Saleemuddin, M. https://doi.org/10.1007/3-540-49811-7_6
- Biotechnology v.11 Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli Schatz, P.J. https://doi.org/10.1038/nbt1093-1138
- Biotechnology v.13 Calmodulin as a versatile tag for antibody fragments Neri, D.;De Lalla, C.;Petrul, H.;Neri, P.;Winter, G. https://doi.org/10.1038/nbt0495-373
- Biotech. Prog. v.20 Solid-phase refolding of cyclodextrin glycosyltransferase adsorbed on cationic-exchange resin Kweon, D.H.;Lee, D.H.;Han, N.S.;Seo, J.H. https://doi.org/10.1021/bp0341895
- Biotechnol. Prog. v.7 Improved adsorption to starch of a beta-galactosidase fusion protein containing the starch-binding domain from Aspergillus glucoamylase Chen, L.J.;Ford, C.;Kusnadi, A.;Nikolov, Z.L. https://doi.org/10.1021/bp00009a004
- Biotechnol. Prog. v.18 Separation of MBP fusion proteins through affinity membranes Cattoli, F.;Sarti, G.C. https://doi.org/10.1021/bp010119r
- Biotechnol. Adv. v.20 Cellulose-binding domains: biotechnological applications Levy, I.;Shoseyov, O. https://doi.org/10.1016/S0734-9750(02)00006-X
- J. Bacteriol. v.186 Conserved repeat motifs and glucan binding by glucansucrases of oral streptococci and Leuconostoc mesenteroides Shah, D.S.;Joucla, G.;Remaud-Simeon, M.;Russell, R.R. https://doi.org/10.1128/JB.186.24.8301-8308.2004