메뉴 건너뛰기




Volumn 80, Issue 8, 2005, Pages 845-860

Leuconostoc dextransucrase and dextran: Production, properties and applications

Author keywords

Dextran dextrinase; Dextransucrase; Gluconobacter; Leuconostoc; Oligodextrans

Indexed keywords

BACTERIA; BIOCATALYSTS; BIOPOLYMERS; CATALYSIS; FERMENTATION; POLYSACCHARIDES;

EID: 22744443702     PISSN: 02682575     EISSN: None     Source Type: Journal    
DOI: 10.1002/jctb.1322     Document Type: Review
Times cited : (364)

References (133)
  • 1
    • 33044508973 scopus 로고
    • Investigation on the nature of the gelatinous excretion (so-called frog's spawn) which is observed in production of beet-sugar juices
    • Scheibler C, Investigation on the nature of the gelatinous excretion (so-called frog's spawn) which is observed in production of beet-sugar juices. Z Dtsch Zucker-Ind 24:309-335 (1874).
    • (1874) Z. Dtsch. Zucker-Ind. , vol.24 , pp. 309-335
    • Scheibler, C.1
  • 2
    • 0010375186 scopus 로고
    • On the viscous fermentation and the butyrous fermentation
    • Pasteur L, On the viscous fermentation and the butyrous fermentation. Bull Soc Chim Fr 30-31 (1861).
    • (1861) Bull. Soc. Chim. Fr. , pp. 30-31
    • Pasteur, L.1
  • 5
    • 0003790272 scopus 로고
    • Natural synthesis of low molecular weight (clinical type) dextran by a Streptococcus strain
    • Hehre EJ, Natural synthesis of low molecular weight (clinical type) dextran by a Streptococcus strain. J Biol Chem 222:739-750 (1956).
    • (1956) J. Biol. Chem. , vol.222 , pp. 739-750
    • Hehre, E.J.1
  • 6
    • 0016366368 scopus 로고
    • Purification and properties of dextransucrase from Streptococcus mutans
    • Chludzinski AM, Germaine GR and Schachtele CF, Purification and properties of dextransucrase from Streptococcus mutans. J Bacteriol 118:1-7 (1974).
    • (1974) J. Bacteriol. , vol.118 , pp. 1-7
    • Chludzinski, A.M.1    Germaine, G.R.2    Schachtele, C.F.3
  • 8
    • 0000715899 scopus 로고
    • Dextran
    • ed by Kroschwitz JI. Wiley-VCH, New York
    • Robyt JF, Dextran, in Encyclopaedia of Polymer Science, Vol 4, ed by Kroschwitz JI. Wiley-VCH, New York, pp 753-767 (1985).
    • (1985) Encyclopaedia of Polymer Science , vol.4 , pp. 753-767
    • Robyt, J.F.1
  • 9
    • 0028244773 scopus 로고
    • Purification and some properties of dextransucrase from Streptococcus bovis 148
    • Takagi K, Ioroi R, Uchimura T, Kozaki M and Komagata K, Purification and some properties of dextransucrase from Streptococcus bovis 148. J Ferment Bioeng 77:551-553 (1994).
    • (1994) J. Ferment. Bioeng. , vol.77 , pp. 551-553
    • Takagi, K.1    Ioroi, R.2    Uchimura, T.3    Kozaki, M.4    Komagata, K.5
  • 10
    • 0005404906 scopus 로고
    • Bacterial conversion of dextrin into a polysaccharide with the serological properties of dextran
    • Hehre EJ and Hamilton DM, Bacterial conversion of dextrin into a polysaccharide with the serological properties of dextran. Proc Soc Exp Biol Med 71:336-339 (1949).
    • (1949) Proc. Soc. Exp. Biol. Med. , vol.71 , pp. 336-339
    • Hehre, E.J.1    Hamilton, D.M.2
  • 11
    • 33044492633 scopus 로고
    • Immunopolysaccharides. Part XI. Structure of an Acetobacter capsulatum dextran
    • Barker SA, Bourne EJ, Bruce GT and Stacey M, Immunopolysaccharides. Part XI. Structure of an Acetobacter capsulatum dextran. J ChemSoc 4:4414-4416 (1958).
    • (1958) J. Chem. Soc. , vol.4 , pp. 4414-4416
    • Barker, S.A.1    Bourne, E.J.2    Bruce, G.T.3    Stacey, M.4
  • 12
    • 84984081801 scopus 로고
    • Chemical synthesis of a dextran model, poly-α-(1,6)-anhydro-D-glucopyranose
    • ed by Goodman M. Wiley, Chichester
    • Ruckel ER and Schuerch C, Chemical synthesis of a dextran model, poly-α-(1,6)-anhydro-D-glucopyranose, in Biopolymers, Vol 5, ed by Goodman M. Wiley, Chichester, pp 515-523 (1967).
    • (1967) Biopolymers , vol.5 , pp. 515-523
    • Ruckel, E.R.1    Schuerch, C.2
  • 14
    • 0345680257 scopus 로고
    • Structural studies on dextran from Leuconostoc mesenteroides NRRL B-512
    • Lindberg B and Svensson S, Structural studies on dextran from Leuconostoc mesenteroides NRRL B-512. Acta Chem Scand 22:1907-1912 (1968).
    • (1968) Acta Chem. Scand. , vol.22 , pp. 1907-1912
    • Lindberg, B.1    Svensson, S.2
  • 15
    • 0018402562 scopus 로고
    • Production, purification and properties of dextransucrase from Leuconostoc mesenteroides NRRL B-512F
    • Robyt JF and Walseth TF, Production, purification and properties of dextransucrase from Leuconostoc mesenteroides NRRL B-512F. Carbohydr Res 68:95-111 (1979).
    • (1979) Carbohydr. Res. , vol.68 , pp. 95-111
    • Robyt, J.F.1    Walseth, T.F.2
  • 16
    • 0020981521 scopus 로고
    • Industrial production of dextrans
    • ed by Bushell ME. Elsevier, Amsterdam
    • Alsop RM, Industrial production of dextrans, in Microbial Polysaccharides, ed by Bushell ME. Elsevier, Amsterdam, pp 1-44 (1983).
    • (1983) Microbial Polysaccharides , pp. 1-44
    • Alsop, R.M.1
  • 17
    • 0014144281 scopus 로고
    • Biochemical and morphological aspects of extracellular polysaccharides produced by cariogenic streptococci
    • Guggenheim B and Schroeder HE, Biochemical and morphological aspects of extracellular polysaccharides produced by cariogenic streptococci. Helv Odontol Acta 11:131-152 (1967).
    • (1967) Helv. Odontol. Acta , vol.11 , pp. 131-152
    • Guggenheim, B.1    Schroeder, H.E.2
  • 18
    • 0040288820 scopus 로고    scopus 로고
    • Induction and transcription studies of the dextransucrase gene in Leuconostoc mesenteroides NRRL B-512F
    • Quirasco M, Lopez-Munguia A, Remaud-Simeon M, Monsan P and Farres A. Induction and transcription studies of the dextransucrase gene in Leuconostoc mesenteroides NRRL B-512F. Appl Environ Microbiol 65:5504-5509 (1999).
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5504-5509
    • Quirasco, M.1    Lopez-Munguia, A.2    Remaud-Simeon, M.3    Monsan, P.4    Farres, A.5
  • 19
    • 0028645661 scopus 로고
    • Properties of Leuconostoc mesenteroides B-512FMC constitutive dextransucrase
    • Kim D and Robyt JF, Properties of Leuconostoc mesenteroides B-512FMC constitutive dextransucrase. Enzyme Microb Technol 16:1010-1015 (1994).
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 1010-1015
    • Kim, D.1    Robyt, J.F.2
  • 20
    • 0028302763 scopus 로고
    • Constitutive mutants for dextransucrase from Leuconostoc mesenteroides NRRL B-512F
    • Mizutani N, Yamada M, Takayama K and Shoda M, Constitutive mutants for dextransucrase from Leuconostoc mesenteroides NRRL B-512F. J Ferment Bioeng 77:248-251 (1994).
    • (1994) J. Ferment. Bioeng. , vol.77 , pp. 248-251
    • Mizutani, N.1    Yamada, M.2    Takayama, K.3    Shoda, M.4
  • 21
    • 0032079697 scopus 로고    scopus 로고
    • Use of a microtiter plate screening method for obtaining Leuconostoc mesenteroides mutants constitutive for glucansucrase
    • Kitaoka M and Robyt JF, Use of a microtiter plate screening method for obtaining Leuconostoc mesenteroides mutants constitutive for glucansucrase. Enzyme Microb Technol 22:527-531 (1998).
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 527-531
    • Kitaoka, M.1    Robyt, J.F.2
  • 22
    • 0034021049 scopus 로고    scopus 로고
    • Cloning of a dextransucrase gene (fmcmds) from a constitutive dextransucrase hyper-producing Leuconostoc mesenteroides B-512 FMCM developed using VUV
    • Ryu HJ, Kim D, Kim DW, Moon YY and Robyt JF, Cloning of a dextransucrase gene (fmcmds) from a constitutive dextransucrase hyper-producing Leuconostoc mesenteroides B-512 FMCM developed using VUV. Biotechnol Lett 22:421-425 (2000).
    • (2000) Biotechnol. Lett. , vol.22 , pp. 421-425
    • Ryu, H.J.1    Kim, D.2    Kim, D.W.3    Moon, Y.Y.4    Robyt, J.F.5
  • 23
    • 0021681486 scopus 로고
    • Production and purification of dextransucrase from Leuconostoc mesenteroides NRRL B-512(F)
    • Paul F, Auriol D, Oriol E and Monsan P, Production and purification of dextransucrase from Leuconostoc mesenteroides NRRL B-512(F). Ann N Y Acad Sci 434:267-270 (1984).
    • (1984) Ann. N. Y. Acad. Sci. , vol.434 , pp. 267-270
    • Paul, F.1    Auriol, D.2    Oriol, E.3    Monsan, P.4
  • 24
    • 0022688940 scopus 로고
    • Milligram to gram scale purification and characterization of dextransucrase from Leuconostoc mesenteroides B-512F
    • Miller AW, Eklund SH and Robyt JF, Milligram to gram scale purification and characterization of dextransucrase from Leuconostoc mesenteroides B-512F. Carbohydr Res 147:119-133 (1986).
    • (1986) Carbohydr. Res. , vol.147 , pp. 119-133
    • Miller, A.W.1    Eklund, S.H.2    Robyt, J.F.3
  • 25
    • 0025094378 scopus 로고
    • A facile purification of Leuconostoc mesenteroides B-512FM dextransucrase
    • Fu D and Robyt JF, A facile purification of Leuconostoc mesenteroides B-512FM dextransucrase. Prep Biochem 20:93-106 (1990).
    • (1990) Prep. Biochem. , vol.20 , pp. 93-106
    • Fu, D.1    Robyt, J.F.2
  • 26
    • 0019321336 scopus 로고
    • Characterization of the multiple forms and main component of dextransucrase from Leuconostoc mesenteroides NRRL B-512F
    • Kobayashi M and Matsuda K, Characterization of the multiple forms and main component of dextransucrase from Leuconostoc mesenteroides NRRL B-512F. Biochim Biophys Acta 614:46-62 (1980).
    • (1980) Biochim. Biophys. Acta , vol.614 , pp. 46-62
    • Kobayashi, M.1    Matsuda, K.2
  • 27
    • 0024955235 scopus 로고
    • Effects of dextran on the activity and stability of dextransucrase from Leuconostoc mesenteroides
    • Willemot RM, Monsan P and Durand G, Effects of dextran on the activity and stability of dextransucrase from Leuconostoc mesenteroides. Ann N Y Acad Sci 542:169-172 (1988).
    • (1988) Ann. N. Y. Acad. Sci. , vol.542 , pp. 169-172
    • Willemot, R.M.1    Monsan, P.2    Durand, G.3
  • 28
    • 0028794808 scopus 로고
    • Mechanism of dextran activation of dextransucrase
    • Robyt JF, Kim D and Yu L, Mechanism of dextran activation of dextransucrase. Carbohydr Res 266:293-299 (1995).
    • (1995) Carbohydr. Res. , vol.266 , pp. 293-299
    • Robyt, J.F.1    Kim, D.2    Yu, L.3
  • 29
    • 0001282861 scopus 로고
    • Stereochemistry involved in the mechanism of action of dextransucrase in the synthesis of dextran and the formation of acceptor products
    • Robyt JF and Eklund SH, Stereochemistry involved in the mechanism of action of dextransucrase in the synthesis of dextran and the formation of acceptor products. Bioorg Chem 11:115-132 (1982).
    • (1982) Bioorg. Chem. , vol.11 , pp. 115-132
    • Robyt, J.F.1    Eklund, S.H.2
  • 30
    • 0011127054 scopus 로고    scopus 로고
    • Mechanism and action of glucansucrases
    • ed by Park KH, Robyt JF and Choi YD. Elsevier, Amsterdam
    • Robyt JF, Mechanism and action of glucansucrases, in Enzymes for Carbohydrate Engineering, ed by Park KH, Robyt JF and Choi YD. Elsevier, Amsterdam, pp 1-21 (1996).
    • (1996) Enzymes for Carbohydrate Engineering , pp. 1-21
    • Robyt, J.F.1
  • 31
    • 0016363519 scopus 로고
    • The mechanism of dextransucrase action: Direction of dextran biosynthesis
    • Robyt JF, Kimble BK and Walseth TF, The mechanism of dextransucrase action: direction of dextran biosynthesis. Arch Biochem Biophys 165:634-640 (1974).
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 634-640
    • Robyt, J.F.1    Kimble, B.K.2    Walseth, T.F.3
  • 32
    • 0020729907 scopus 로고
    • Mechanism of synthesis of D-glucans by D-glucosyltransferases from Streptococcus mutans 6715
    • Robyt JF and Martin PJ, Mechanism of synthesis of D-glucans by D-glucosyltransferases from Streptococcus mutans 6715. Carbohydr Res 113:301-315 (1983).
    • (1983) Carbohydr. Res. , vol.113 , pp. 301-315
    • Robyt, J.F.1    Martin, P.J.2
  • 33
    • 0021106321 scopus 로고
    • A D-glucosylated form of dextransucrase: Demonstration of partial reactions
    • Luzio GA, Parnaik VK and Mayer RM, A D-glucosylated form of dextransucrase: Demonstration of partial reactions. Carbohydr Res 121:269-278 (1983).
    • (1983) Carbohydr. Res. , vol.121 , pp. 269-278
    • Luzio, G.A.1    Parnaik, V.K.2    Mayer, R.M.3
  • 34
    • 0014239722 scopus 로고
    • Mechanisms of biopolymer growth: The formation of dextran and levan
    • Ebert KH and Schenk G, Mechanisms of biopolymer growth: the formation of dextran and levan. Adv Enzymol 30:179-219 (1968).
    • (1968) Adv. Enzymol. , vol.30 , pp. 179-219
    • Ebert, K.H.1    Schenk, G.2
  • 35
    • 0017950850 scopus 로고
    • The mechanism of acceptor reactions of Leuconostoc mesenteroides B-512F dextransucrase
    • Robyt JF and Walseth TF, The mechanism of acceptor reactions of Leuconostoc mesenteroides B-512F dextransucrase. Carbohydr Res 61:433-445 (1978).
    • (1978) Carbohydr. Res. , vol.61 , pp. 433-445
    • Robyt, J.F.1    Walseth, T.F.2
  • 36
    • 0021106318 scopus 로고
    • Relative, quantitative effects of acceptors in the reaction of Leuconostoc mesenteroides B-512F dextransucrase
    • Robyt JF and Eklund SH, Relative, quantitative effects of acceptors in the reaction of Leuconostoc mesenteroides B-512F dextransucrase. Carbohydr Res 121:279-286 (1983).
    • (1983) Carbohydr. Res. , vol.121 , pp. 279-286
    • Robyt, J.F.1    Eklund, S.H.2
  • 37
    • 0025612223 scopus 로고
    • Acceptor reactions of maltodextrins with Leuconostoc mesenteroides B-512FM dextransucrase
    • Fu D and Robyt JF, Acceptor reactions of maltodextrins with Leuconostoc mesenteroides B-512FM dextransucrase. Arch Biochem Biophys 283:379-387 (1990).
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 379-387
    • Fu, D.1    Robyt, J.F.2
  • 38
    • 0027130371 scopus 로고
    • Control of the synthesis of dextran and acceptor-reactions by Leuconostoc mesenteroides B-512FM dextransucrase
    • Su D and Robyt JF, Control of the synthesis of dextran and acceptor-reactions by Leuconostoc mesenteroides B-512FM dextransucrase. Carbohydr Res 248:339-348 (1993).
    • (1993) Carbohydr. Res. , vol.248 , pp. 339-348
    • Su, D.1    Robyt, J.F.2
  • 39
    • 0031916883 scopus 로고    scopus 로고
    • In vitro synthesis of oligosaccharides by acceptor reaction of dextransucrase from Leuconostoc mesenteroides
    • Pereira AM, Costa FAA, Rodrigues MI and Maugeri F, In vitro synthesis of oligosaccharides by acceptor reaction of dextransucrase from Leuconostoc mesenteroides. Biotechnol Lett 20:397-401 (1998).
    • (1998) Biotechnol. Lett. , vol.20 , pp. 397-401
    • Pereira, A.M.1    Costa, F.A.A.2    Rodrigues, M.I.3    Maugeri, F.4
  • 40
    • 0008721469 scopus 로고
    • A simplified method for preparing linear isomalto-oligosaccharides
    • Smiley KL, Slodki ME, Boundy JA and Plattner RD, A simplified method for preparing linear isomalto-oligosaccharides. Carbohydr Res 108:279-283 (1982).
    • (1982) Carbohydr. Res. , vol.108 , pp. 279-283
    • Smiley, K.L.1    Slodki, M.E.2    Boundy, J.A.3    Plattner, R.D.4
  • 41
    • 0031395447 scopus 로고    scopus 로고
    • Structural characterization of the maltose acceptor-products synthesised by Leuconostoc mesenteroides NRRL B-1299 dextransucrase
    • Dols M, Remaud-Simeon M, Willemot RM, Vignon MR and Monsan PF, Structural characterization of the maltose acceptor-products synthesised by Leuconostoc mesenteroides NRRL B-1299 dextransucrase. Carbohydr Res 305:549-559 (1997).
    • (1997) Carbohydr. Res. , vol.305 , pp. 549-559
    • Dols, M.1    Remaud-Simeon, M.2    Willemot, R.M.3    Vignon, M.R.4    Monsan, P.F.5
  • 44
    • 0023082931 scopus 로고
    • Transfer reaction of glucosyl residues to maltose and purified oligosaccharides using highly active Leuconostoc mesenteroides NRRL B-512F dextransucrase
    • Oriol E, Paul F, Monsan P, Heyraud A and Rinaudo M, Transfer reaction of glucosyl residues to maltose and purified oligosaccharides using highly active Leuconostoc mesenteroides NRRL B-512F dextransucrase. Anne N Y Acad Sci 501:210-215 (1987).
    • (1987) Anne. N. Y. Acad. Sci. , vol.501 , pp. 210-215
    • Oriol, E.1    Paul, F.2    Monsan, P.3    Heyraud, A.4    Rinaudo, M.5
  • 45
    • 0003816265 scopus 로고
    • Acceptor reaction of a highly purified dextransucrase with maltose and oligosaccharides. Application to the synthesis of controlled-molecular-weight dextrans
    • Paul F, Oriol E, Auriol D and Monsan P, Acceptor reaction of a highly purified dextransucrase with maltose and oligosaccharides. Application to the synthesis of controlled-molecular-weight dextrans. Carbohydr Res 149:433-441 (1986).
    • (1986) Carbohydr. Res. , vol.149 , pp. 433-441
    • Paul, F.1    Oriol, E.2    Auriol, D.3    Monsan, P.4
  • 46
    • 0028518896 scopus 로고
    • A new process for the production of clinical dextran by mixed-culture fermentation of Lipomyces starkeyi and Leuconostoc mesenteroides
    • Kim D and Day DF, A new process for the production of clinical dextran by mixed-culture fermentation of Lipomyces starkeyi and Leuconostoc mesenteroides. Enzyme Microb Technol 16:844-848 (1994).
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 844-848
    • Kim, D.1    Day, D.F.2
  • 47
    • 0017133665 scopus 로고
    • The mechanism of dextransucrase action: Biosynthesis of branch linkages by acceptor reactions with dextran
    • Robyt JF and Taniguchi H, The mechanism of dextransucrase action: biosynthesis of branch linkages by acceptor reactions with dextran. Arch Biochem Biophys 174:129-135 (1976).
    • (1976) Arch. Biochem. Biophys. , vol.174 , pp. 129-135
    • Robyt, J.F.1    Taniguchi, H.2
  • 49
    • 11144320820 scopus 로고    scopus 로고
    • Role of the two catalytic domains of DSR-E dextransucrase and their involvement in the formation of highly alpha-1,2 branched dextran
    • Fabre E, Bozonnet S, Arcache A, Willemot RM, Vignon M, Monsan P and Remaud-Simeon M, Role of the two catalytic domains of DSR-E dextransucrase and their involvement in the formation of highly alpha-1,2 branched dextran. J Bacteriol 187:296-303 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 296-303
    • Fabre, E.1    Bozonnet, S.2    Arcache, A.3    Willemot, R.M.4    Vignon, M.5    Monsan, P.6    Remaud-Simeon, M.7
  • 51
    • 0031454064 scopus 로고    scopus 로고
    • Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutant streptococci
    • Devulapalle KS, Goodman SD, Gao Q, Hemsley A and Mooser G, Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutant streptococci. Protein Sci 6:2489-2493 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 2489-2493
    • Devulapalle, K.S.1    Goodman, S.D.2    Gao, Q.3    Hemsley, A.4    Mooser, G.5
  • 52
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G and Henrissat B, Structures and mechanisms of glycosyl hydrolases. Structure 3:853-859 (1995).
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 53
    • 0028362002 scopus 로고
    • Subsite specificity of the active site of glucosyltransferases from Streptococcus sobrinus
    • Devulapalle KS and Mooser G, Subsite specificity of the active site of glucosyltransferases from Streptococcus sobrinus. J Biol Chem 269:11967-11971 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 11967-11971
    • Devulapalle, K.S.1    Mooser, G.2
  • 54
    • 0021871040 scopus 로고
    • Kinetic studies on dextransucrase from the cariogenic oral bacterium Streptococcus mutans
    • Mooser G, Shur D, Lyou M and Watanabe C, Kinetic studies on dextransucrase from the cariogenic oral bacterium Streptococcus mutans. J Biol Chem 260:6907-6915 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 6907-6915
    • Mooser, G.1    Shur, D.2    Lyou, M.3    Watanabe, C.4
  • 55
    • 0025827032 scopus 로고
    • Isolation and sequence of an active-site peptide containing a catalytic aspartic acid from two Streptococcus sobrinus alpha-glucosyltransferases
    • Mooser G, Hefta SA, Paxton RJ, Shively JE and Lee TD, Isolation and sequence of an active-site peptide containing a catalytic aspartic acid from two Streptococcus sobrinus alpha-glucosyltransferases. J Biol Chem 266:8916-8922 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 8916-8922
    • Mooser, G.1    Hefta, S.A.2    Paxton, R.J.3    Shively, J.E.4    Lee, T.D.5
  • 58
    • 33044502018 scopus 로고    scopus 로고
    • Optimization of culture conditions for the production of dextran by Leuconostoc mesenteroides
    • Yusef HH, El-Aassar SA and Fathy SMF, Optimization of culture conditions for the production of dextran by Leuconostoc mesenteroides. Adv Food Sci 19:152-158 (1997).
    • (1997) Adv. Food Sci. , vol.19 , pp. 152-158
    • Yusef, H.H.1    El-Aassar, S.A.2    Fathy, S.M.F.3
  • 59
    • 0027609433 scopus 로고
    • Interpretation of dextransucrase inhibition at high sucrose concentrations
    • Tanriseven A and Robyt JF, Interpretation of dextransucrase inhibition at high sucrose concentrations. Carbohydr Res 245:97-104 (1993).
    • (1993) Carbohydr. Res. , vol.245 , pp. 97-104
    • Tanriseven, A.1    Robyt, J.F.2
  • 60
    • 0001192314 scopus 로고
    • The genus Leuconostoc
    • ed by Balows A, Trupper HG, Dworkin M, Harder W and Schleifer KH. Springer, New York
    • Holzapfel WH and Schillinger U, The genus Leuconostoc, in The Prokaryotes, Vol. 2, ed by Balows A, Trupper HG, Dworkin M, Harder W and Schleifer KH. Springer, New York, pp 1508-1534 (1992).
    • (1992) The Prokaryotes , vol.2 , pp. 1508-1534
    • Holzapfel, W.H.1    Schillinger, U.2
  • 61
    • 0026911061 scopus 로고
    • Investigation of production of dextran and dextransucrase by Leuconostoc mesenteroides immobilized within porous stainless steel
    • El-Sayed AHMM, Abdul-Wahid K and Coughlin RW, Investigation of production of dextran and dextransucrase by Leuconostoc mesenteroides immobilized within porous stainless steel. Biotechnol Bioeng 40:617-624 (1992).
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 617-624
    • El-Sayed, A.H.M.M.1    Abdul-Wahid, K.2    Coughlin, R.W.3
  • 62
    • 0032805959 scopus 로고    scopus 로고
    • Immobilization of native and dextran-free dextransucrase from Leuconostoc mesenteroides NRRL B-512 F for the synthesis of glucooligosaccharides
    • Alcalde M, Plou FJ, Gomez de Segura A, Remaud-Simeon M, Willemot RM, Monsan P and Ballesteros A, Immobilization of native and dextran-free dextransucrase from Leuconostoc mesenteroides NRRL B-512 F for the synthesis of glucooligosaccharides. Biotechnol Tech 13:749-755 (1999).
    • (1999) Biotechnol. Tech. , vol.13 , pp. 749-755
    • Alcalde, M.1    Plou, F.J.2    Gomez de Segura, A.3    Remaud-Simeon, M.4    Willemot, R.M.5    Monsan, P.6    Ballesteros, A.7
  • 63
    • 0036203512 scopus 로고    scopus 로고
    • Production of isomalto-oligosaccharides using dextransucrase immobilized in alginate fibres
    • Tanriseven A and Dogan S, Production of isomalto-oligosaccharides using dextransucrase immobilized in alginate fibres. Process Biochem 37:1111-1115 (2002).
    • (2002) Process. Biochem. , vol.37 , pp. 1111-1115
    • Tanriseven, A.1    Dogan, S.2
  • 64
    • 0028951034 scopus 로고
    • Enzymatic synthesis of oligosaccharides
    • Monsan P and Paul F, Enzymatic synthesis of oligosaccharides. FEMS Microbiol Rev 16:187-192 (1995).
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 187-192
    • Monsan, P.1    Paul, F.2
  • 66
    • 2142784960 scopus 로고
    • Production and use of glucosyltransferases from Leuconostoc mesenteroides NRRL B-1299 for the synthesis of oligosaccharides containing alpha-(1 → 2) linkages
    • Remaud-Simeon M, Lopez-Munguia A, Pelenc V, Paul F and Monsan P, Production and use of glucosyltransferases from Leuconostoc mesenteroides NRRL B-1299 for the synthesis of oligosaccharides containing alpha-(1 → 2) linkages. Appl Biochem Biotechnol 44:101-117 (1994).
    • (1994) Appl. Biochem. Biotechnol. , vol.44 , pp. 101-117
    • Remaud-Simeon, M.1    Lopez-Munguia, A.2    Pelenc, V.3    Paul, F.4    Monsan, P.5
  • 67
    • 0001651252 scopus 로고
    • Characterization of α-(1 → 3) branched oligosaccharides synthesized by acceptor reaction with the extracellular glucosyltransferases from L. mesenteroides NRRL B-742
    • Remaud M, Paul F and Monsan P, Characterization of α-(1 → 3) branched oligosaccharides synthesized by acceptor reaction with the extracellular glucosyltransferases from L. mesenteroides NRRL B-742. J Carbohydr Chem 11:359-378 (1992).
    • (1992) J. Carbohydr. Chem. , vol.11 , pp. 359-378
    • Remaud, M.1    Paul, F.2    Monsan, P.3
  • 68
    • 0342534180 scopus 로고
    • Preparation and characterization of dextran from Leuconostoc mesenteroides
    • Jeanes A, Wilham CA and Miers JC, Preparation and characterization of dextran from Leuconostoc mesenteroides. J Biol Chem 176:603-615 (1947).
    • (1947) J. Biol. Chem. , vol.176 , pp. 603-615
    • Jeanes, A.1    Wilham, C.A.2    Miers, J.C.3
  • 70
    • 0021753546 scopus 로고
    • An improved procedure for the methylation analysis of oligosaccharides and polysaccharides
    • Harris PJ, Henry RJ, Blakeney AB and Stone BA, An improved procedure for the methylation analysis of oligosaccharides and polysaccharides. Carbohydr Res 127:59-73 (1984).
    • (1984) Carbohydr. Res. , vol.127 , pp. 59-73
    • Harris, P.J.1    Henry, R.J.2    Blakeney, A.B.3    Stone, B.A.4
  • 71
    • 0032741243 scopus 로고    scopus 로고
    • A study of dextran production from maltodextrin by cell suspensions of Gluconobacter oxydans NCIB 4943
    • Mountzouris KC, Gilmour SG, Jay AJ and Rastall RA, A study of dextran production from maltodextrin by cell suspensions of Gluconobacter oxydans NCIB 4943. J Appl Microbiol 87:546-556 (1999).
    • (1999) J. Appl. Microbiol. , vol.87 , pp. 546-556
    • Mountzouris, K.C.1    Gilmour, S.G.2    Jay, A.J.3    Rastall, R.A.4
  • 72
    • 2842533058 scopus 로고
    • Hydrolysis of fourteen native dextrans by Arthrobacter isomaltodextranase and correlation with dextran structure
    • Sawai T, Tohyama T and Natsume T, Hydrolysis of fourteen native dextrans by Arthrobacter isomaltodextranase and correlation with dextran structure. Carbohydr Res 66:195-205 (1978).
    • (1978) Carbohydr. Res. , vol.66 , pp. 195-205
    • Sawai, T.1    Tohyama, T.2    Natsume, T.3
  • 73
    • 0025564743 scopus 로고
    • Dextran structural details from high-field proton NMR spectroscopy
    • Cheetham NWH, Fiala-Beer E and Walker GJ, Dextran structural details from high-field proton NMR spectroscopy. Carbohydre Polym 14:149-158 (1991).
    • (1991) Carbohydre. Polym. , vol.14 , pp. 149-158
    • Cheetham, N.W.H.1    Fiala-Beer, E.2    Walker, G.J.3
  • 74
    • 0035401221 scopus 로고    scopus 로고
    • Characterisation of polysaccharides synthesised by Gluconobacter oxydans NCIMB 4943
    • Sims IM, Thomson A, Hubl U, Larsen NG and Furneaux RH, Characterisation of polysaccharides synthesised by Gluconobacter oxydans NCIMB 4943. Carbohydr Polyms 45:285-292 (2001).
    • (2001) Carbohydr. Polyms. , vol.45 , pp. 285-292
    • Sims, I.M.1    Thomson, A.2    Hubl, U.3    Larsen, N.G.4    Furneaux, R.H.5
  • 75
    • 33044495435 scopus 로고
    • Frequency and distribution of branching in a dextran: An enzymic method
    • Covacevich MT and Richards GN, Frequency and distribution of branching in a dextran: an enzymic method. Carbohydr Res 54:311-315 (1977).
    • (1977) Carbohydr. Res. , vol.54 , pp. 311-315
    • Covacevich, M.T.1    Richards, G.N.2
  • 76
    • 0026203847 scopus 로고
    • High-performance anion-exchange chromatography with pulsed amperometric detection of linear and branched glucose oligosaccharides
    • Ammeraal RN, Delgado GA, Tenbarge FL and Friedman RB, High-performance anion-exchange chromatography with pulsed amperometric detection of linear and branched glucose oligosaccharides. Carbohydr Res 215:179-192 (1991).
    • (1991) Carbohydr. Res. , vol.215 , pp. 179-192
    • Ammeraal, R.N.1    Delgado, G.A.2    Tenbarge, F.L.3    Friedman, R.B.4
  • 77
    • 0015158416 scopus 로고
    • Studies on the length of the side-chains of the dextran elaborated by Leuconostoc mesenteroides NRRL B-512
    • Larm O, Lindberg B and Svensson S, Studies on the length of the side-chains of the dextran elaborated by Leuconostoc mesenteroides NRRL B-512. Carbohydr Res 20:39-48 (1971).
    • (1971) Carbohydr. Res. , vol.20 , pp. 39-48
    • Larm, O.1    Lindberg, B.2    Svensson, S.3
  • 78
    • 0037517455 scopus 로고
    • Application of high-performance liquid chromatography to a study of branching in dextrans
    • Taylor C, Cheetham NWH and Walker GJ, Application of high-performance liquid chromatography to a study of branching in dextrans. Carbohydr Res 137:1-12 (1985).
    • (1985) Carbohydr. Res. , vol.137 , pp. 1-12
    • Taylor, C.1    Cheetham, N.W.H.2    Walker, G.J.3
  • 79
    • 0017842066 scopus 로고
    • Action of a glucoamylase on dextrans as an endodextranase
    • Kobayashi M and Matsuda K, Action of a glucoamylase on dextrans as an endodextranase. Agric Biol Chem 42:181-183 (1978).
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 181-183
    • Kobayashi, M.1    Matsuda, K.2
  • 80
    • 33044497424 scopus 로고
    • An enzymic method for the determination of the degree of polymerisation of glucans
    • Manners DJ, Masson AJ and Sturgeon RJ, An enzymic method for the determination of the degree of polymerisation of glucans. Carbohydr Res 17:109-114 (1971).
    • (1971) Carbohydr. Res. , vol.17 , pp. 109-114
    • Manners, D.J.1    Masson, A.J.2    Sturgeon, R.J.3
  • 81
    • 33044491226 scopus 로고
    • Polymeerchemie
    • Het Spectrum, Utrecht
    • Challa G, Polymeerchemie, in Prisma Technica 52. Het Spectrum, Utrecht, pp 101-118 (1973).
    • (1973) Prisma Technica 52 , pp. 101-118
    • Challa, G.1
  • 82
    • 33044499991 scopus 로고
    • Quality assurance in clinical dextran manufacture by molecular weight characterisation
    • Alsop RM, Byrne GA, Done JN, Earl IE and Gibbs R, Quality assurance in clinical dextran manufacture by molecular weight characterisation. Process Biochem 12:15-35 (1977).
    • (1977) Process. Biochem. , vol.12 , pp. 15-35
    • Alsop, R.M.1    Byrne, G.A.2    Done, J.N.3    Earl, I.E.4    Gibbs, R.5
  • 84
    • 0024110502 scopus 로고
    • Studies on dextran fermentation broth rheology
    • Veljkovic VB and Lazic ML, Studies on dextran fermentation brodi rheology. Enzyme Microb Technol 10:686-688 (1988).
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 686-688
    • Veljkovic, V.B.1    Lazic, M.L.2
  • 85
    • 0025831211 scopus 로고
    • Viscous properties and molecular characterization of enzymatically size-controlled oligodextrans in aqueous solutions
    • Gasciolli V, Choplin L, Paul F and Monsan P, Viscous properties and molecular characterization of enzymatically size-controlled oligodextrans in aqueous solutions. J Biotechnol 19:193-202 (1991).
    • (1991) J. Biotechnol. , vol.19 , pp. 193-202
    • Gasciolli, V.1    Choplin, L.2    Paul, F.3    Monsan, P.4
  • 86
    • 33044485214 scopus 로고
    • Modified method of universal calibration for the determination of molecular weight and molecular-weight distribution
    • Sun SF and Wong E, Modified method of universal calibration for the determination of molecular weight and molecular-weight distribution. J Chromatogr 208:253-259 (1981).
    • (1981) J. Chromatogr. , vol.208 , pp. 253-259
    • Sun, S.F.1    Wong, E.2
  • 88
    • 0031213631 scopus 로고    scopus 로고
    • Production of alternansucrase by Leuconostoc mesenteroides NRRL B-1335 in batch fermentation with controlled pH and dissolved oxygen
    • Raemakers MHM and Vandamme EJ, Production of alternansucrase by Leuconostoc mesenteroides NRRL B-1335 in batch fermentation with controlled pH and dissolved oxygen. J Chem Technol Biotechnol 69:470-478 (1997).
    • (1997) J. Chem. Technol. Biotechnol. , vol.69 , pp. 470-478
    • Raemakers, M.H.M.1    Vandamme, E.J.2
  • 89
    • 0031773666 scopus 로고    scopus 로고
    • A mutant strain of Leuconostoc mesenteroides B-1355 producing a glucosyltransferase synthesizing α(1,2) glucosidic linkages
    • Smith MR, Zahnley JC, Wong RY, Lundin RE and Ahlgren JA. A mutant strain of Leuconostoc mesenteroides B-1355 producing a glucosyltransferase synthesizing α(1,2) glucosidic linkages. J Ind Microbiol Biotechnol 21:37-45 (1998).
    • (1998) J. Ind. Microbiol. Biotechnol. , vol.21 , pp. 37-45
    • Smith, M.R.1    Zahnley, J.C.2    Wong, R.Y.3    Lundin, R.E.4    Ahlgren, J.A.5
  • 90
    • 0032790692 scopus 로고    scopus 로고
    • Some structural features of an insoluble α-D-glucan from a mutant strain of Leuconostoc mesenteroides NRRL B-1355
    • Côté GL, Ahlgren JA and Smith MR, Some structural features of an insoluble α-D-glucan from a mutant strain of Leuconostoc mesenteroides NRRL B-1355. J Ind Microbiol Biotechnol 23:656-660 (1999).
    • (1999) J. Ind. Microbiol. Biotechnol. , vol.23 , pp. 656-660
    • Côté, G.L.1    Ahlgren, J.A.2    Smith, M.R.3
  • 91
    • 0003170414 scopus 로고
    • The biological synthesis of dextran from dextrins
    • Hehre EJ. The biological synthesis of dextran from dextrins. J Biol Chem 192:161-174 (1951).
    • (1951) J. Biol. Chem. , vol.192 , pp. 161-174
    • Hehre, E.J.1
  • 92
    • 0000719880 scopus 로고
    • Structure of dextran synthesised by dextrin dextranase from Acetobacter capsulatus ATCC 11894
    • Yamamoto K, Yoshikawa K and Okada S. Structure of dextran synthesised by dextrin dextranase from Acetobacter capsulatus ATCC 11894. Biosci Biotechnol Biochem 57:1450-1453 (1993).
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1450-1453
    • Yamamoto, K.1    Yoshikawa, K.2    Okada, S.3
  • 93
    • 2542583179 scopus 로고    scopus 로고
    • Functional characteristics of a bacterial dextrin dextranase from Acetobacter capsulatum ATCC 11894
    • Suzuki M, Unno T and Okada G, Functional characteristics of a bacterial dextrin dextranase from Acetobacter capsulatum ATCC 11894. J Appl Glycosci 48:143-151 (2001).
    • (2001) J. Appl. Glycosci. , vol.48 , pp. 143-151
    • Suzuki, M.1    Unno, T.2    Okada, G.3
  • 94
    • 0009501261 scopus 로고    scopus 로고
    • Screening of polysaccharide-producing microorganisms, factors influencing the production and recovery of microbial polysaccharides
    • ed by Dumitriu S. Marcel Dekker, New York
    • Morin A, Screening of polysaccharide-producing microorganisms, factors influencing the production and recovery of microbial polysaccharides, in Polysaccharides. Structural Diversity and Functional Versatility, ed by Dumitriu S. Marcel Dekker, New York, pp 275-296 (1998).
    • (1998) Polysaccharides. Structural Diversity and Functional Versatility , pp. 275-296
    • Morin, A.1
  • 95
    • 22744457407 scopus 로고    scopus 로고
    • Transglucosylation and hydrolysis activitiy of Gluconobacter oxydans dextran dextrinase with several donor and acceptor substrates
    • ed by Chiellini E, Gil H, Braunegg G, Burchert J, Gatenholm P and van der Zee M. Kluwer, Dordrecht
    • Naessens M and Vandamme EJ, Transglucosylation and hydrolysis activitiy of Gluconobacter oxydans dextran dextrinase with several donor and acceptor substrates, in Biorelated Polymers: Sustainable Polymer Science and Technology, ed by Chiellini E, Gil H, Braunegg G, Burchert J, Gatenholm P and van der Zee M. Kluwer, Dordrecht, pp 195-203 (2001).
    • (2001) Biorelated Polymers: Sustainable Polymer Science and Technology , pp. 195-203
    • Naessens, M.1    Vandamme, E.J.2
  • 96
    • 0036985909 scopus 로고    scopus 로고
    • Relationship between intra- and extracellular dextran dextrinase from Gluconobacter oxydans ATCC 11894
    • Naessens M, Vercauteren R and Vandamme EJ, Relationship between intra- and extracellular dextran dextrinase from Gluconobacter oxydans ATCC 11894. Med Fac Landbouw Univ Gent 67:41-44 (2002).
    • (2002) Med. Fac. Landbouw. Univ. Gent. , vol.67 , pp. 41-44
    • Naessens, M.1    Vercauteren, R.2    Vandamme, E.J.3
  • 97
    • 22744434044 scopus 로고    scopus 로고
    • Dextran dextrinase of Gluconobacter oxydans: Production and characterisation
    • PhD Thesis, Faculty of Bioscience Engineering, Ghent University
    • Naessens M, Dextran dextrinase of Gluconobacter oxydans: production and characterisation. PhD Thesis, Faculty of Bioscience Engineering, Ghent University (2003).
    • (2003)
    • Naessens, M.1
  • 98
    • 0042130100 scopus 로고    scopus 로고
    • Multiple forms of microbial enzymes
    • Naessens M and Vandamme EJ, Multiple forms of microbial enzymes. Biotechnol Lett 25:1119-1124 (2003).
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1119-1124
    • Naessens, M.1    Vandamme, E.J.2
  • 99
    • 2542609922 scopus 로고    scopus 로고
    • Three factor response surface optimisation of the production of intracellular dextran dextrinase by Gluconobacter oxydans
    • Naessens M, Vercauteren R and Vandamme EJ, Three factor response surface optimisation of the production of intracellular dextran dextrinase by Gluconobacter oxydans. Process Biochem 39:1299-1304 (2004).
    • (2004) Process. Biochem. , vol.39 , pp. 1299-1304
    • Naessens, M.1    Vercauteren, R.2    Vandamme, E.J.3
  • 101
    • 85052601694 scopus 로고    scopus 로고
    • Medical applications of dextran and its derivatives
    • ed by Dumitriu S. Marcel Dekker, New York
    • De Belder AN, Medical applications of dextran and its derivatives, in Polysaccharides in Medicinal Applications, ed by Dumitriu S. Marcel Dekker, New York, pp 505-523 (1996).
    • (1996) Polysaccharides in Medicinal Applications , pp. 505-523
    • De Belder, A.N.1
  • 102
    • 0020039675 scopus 로고
    • Pathomechanism of dextran-induced anaphylactoid/anaphylactic reactions in man
    • Hedin H and Richter W, Pathomechanism of dextran-induced anaphylactoid/anaphylactic reactions in man. Int Arch Allergy Appl Immunol 68:122 (1982).
    • (1982) Int. Arch. Allergy Appl. Immunol. , vol.68 , pp. 122
    • Hedin, H.1    Richter, W.2
  • 103
    • 33044484600 scopus 로고    scopus 로고
    • Dextran: 50 years - Still going strong
    • Anonymous, March/April
    • Anonymous, Dextran: 50 years - still going strong. Agro-Food-Industry Hi-Tech March/April:10-11 (1997).
    • (1997) Agro-Food-Industry Hi-Tech. , pp. 10-11
  • 105
    • 0031897948 scopus 로고    scopus 로고
    • Intravenous infusion of total dose iron is superior to oral iron in treatment of anemia in peritoneal dialysis patients: A single center comparative study
    • Ahsan N, Intravenous infusion of total dose iron is superior to oral iron in treatment of anemia in peritoneal dialysis patients: a single center comparative study. J Am Soc Nephrol 9:664-668 (1998).
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 664-668
    • Ahsan, N.1
  • 108
    • 0023195892 scopus 로고
    • Anti-HIV synergism between dextran sulfate and zidovudine
    • Ueno R and Kuno S, Anti-HIV synergism between dextran sulfate and zidovudine. Lancet 3:796-797 (1987).
    • (1987) Lancet , vol.3 , pp. 796-797
    • Ueno, R.1    Kuno, S.2
  • 111
    • 33044497857 scopus 로고    scopus 로고
    • Opinion of the Scientific Committee on Food on a Dextran Preparation, Produced Using Leuconostoc mesenteroides, Saccharomyces cerevisiae and Lactobacillus spp, as a Novel Food Ingredient in Bakery Products
    • Food SCO, European Commission, Health and Consumer Protection Directorate-General, Brussels
    • Food SCO, Opinion of the Scientific Committee on Food on a Dextran Preparation, Produced Using Leuconostoc mesenteroides, Saccharomyces cerevisiae and Lactobacillus spp, as a Novel Food Ingredient in Bakery Products. European Commission, Health and Consumer Protection Directorate-General, Brussels (2000).
    • (2000)
  • 114
    • 0025936694 scopus 로고
    • Molecular characterization of a cluster of at least two glucosyltransferase genes in Streptococcus salivarius ATCC 25 975
    • Giffard PM, Simpson CL, Milward CP and Jacques NA, Molecular characterization of a cluster of at least two glucosyltransferase genes in Streptococcus salivarius ATCC 25 975. J Gen Microbiol 137:2577-2593 (1991).
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2577-2593
    • Giffard, P.M.1    Simpson, C.L.2    Milward, C.P.3    Jacques, N.A.4
  • 115
    • 0014593734 scopus 로고
    • Extracellular glucosyltransferase activity of an HS strain of Streptococcus mutans
    • Guggenheim B and Newbrun E, Extracellular glucosyltransferase activity of an HS strain of Streptococcus mutans. Helv Odontol Acta 13:84-97 (1969).
    • (1969) Helv. Odontol. Acta , vol.13 , pp. 84-97
    • Guggenheim, B.1    Newbrun, E.2
  • 116
    • 0015253466 scopus 로고
    • Extracellular polysaccharides synthesized by glucosyltransferases of oral Streptococci
    • Newbrun E, Extracellular polysaccharides synthesized by glucosyltransferases of oral Streptococci. Caries Res 6:132-147 (1972).
    • (1972) Caries Res. , vol.6 , pp. 132-147
    • Newbrun, E.1
  • 117
    • 0018718362 scopus 로고
    • Synthesis and binding of glucosyltransferase and in vitro adherence of Streptococcus mutans grown in a synthetic medium
    • Hamada S and Slade HD, Synthesis and binding of glucosyltransferase and in vitro adherence of Streptococcus mutans grown in a synthetic medium. Arch Oral Biol 24:399-402 (1979).
    • (1979) Arch. Oral Biol. , vol.24 , pp. 399-402
    • Hamada, S.1    Slade, H.D.2
  • 118
    • 0025979819 scopus 로고
    • Presence of an extracellular glycosyltransferase in human dental plaque
    • Ugarte MA and Rodriguez P, Presence of an extracellular glycosyltransferase in human dental plaque. Int J Biochem 23:719-726 (1991).
    • (1991) Int. J. Biochem. , vol.23 , pp. 719-726
    • Ugarte, M.A.1    Rodriguez, P.2
  • 119
    • 0014369437 scopus 로고
    • A possible correlation between specific bacterial enzyme activities, dental plaque formation and cariogenicity
    • Leach SA and Hayes ML, A possible correlation between specific bacterial enzyme activities, dental plaque formation and cariogenicity. Caries Res 2:38-46 (1968).
    • (1968) Caries Res. , vol.2 , pp. 38-46
    • Leach, S.A.1    Hayes, M.L.2
  • 120
    • 0014557741 scopus 로고
    • Improvements in the dextran assay of cane sugar materials
    • Keniry JS, Lee JB and Mahoney VC, Improvements in the dextran assay of cane sugar materials. Int Sugar J 17:230-233 (1969).
    • (1969) Int. Sugar J. , vol.17 , pp. 230-233
    • Keniry, J.S.1    Lee, J.B.2    Mahoney, V.C.3
  • 121
    • 0002757863 scopus 로고
    • A quantitative method for dextran analysis
    • Roberts EJ, A quantitative method for dextran analysis. Int Sugar J 85:10-13 (1983).
    • (1983) Int. Sugar J. , vol.85 , pp. 10-13
    • Roberts, E.J.1
  • 123
    • 0346721076 scopus 로고    scopus 로고
    • Dextran in sugar factories: Causes and control
    • November
    • Clarke MA, Dextran in sugar factories: causes and control. Sugar y Azucar November:22-34 (1997).
    • (1997) Sugar Y Azucar , pp. 22-34
    • Clarke, M.A.1
  • 124
    • 0009932536 scopus 로고
    • Measuring dextran in raw sugars - Historical perspective and state of the art
    • DeStefano RP and Irey MS, Measuring dextran in raw sugars - historical perspective and state of the art. J Am Sugar Cane Technol 6:112-120 (1986).
    • (1986) J. Am. Sugar Cane Technol. , vol.6 , pp. 112-120
    • DeStefano, R.P.1    Irey, M.S.2
  • 125
    • 0009949754 scopus 로고
    • Specific method for quantitative measurement of the total dextran content of raw sugar
    • Brown CF and Inkerman PA, Specific method for quantitative measurement of the total dextran content of raw sugar. J Agric Food Chem 40:227-233 (1992).
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 227-233
    • Brown, C.F.1    Inkerman, P.A.2
  • 126
    • 0001308912 scopus 로고    scopus 로고
    • Leuconostoc
    • ed by Robinson RK, Batt CA and Patel PD. Academic Press, London
    • Lonvaud-Funel A, Leuconostoc, in Encyclopedia of Food Microbiology, Vol 2, ed by Robinson RK, Batt CA and Patel PD. Academic Press, London, pp 1191-1194 (2000).
    • (2000) Encyclopedia of Food Microbiology , vol.2 , pp. 1191-1194
    • Lonvaud-Funel, A.1
  • 127
    • 84978600317 scopus 로고
    • The rapid detection of brewery spoilage micro-organisms
    • Harisson J, Webb TJB and Martin PA, The rapid detection of brewery spoilage micro-organisms. J Inst Brew 80:390-398 (1974).
    • (1974) J. Inst. Brew. , vol.80 , pp. 390-398
    • Harisson, J.1    Webb, T.J.B.2    Martin, P.A.3
  • 128
    • 33044492784 scopus 로고
    • Hygiène en bouteillerie: Sources potentielles d'infection
    • Compagnion D, Hygiène en bouteillerie: sources potentielles d'infection. Cerevisia and Biotechnology 3:59-61 (1991).
    • (1991) Cerevisia and Biotechnology , vol.3 , pp. 59-61
    • Compagnion, D.1
  • 129
    • 9644271489 scopus 로고
    • Beer spoilage organisms: Occurence and detection with particular reference to a new genus Pectinatus
    • PhD Thesis, Faculty of Agriculture and Forestry, University of Helsinki
    • Haikara A, Beer spoilage organisms: occurence and detection with particular reference to a new genus Pectinatus. PhD Thesis, Faculty of Agriculture and Forestry, University of Helsinki (1984).
    • (1984)
    • Haikara, A.1
  • 130
    • 2542539115 scopus 로고
    • A study of microorganisms causing ropiness in beer and wort
    • Baker JL, Day FE and Hulton HFE, A study of microorganisms causing ropiness in beer and wort. J Inst Brew 18:651-672 (1912).
    • (1912) J. Inst. Brew. , vol.18 , pp. 651-672
    • Baker, J.L.1    Day, F.E.2    Hulton, H.F.E.3
  • 131
    • 0005451879 scopus 로고
    • A study of ropiness in beer
    • Shimwell JL, A study of ropiness in beer. J Inst Brew 53:280-294 (1947).
    • (1947) J. Inst. Brew. , vol.53 , pp. 280-294
    • Shimwell, J.L.1
  • 132
    • 33044486989 scopus 로고
    • Filage
    • 2nd edn, ed by De Clerck J. Chaire Jean De Clerck, Louvain-la-Neuve
    • De Clerck J, Filage, in Cours de Brasserie, 2nd edn, Vol. 1, ed by De Clerck J. Chaire Jean De Clerck, Louvain-la-Neuve, pp 871-872 (1984).
    • (1984) Cours De Brasserie , vol.1 , pp. 871-872
    • De Clerck, J.1
  • 133
    • 0002754773 scopus 로고
    • The status of the generic name Gluconobacter
    • De Ley J and Frateur J, The status of the generic name Gluconobacter. Int J Syst Bacteriol 20:83-95 (1970).
    • (1970) Int. J. Syst. Bacteriol. , vol.20 , pp. 83-95
    • De Ley, J.1    Frateur, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.