메뉴 건너뛰기




Volumn 38, Issue 4, 1999, Pages 319-328

Polysaccharases for microbial exopolysaccharides

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGES; DEGRADATION; ENZYME KINETICS; ENZYMES; HYDROLYSIS; MICROBIOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC ACIDS;

EID: 0033115002     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0144-8617(98)00114-3     Document Type: Article
Times cited : (156)

References (111)
  • 1
    • 0345552598 scopus 로고
    • An endo-(1→6)-β-D-glucanase of Flavobacterium M64 hydrolyzing the octasaccharide repeating unit of succinoglycan to two tetrasaccharides
    • Abe M., Amemura A., Harada T. An endo-(1→6)-β-D-glucanase of Flavobacterium M64 hydrolyzing the octasaccharide repeating unit of succinoglycan to two tetrasaccharides. Agric. Biol. Chem. 44:1980;1877-1884.
    • (1980) Agric. Biol. Chem , vol.44 , pp. 1877-1884
    • Abe, M.1    Amemura, A.2    Harada, T.3
  • 2
    • 0027908707 scopus 로고
    • Klebsiella K43 capsular polysaccharide: Primary structure and depolymerisation by a viral borne endoglycanase
    • Aereboe M., Parolis H., Parolis L.A.S. Klebsiella K43 capsular polysaccharide: primary structure and depolymerisation by a viral borne endoglycanase. Carbohydr. Res. 248:1993;213-223.
    • (1993) Carbohydr. Res. , vol.248 , pp. 213-223
    • Aereboe, M.1    Parolis, H.2    Parolis, L.A.S.3
  • 3
    • 0025875477 scopus 로고
    • Purification and characterization of a pyruvated-mannose specific xanthan lyase from heat-stable salt-tolerant bacteria
    • Ahlgren J.A. Purification and characterization of a pyruvated-mannose specific xanthan lyase from heat-stable salt-tolerant bacteria. Appl. Env. Microbiol. 57:1991;2523-2528.
    • (1991) Appl. Env. Microbiol. , vol.57 , pp. 2523-2528
    • Ahlgren, J.A.1
  • 4
    • 0022546209 scopus 로고
    • A bacteriophage associated glycanase cleaving β-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid
    • Altmann F., Kwiatkowski B., Stirm S. A bacteriophage associated glycanase cleaving β-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid. Biochem. Biophys. Res. Commun. 136:1986;329-335.
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , pp. 329-335
    • Altmann, F.1    Kwiatkowski, B.2    Stirm, S.3
  • 5
    • 0023669327 scopus 로고
    • Two additional phage-associated glycan hydrolases cleaving ketosidic bonds of 3-deoxy-D-manno-octulosonic acid in capsular polysaccharides of Escherichia coli
    • Altmann F., Maerz L., Stirm S., Unger F.M. Two additional phage-associated glycan hydrolases cleaving ketosidic bonds of 3-deoxy-D-manno-octulosonic acid in capsular polysaccharides of Escherichia coli. FEBS Lett. 221:1987;145-149.
    • (1987) FEBS Lett. , vol.221 , pp. 145-149
    • Altmann, F.1    Maerz, L.2    Stirm, S.3    Unger, F.M.4
  • 6
    • 0006559422 scopus 로고
    • Enzymic degradation of chemically modified extracellular polysaccharides from Rhizobia
    • Anderson M.A., Stone B.A. Enzymic degradation of chemically modified extracellular polysaccharides from Rhizobia. Carbohydr. Res. 61:1978;479-492.
    • (1978) Carbohydr. Res. , vol.61 , pp. 479-492
    • Anderson, M.A.1    Stone, B.A.2
  • 7
    • 0024677528 scopus 로고
    • Investigation of the structure of the capsular polysaccharide of Escherichia coli K55 using Klebsiella bacteriophage f5. Carbohydr
    • Anderson A.N., Parolis H. Investigation of the structure of the capsular polysaccharide of Escherichia coli K55 using Klebsiella bacteriophage f5. Carbohydr. Polymers. 188:1989;157-168.
    • (1989) Polymers , vol.188 , pp. 157-168
    • Anderson, A.N.1    Parolis, H.2
  • 8
    • 0023655968 scopus 로고
    • Klebsiella serotype K39: Structure of an unusual capsular antigen deduced by use of a viral endoglucosidase
    • Anderson A.N., Parolis H., Dutton G.G.S., Leek D.M. Klebsiella serotype K39: Structure of an unusual capsular antigen deduced by use of a viral endoglucosidase. Carbohydr. Res. 167:1987;279-290.
    • (1987) Carbohydr. Res. , vol.167 , pp. 279-290
    • Anderson, A.N.1    Parolis, H.2    Dutton, G.G.S.3    Leek, D.M.4
  • 9
    • 0024287909 scopus 로고
    • Bacteriophage degradation of the capsular polysaccharide of Klebsiella K24 and determination of the position of the O-acetyl group
    • Annison G., Dutton G.G.S., Mandal P.K. Bacteriophage degradation of the capsular polysaccharide of Klebsiella K24 and determination of the position of the O-acetyl group. Carbohydr. Res. 177:1988;278-284.
    • (1988) Carbohydr. Res. , vol.177 , pp. 278-284
    • Annison, G.1    Dutton, G.G.S.2    Mandal, P.K.3
  • 10
    • 0029816431 scopus 로고    scopus 로고
    • Interactions of phage P22 tails with their cellular receptor Salmonella O-antigen polysaccharide
    • Baxa U., Steinbacher S., Miller S., Weintraub A., Huber R., Seckler R. Interactions of phage P22 tails with their cellular receptor Salmonella O-antigen polysaccharide. Biophys. J. 71:1996;2040-2048.
    • (1996) Biophys. J. , vol.71 , pp. 2040-2048
    • Baxa, U.1    Steinbacher, S.2    Miller, S.3    Weintraub, A.4    Huber, R.5    Seckler, R.6
  • 11
    • 0018358607 scopus 로고
    • Penetration of the polysaccharide capsule of Escherichia coli
    • Bayer M.E., Thurow H., Bayer M.H. Penetration of the polysaccharide capsule of Escherichia coli. Virol. 94:1979;95-118.
    • (1979) Virol. , vol.94 , pp. 95-118
    • Bayer, M.E.1    Thurow, H.2    Bayer, M.H.3
  • 12
    • 0014031138 scopus 로고
    • Lyase activity of inducible S8-depolymerases from Bacillus palustris
    • Becker G.E., Pappenheimer A.M. Lyase activity of inducible S8-depolymerases from Bacillus palustris. Biochim. Biophys. Acta. 121:1966;343-348.
    • (1966) Biochim. Biophys. Acta , vol.121 , pp. 343-348
    • Becker, G.E.1    Pappenheimer, A.M.2
  • 13
    • 0027513371 scopus 로고
    • Isolation and characterization of a Bacillus strain capable of degrading the extracellular glucan from Cellulomonas flavigena strain KU
    • Bertram P.A., Buller C.S., Stewart G.C., Akagi J.M. Isolation and characterization of a Bacillus strain capable of degrading the extracellular glucan from Cellulomonas flavigena strain KU. J. appl. Bact. 74:1993;460-465.
    • (1993) J. Appl. Bact. , vol.74 , pp. 460-465
    • Bertram, P.A.1    Buller, C.S.2    Stewart, G.C.3    Akagi, J.M.4
  • 14
    • 0015858563 scopus 로고
    • A bacteriophage-induced depolymerase active on Klebsiella K11 capsular polysaccharide
    • Bessler W., Freund-Mölbert ., Knüfermann ., Rudolph C., Thurow ., Stirm . A bacteriophage-induced depolymerase active on Klebsiella K11 capsular polysaccharide. Virol. 56:1973;134.
    • (1973) Virol. , vol.56 , pp. 134
    • Bessler, W.1    Freund-Mölbert2    Knüfermann3    Rudolph, C.4    Thurow5    Stirm6
  • 15
    • 0022824238 scopus 로고
    • Depolymerization of the capsular polysaccharide from Klebsiella K19 by the glycanase associated with particles of Klebsiella bacteriophage P19
    • Beurret M., Joseleau J.-P. Depolymerization of the capsular polysaccharide from Klebsiella K19 by the glycanase associated with particles of Klebsiella bacteriophage P19. Carbohydr. Res. 157:1986;27-51.
    • (1986) Carbohydr. Res. , vol.157 , pp. 27-51
    • Beurret, M.1    Joseleau, J.-P.2
  • 16
    • 0028340887 scopus 로고
    • Role of alginate lyase in cell detachment of Pseudomonas aeruginosa
    • Boyd A., Chakrabarty A.M. Role of alginate lyase in cell detachment of Pseudomonas aeruginosa. Appl. Env. Microbiol. 60:1994;2355-2359.
    • (1994) Appl. Env. Microbiol. , vol.60 , pp. 2355-2359
    • Boyd, A.1    Chakrabarty, A.M.2
  • 19
    • 0010541496 scopus 로고
    • Susceptibility of scleroglucan to the (1(3)-(-D-glucanase zymolyase
    • Catley B.J., Fraser M.E. Susceptibility of scleroglucan to the (1(3)-(-D-glucanase zymolyase. Carbohydr. Res. 183:1988;83-88.
    • (1988) Carbohydr. Res. , vol.183 , pp. 83-88
    • Catley, B.J.1    Fraser, M.E.2
  • 20
    • 0344258795 scopus 로고
    • Isolation and enzymic determination of pullulan: Preparation of maltotriose
    • Catley B.J. Isolation and enzymic determination of pullulan: Preparation of maltotriose. Methods in Carbohydrate Chemistry. 10:1994;105-110.
    • (1994) Methods in Carbohydrate Chemistry , vol.10 , pp. 105-110
    • Catley, B.J.1
  • 21
    • 0028356152 scopus 로고
    • On the specificity of a bacteriophage borne endoglycanase for the native capsular polysaccharide produced by Klebsiella pneumoniae SK1 and its derived polymers
    • Cescutti P., Paoletti S. On the specificity of a bacteriophage borne endoglycanase for the native capsular polysaccharide produced by Klebsiella pneumoniae SK1 and its derived polymers. Biochem. Biophys. Res. Comm. 198:1994;1128-1134.
    • (1994) Biochem. Biophys. Res. Comm. , vol.198 , pp. 1128-1134
    • Cescutti, P.1    Paoletti, S.2
  • 22
    • 0021934215 scopus 로고
    • Depolymerization of capsular polysaccharide by glycanase activity of Klebsiella bacteriophage 51
    • Chakraborty A.K. Depolymerization of capsular polysaccharide by glycanase activity of Klebsiella bacteriophage 51. Ind. J. Biochem. 22:1985;22-26.
    • (1985) Ind. J. Biochem. , vol.22 , pp. 22-26
    • Chakraborty, A.K.1
  • 23
    • 0028243558 scopus 로고
    • Alginate from Pseudomonas fluorescens and Pseudomonas putida: Production and properties
    • Conti E., Flaibani A., O'Regan M., Sutherland I.W. Alginate from Pseudomonas fluorescens and Pseudomonas putida: production and properties. Microbiol. 140:1994;1128-1132.
    • (1994) Microbiol , vol.140 , pp. 1128-1132
    • Conti, E.1    Flaibani, A.2    O'Regan, M.3    Sutherland, I.W.4
  • 26
    • 0031912439 scopus 로고    scopus 로고
    • Purification and characterization of an acetyl xylan esterase from Bacillus pumilis
    • Degrassi G., Okeke B.C., Bruschi C.V., Venturi V. Purification and characterization of an acetyl xylan esterase from Bacillus pumilis. Appl. Env. Microbiol. 64:1998;789-792.
    • (1998) Appl. Env. Microbiol. , vol.64 , pp. 789-792
    • Degrassi, G.1    Okeke, B.C.2    Bruschi, C.V.3    Venturi, V.4
  • 27
    • 0021763030 scopus 로고
    • Preparation of a branched heptasaccharide by bacteriophage depolymerization of Klebsiella K60 capsular polysaccharide
    • DiFabio J.L., Dutton G.G.S., Parolis H. Preparation of a branched heptasaccharide by bacteriophage depolymerization of Klebsiella K60 capsular polysaccharide. Carbohydr. Res. 126:1984;261-269.
    • (1984) Carbohydr. Res. , vol.126 , pp. 261-269
    • Difabio, J.L.1    Dutton, G.G.S.2    Parolis, H.3
  • 28
    • 0022310990 scopus 로고
    • Novel oligosaccharides obtained by bacteriophage degradation of the olysaccharide from Klebsiella serotype K26
    • DiFabio J.L., Karunaratne D.N., Dutton G.G.S. Novel oligosaccharides obtained by bacteriophage degradation of the olysaccharide from Klebsiella serotype K26. Carbohydr. Res. 144:1986;251-261.
    • (1986) Carbohydr. Res. , vol.144 , pp. 251-261
    • Difabio, J.L.1    Karunaratne, D.N.2    Dutton, G.G.S.3
  • 29
    • 0345121296 scopus 로고
    • Use of a bacteriophage to depolymerize a polysaccharide
    • Dutton G.G.S., Savage A.V., Vignon M. Use of a bacteriophage to depolymerize a polysaccharide. Canad. J. Chem. 58:1980;2588-2591.
    • (1980) Canad. J. Chem. , vol.58 , pp. 2588-2591
    • Dutton, G.G.S.1    Savage, A.V.2    Vignon, M.3
  • 30
    • 0024289342 scopus 로고
    • N-acetyl-β-D-galactosaminidase activity of Escherichia coli phage 44
    • Dutton G.G.S, Lam Z., Lim A.V.S. N-acetyl-β-D-galactosaminidase activity of Escherichia coli phage 44. Carbohydr. Res. 183:1988;123-125.
    • (1988) Carbohydr. Res. , vol.183 , pp. 123-125
    • Dutton, G.S.1    Lam, Z.2    Lim, A.V.S.3
  • 31
    • 0022426101 scopus 로고
    • Bacteriophage degradation of Klebsiella K44 polysaccharide: An NMR study
    • Dutton G.G.S., Karunaratne D.N. Bacteriophage degradation of Klebsiella K44 polysaccharide: an NMR study. Carbohydr. Res. 138:1985;277-291.
    • (1985) Carbohydr. Res. , vol.138 , pp. 277-291
    • Dutton, G.G.S.1    Karunaratne, D.N.2
  • 32
    • 0023656705 scopus 로고
    • Structure of Escherichia coli capsular antigen K34
    • Dutton G.G.S., Kuma-Mintah A. Structure of Escherichia coli capsular antigen K34. Carbohydr. Res. 169:1987;213-220.
    • (1987) Carbohydr. Res. , vol.169 , pp. 213-220
    • Dutton, G.G.S.1    Kuma-Mintah, A.2
  • 33
    • 0020134063 scopus 로고
    • Acylated oligosaccharides from Klebsiella K63 capsular polysaccharide: Depolymerization by partial hydrolysis by bacteriophage-borne enzymes
    • Dutton G.G.S., Merrifield E.H. Acylated oligosaccharides from Klebsiella K63 capsular polysaccharide: depolymerization by partial hydrolysis by bacteriophage-borne enzymes. Carbohydr. Res. 103:1982;107-128.
    • (1982) Carbohydr. Res. , vol.103 , pp. 107-128
    • Dutton, G.G.S.1    Merrifield, E.H.2
  • 34
    • 0019871653 scopus 로고
    • Preparation of oligosaccharides by the action of bacteriophage borne enzymes on Klebsiella capsular polysaccharides
    • Dutton G.G.S., Fabio J.L.D., Leek D.M., Merrifield E.H., Nunn J.R., Stephen A.M. Preparation of oligosaccharides by the action of bacteriophage borne enzymes on Klebsiella capsular polysaccharides. Carbohydr. Res. 97:1981;127-138.
    • (1981) Carbohydr. Res. , vol.97 , pp. 127-138
    • Dutton, G.G.S.1    Fabio, J.L.D.2    Leek, D.M.3    Merrifield, E.H.4    Nunn, J.R.5    Stephen, A.M.6
  • 35
    • 0024289342 scopus 로고
    • N-acetyl-β-D-galactosaminidase activity of Escherichia coli phage 44
    • Dutton G.G.S., Lam Z., Lim A.V.S. N-acetyl-β-D-galactosaminidase activity of Escherichia coli phage 44. Carbohydr. Res. 183:1988;123-125.
    • (1988) Carbohydr. Res. , vol.183 , pp. 123-125
    • Dutton, G.G.S.1    Lam, Z.2    Lim, A.V.S.3
  • 36
    • 0022747109 scopus 로고
    • The use of bacteriophage depolymerization in the structural investigation of the capsular polysaccharide from Klebsiella serotype K3
    • Dutton G.G.S., Parolis H., Joseleau J.-P., Marais M.-F. The use of bacteriophage depolymerization in the structural investigation of the capsular polysaccharide from Klebsiella serotype K3. Carbohydr. Res. 149:1986;411-423.
    • (1986) Carbohydr. Res. , vol.149 , pp. 411-423
    • Dutton, G.G.S.1    Parolis, H.2    Joseleau, J.-P.3    Marais, M.-F.4
  • 38
    • 0019871188 scopus 로고
    • Substrate specificity of the glycanase activity associated with particles of Klebsiella bacteriophage no. 6
    • Elsässer-Beile U., Stirm S. Substrate specificity of the glycanase activity associated with particles of Klebsiella bacteriophage no. 6. Carbohydr Res. 88:1981;315-322.
    • (1981) Carbohydr Res , vol.88 , pp. 315-322
    • Elsässer-Beile, U.1    Stirm, S.2
  • 39
    • 0016701661 scopus 로고
    • Escherichia coli capsule bacteriophages. VII. Bacteriophage 29 - host capsular polysaccharide interactions
    • Fehmel F., Feige U., Niemann H., Stirm S. Escherichia coli capsule bacteriophages. VII. Bacteriophage 29 - host capsular polysaccharide interactions. J. Virol. 16:1975;591-601.
    • (1975) J. Virol. , vol.16 , pp. 591-601
    • Fehmel, F.1    Feige, U.2    Niemann, H.3    Stirm, S.4
  • 42
    • 0027109194 scopus 로고
    • Selective removal of α-D-galactose side chains from Rhizobium capsular polysaccharide by guar α-D-galactosidase: Effect on conformational stability and gelation
    • Gidley M.J., Eggleston G., Morris E.R. Selective removal of α-D-galactose side chains from Rhizobium capsular polysaccharide by guar α-D-galactosidase: effect on conformational stability and gelation. Carbohydr. Res. 231:1992;185-196.
    • (1992) Carbohydr. Res. , vol.231 , pp. 185-196
    • Gidley, M.J.1    Eggleston, G.2    Morris, E.R.3
  • 45
    • 0027380694 scopus 로고
    • Genes needed for the modification, polymerization, export and processing of succinoglycan by Rhizobium meliloti: A model for succinoglycan biosynthesis
    • Glucksman M.A, Reuber T.L., Walker G.C. Genes needed for the modification, polymerization, export and processing of succinoglycan by Rhizobium meliloti: a model for succinoglycan biosynthesis. J. Bacteriol. 175:1993;7045-7055.
    • (1993) J. Bacteriol. , vol.175 , pp. 7045-7055
    • Glucksman, M.A.1    Reuber, T.L.2    Walker, G.C.3
  • 46
    • 0028762581 scopus 로고
    • Structure of the capsular polysaccharide and the O-side chain of the lps from Acetobacter methanolicus
    • Grimmeke H.-D., Knirel Y.A., Shashkov A.S., Kiesel B., Lauk W., Voges M. Structure of the capsular polysaccharide and the O-side chain of the lps from Acetobacter methanolicus. Carbohydr. Res. 253:1994;277-282.
    • (1994) Carbohydr. Res. , vol.253 , pp. 277-282
    • Grimmeke, H.-D.1    Knirel, Y.A.2    Shashkov, A.S.3    Kiesel, B.4    Lauk, W.5    Voges, M.6
  • 47
    • 0028500630 scopus 로고
    • Structural investigation of the capsular polysaccharide of Escherichia coli O101:K103:H- using bacteriophage degradation and NMR spectroscopy
    • Grue M.R., Parolis H., Parolis L.A.S. Structural investigation of the capsular polysaccharide of Escherichia coli O101:K103:H- using bacteriophage degradation and NMR spectroscopy. Carbohydr. Res. 262:1994;311-322.
    • (1994) Carbohydr. Res. , vol.262 , pp. 311-322
    • Grue, M.R.1    Parolis, H.2    Parolis, L.A.S.3
  • 48
    • 0023955999 scopus 로고
    • A structural investigation of the capsular polysaccharide of Klebsiella K69
    • Hackland P.L., Parolis H., Parolis L.A.S. A structural investigation of the capsular polysaccharide of Klebsiella K69. Carbohydr. Res. 172:1988;209-216.
    • (1988) Carbohydr. Res. , vol.172 , pp. 209-216
    • Hackland, P.L.1    Parolis, H.2    Parolis, L.A.S.3
  • 49
    • 0023654291 scopus 로고
    • Purification, properties of a bacteriophage-induced endo-N-acetylneuraminidase
    • Hallenbeck P.C., Vimr E.R., Yu F., Bassler B., Troy F.A. Purification, properties of a bacteriophage-induced endo-N-acetylneuraminidase. J. Biol. Chem. 262:1987;3553-3561.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3553-3561
    • Hallenbeck, P.C.1    Vimr, E.R.2    Yu, F.3    Bassler, B.4    Troy, F.A.5
  • 50
    • 0029781011 scopus 로고    scopus 로고
    • Analysis of the enzymatic cleavage (β-elimination.) of the capsular K5 polysaccharide of Escherichia coli by the K5-specific coliphage: A re-examination
    • Hänfling P., Shashkov A.S., Jann B., Jann K. Analysis of the enzymatic cleavage (β-elimination.) of the capsular K5 polysaccharide of Escherichia coli by the K5-specific coliphage: a re-examination. J. Bacteriol. 178:1996;4747-4750.
    • (1996) J. Bacteriol. , vol.178 , pp. 4747-4750
    • Hänfling, P.1    Shashkov, A.S.2    Jann, B.3    Jann, K.4
  • 51
    • 0344258788 scopus 로고
    • Determination of the structure of β-D-glycans from strains of Agrobacterium and Rhizobium
    • Harada T. Determination of the structure of β-D-glycans from strains of Agrobacterium and Rhizobium. Methods in Carbohydrate Chemistry. 10:1994;155-164.
    • (1994) Methods in Carbohydrate Chemistry , vol.10 , pp. 155-164
    • Harada, T.1
  • 52
    • 0031106252 scopus 로고    scopus 로고
    • Microbial system for polysaccharide depolymerization - enzymatic route for gellan depolymerization by Bacillus sp. Gl1
    • Hashimoto W., Maesaka K., Sato N., Kimura S., Yamamoto K., Kumagai H., Murata K. Microbial system for polysaccharide depolymerization - enzymatic route for gellan depolymerization by Bacillus sp. Gl1. Arch. Biochem. Biophys. 339:1997;17-23.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 17-23
    • Hashimoto, W.1    Maesaka, K.2    Sato, N.3    Kimura, S.4    Yamamoto, K.5    Kumagai, H.6    Murata, K.7
  • 53
    • 0031858250 scopus 로고    scopus 로고
    • Polysaccharide lyase - molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1
    • Hashimoto W., Sato N., Kimura S., Murata K. Polysaccharide lyase - molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1. Arch. Biochem. Biophys. 354:1997;31-39.
    • (1997) Arch. Biochem. Biophys. , vol.354 , pp. 31-39
    • Hashimoto, W.1    Sato, N.2    Kimura, S.3    Murata, K.4
  • 54
    • 0022507398 scopus 로고
    • Biodegradation of xanthan by salt-tolerant aerobic microorganisms
    • Hou C.T., Barnabe N., Greaney K. Biodegradation of xanthan by salt-tolerant aerobic microorganisms. J. Ind. Microbiol. 1:1986;31-37.
    • (1986) J. Ind. Microbiol. , vol.1 , pp. 31-37
    • Hou, C.T.1    Barnabe, N.2    Greaney, K.3
  • 56
    • 0017188545 scopus 로고
    • Deacetylation reaction catalyzed by Salmonella phage
    • Iwashita S., Kanegasaki S. Deacetylation reaction catalyzed by Salmonella phage. J. Biol. Chem. 251:1976;5361-5365.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5361-5365
    • Iwashita, S.1    Kanegasaki, S.2
  • 57
    • 0030799166 scopus 로고    scopus 로고
    • Enzymatic removal and disinfection of bacterial biofilms
    • Johansen C., Falholt P., Gram L. Enzymatic removal and disinfection of bacterial biofilms. Appl. Env. Microbiol. 63:1997;3724-3728.
    • (1997) Appl. Env. Microbiol. , vol.63 , pp. 3724-3728
    • Johansen, C.1    Falholt, P.2    Gram, L.3
  • 58
    • 0028075943 scopus 로고
    • Gellan lyases - novel polysaccharide lyases
    • Kennedy L., Sutherland I.W. Gellan lyases - novel polysaccharide lyases. Microbiol. 140:1994;3007-3013.
    • (1994) Microbiol. , vol.140 , pp. 3007-3013
    • Kennedy, L.1    Sutherland, I.W.2
  • 60
    • 0016818521 scopus 로고
    • Disruption of Vi bacteriophage III and localization of its deacetylase activity
    • Kwiatkowski B., Beilharz H., Stirm S. Disruption of Vi bacteriophage III and localization of its deacetylase activity. J. Gen. Virol. 29:1975;267-280.
    • (1975) J. Gen. Virol. , vol.29 , pp. 267-280
    • Kwiatkowski, B.1    Beilharz, H.2    Stirm, S.3
  • 61
    • 0020701818 scopus 로고
    • Substrate specificity of two bacteriophage associated endo-N-acetylneuraminidases
    • Kwiatkowski B., Boschek B., Thiele H., Stirm S. Substrate specificity of two bacteriophage associated endo-N-acetylneuraminidases. J. Virol. 45:1983;367-374.
    • (1983) J. Virol , vol.45 , pp. 367-374
    • Kwiatkowski, B.1    Boschek, B.2    Thiele, H.3    Stirm, S.4
  • 62
    • 0025841767 scopus 로고
    • Molecular cloning of the extracellular endodextranase of Streptococcus salivarius
    • Lawman P., Bleiweis A.W. Molecular cloning of the extracellular endodextranase of Streptococcus salivarius. J. Bacteriol. 173:1991;7423-7428.
    • (1991) J. Bacteriol , vol.173 , pp. 7423-7428
    • Lawman, P.1    Bleiweis, A.W.2
  • 64
    • 0028997818 scopus 로고
    • Complete nucleotide sequence of the gene encoding bacteriophage E endosialidase: Implications for K1E endosialidase structure and function
    • Long G.S., Bryant J.M., Taylor P.W., Luzio J.P. Complete nucleotide sequence of the gene encoding bacteriophage E endosialidase: implications for K1E endosialidase structure and function. Biochem. J. 309:1995;43-550.
    • (1995) Biochem. J , vol.309 , pp. 43-550
    • Long, G.S.1    Bryant, J.M.2    Taylor, P.W.3    Luzio, J.P.4
  • 65
    • 0028814992 scopus 로고
    • Genes required for cellulose synthesis in Agrobacterium tumefaciens
    • Matthysse A.G., White S., Lightfoot R. Genes required for cellulose synthesis in Agrobacterium tumefaciens. J. Bacteriol. 177:1995;1069-1075.
    • (1995) J. Bacteriol , vol.177 , pp. 1069-1075
    • Matthysse, A.G.1    White, S.2    Lightfoot, R.3
  • 68
    • 0028843710 scopus 로고
    • Specific beta-glucanases as tools for polysaccharide structure determination
    • Mishra C., Robbins P.W. Specific beta-glucanases as tools for polysaccharide structure determination. Glycobiol. 5:1995;645-654.
    • (1995) Glycobiol , vol.5 , pp. 645-654
    • Mishra, C.1    Robbins, P.W.2
  • 69
    • 0019325732 scopus 로고
    • Dextran a (1→2) debranching enzyme from Flavobacterium
    • Mitsuishi Y., Kobayashi M., Matsuda K. Dextran a (1→2) debranching enzyme from Flavobacterium. Carbohydr. Res. 83:1980;303-313.
    • (1980) Carbohydr. Res. , vol.83 , pp. 303-313
    • Mitsuishi, Y.1    Kobayashi, M.2    Matsuda, K.3
  • 71
    • 0017594837 scopus 로고
    • Klebsiella serotype 25 capsular polysaccharide: Primary structure and deppolymerisation by a bacteriophage-borne glycanase
    • Niemann H., Kwiatkowski B., Westphal U., Stirm S. Klebsiella serotype 25 capsular polysaccharide: primary structure and deppolymerisation by a bacteriophage-borne glycanase. J. Bacteriol. 130:1977;366-374.
    • (1977) J. Bacteriol. , vol.130 , pp. 366-374
    • Niemann, H.1    Kwiatkowski, B.2    Westphal, U.3    Stirm, S.4
  • 72
    • 0345121286 scopus 로고
    • Kinetics and substrate specificity of the glycanase activity associated with particles of Klebsiella bacteriophage no 13
    • Niemann H., Beilharz H., Stirm S. Kinetics and substrate specificity of the glycanase activity associated with particles of Klebsiella bacteriophage no 13. Carbohydr. Res. 60:1978;353-366.
    • (1978) Carbohydr. Res. , vol.60 , pp. 353-366
    • Niemann, H.1    Beilharz, H.2    Stirm, S.3
  • 73
    • 0030801493 scopus 로고    scopus 로고
    • Degradation studies on Escherichia coli capsular polysaccharides by bacteriophages
    • Nimmich W. Degradation studies on Escherichia coli capsular polysaccharides by bacteriophages. FEMS Microbiol. Lett. 153:1997;105-110.
    • (1997) FEMS Microbiol. Lett. , vol.153 , pp. 105-110
    • Nimmich, W.1
  • 75
    • 0027415153 scopus 로고
    • Isolation and characterization of an exopolysaccharide depolymerase from Pseudomonas marginalis HTO41B
    • Osman S.F., Fett W.F., Irwin P.L. Isolation and characterization of an exopolysaccharide depolymerase from Pseudomonas marginalis HTO41B. Curr. Microbiol. 26:1993;299-304.
    • (1993) Curr. Microbiol. , vol.26 , pp. 299-304
    • Osman, S.F.1    Fett, W.F.2    Irwin, P.L.3
  • 76
    • 0020305639 scopus 로고
    • A succinoglycan-decomposing bacterium, Cytophaga arvensicola sp. nov
    • Oyaizu H., Komagata K., Amemura A., Harada T. A succinoglycan-decomposing bacterium, Cytophaga arvensicola sp. nov. J. Gen. Appl. Microbiol. 28:1982;369-388.
    • (1982) J. Gen. Appl. Microbiol. , vol.28 , pp. 369-388
    • Oyaizu, H.1    Komagata, K.2    Amemura, A.3    Harada, T.4
  • 77
    • 0023987839 scopus 로고
    • The use of bacteriophage-mediated depolymerisation in the structural investigation of the capsular polysaccharide from Escherichia coli serotype K36
    • Parolis H., Parolis L.A.S., Stanley S.M.R. The use of bacteriophage-mediated depolymerisation in the structural investigation of the capsular polysaccharide from Escherichia coli serotype K36. Carbohydr. Res. 175:1988;77-83.
    • (1988) Carbohydr. Res. , vol.175 , pp. 77-83
    • Parolis, H.1    Parolis, L.A.S.2    Stanley, S.M.R.3
  • 78
    • 0024614721 scopus 로고
    • Escherichia coli serotype 39 capsular polysaccharide: Primary structure and depolymerisation by a bacteriophage-associated glycanase
    • Parolis H., Parolis L.A.S., Ventner R.D. Escherichia coli serotype 39 capsular polysaccharide: Primary structure and depolymerisation by a bacteriophage-associated glycanase. Carbohydr. Res. 185:1989;225-232.
    • (1989) Carbohydr. Res. , vol.185 , pp. 225-232
    • Parolis, H.1    Parolis, L.A.S.2    Ventner, R.D.3
  • 79
    • 0027972749 scopus 로고
    • Detection of alginate lyase by activity staining after SDS PAGE and subsequent renaturation
    • Pecina A., Paneque A. Detection of alginate lyase by activity staining after SDS PAGE and subsequent renaturation. Analyt. Biochem. 217:1994;124-127.
    • (1994) Analyt. Biochem. , vol.217 , pp. 124-127
    • Pecina, A.1    Paneque, A.2
  • 80
    • 0017202486 scopus 로고
    • Enzymatic action of coliphage 8 and its possible role in infection
    • Prehm P., Jann K. Enzymatic action of coliphage 8 and its possible role in infection. J. Virol. 19:1976;940-949.
    • (1976) J. Virol. , vol.19 , pp. 940-949
    • Prehm, P.1    Jann, K.2
  • 81
    • 0342592236 scopus 로고
    • Purification and substrate specificity of an endo- dextranase of Streptococcus mutans K1-R
    • Pulkownik A., Walker G.J. Purification and substrate specificity of an endo- dextranase of Streptococcus mutans K1-R. Carbohydr. Res. 54:1977;237-251.
    • (1977) Carbohydr. Res. , vol.54 , pp. 237-251
    • Pulkownik, A.1    Walker, G.J.2
  • 82
    • 0345552586 scopus 로고
    • Spectroscopic analysis of oligosaccharides produced by bacteriophage-borne enzyme action on Klebsiella K36 polysaccharide
    • Ravenscroft N., Jackson G.E., Joao H., Stephen A.M. Spectroscopic analysis of oligosaccharides produced by bacteriophage-borne enzyme action on Klebsiella K36 polysaccharide. S. Afr. J. Chem. 41:1988;42.
    • (1988) S. Afr. J. Chem. , vol.41 , pp. 42
    • Ravenscroft, N.1    Jackson, G.E.2    Joao, H.3    Stephen, A.M.4
  • 83
    • 0019598870 scopus 로고
    • Comparative study of host capsule depolymerases associated with Klebsiella bacteriophages
    • Rieger-Hug D., Stirm S. Comparative study of host capsule depolymerases associated with Klebsiella bacteriophages. Virol. 113:1981;363-378.
    • (1981) Virol. , vol.113 , pp. 363-378
    • Rieger-Hug, D.1    Stirm, S.2
  • 84
    • 0002980031 scopus 로고
    • Enzymic hydrolysis of the bacterial polysaccharide xanthan by cellulase
    • Rinaudo M., Milas M. Enzymic hydrolysis of the bacterial polysaccharide xanthan by cellulase. Intern. J. Biol. Macromol. 2:1980;45-48.
    • (1980) Intern. J. Biol. Macromol. , vol.2 , pp. 45-48
    • Rinaudo, M.1    Milas, M.2
  • 85
    • 0015986805 scopus 로고
    • A bacterial dextranase releasing only isomaltose from dextrans
    • Sawai T., Toriyama K., Yano K. A bacterial dextranase releasing only isomaltose from dextrans. J. Biochem. 75:1974;105-112.
    • (1974) J. Biochem. , vol.75 , pp. 105-112
    • Sawai, T.1    Toriyama, K.2    Yano, K.3
  • 86
    • 0027185230 scopus 로고
    • Characterization of the Pseudomonas alginate lyase gene (algL): Cloning, sequencing and expression in Escherichia coli
    • Schiller N.L., Monday S.R., Boyd C., Keen N.T., Ohman D.E. Characterization of the Pseudomonas alginate lyase gene (algL): Cloning, sequencing and expression in Escherichia coli. J. Bacteriol. 175:1993;780-4789.
    • (1993) J. Bacteriol. , vol.175 , pp. 780-4789
    • Schiller, N.L.1    Monday, S.R.2    Boyd, C.3    Keen, N.T.4    Ohman, D.E.5
  • 87
    • 0000092834 scopus 로고
    • The production of alginate by Pseudomonas mendocina in batch and continuous culture
    • Sengha S.S, Anderson A.J., Hacking A.J., Dawes E. The production of alginate by Pseudomonas mendocina in batch and continuous culture. J. Gen. Microbiol. 135:1989;795-804.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 795-804
    • Sengha, S.S.1    Anderson, A.J.2    Hacking, A.J.3    Dawes, E.4
  • 88
    • 0021953149 scopus 로고
    • Exocellular esterase and emulsan release from the cell surface of Acinetobacter calcoaceticus
    • Shabtai Y., Gutnick D.L. Exocellular esterase and emulsan release from the cell surface of Acinetobacter calcoaceticus. J. Bacteriol. 161:1985;1176-1181.
    • (1985) J. Bacteriol. , vol.161 , pp. 1176-1181
    • Shabtai, Y.1    Gutnick, D.L.2
  • 89
    • 0022253054 scopus 로고
    • A sulfatase specific for glucuronic acid 2-sulfate
    • Shaklee P.N., Glaser J.H., Conrad H.E. A sulfatase specific for glucuronic acid 2-sulfate. J. Biol. Chem. 260:1985;9146-9149.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9146-9149
    • Shaklee, P.N.1    Glaser, J.H.2    Conrad, H.E.3
  • 90
    • 0030788755 scopus 로고    scopus 로고
    • Identification of a bacterial pectin acetyl esterase in Erwinia chrysanthemi 3937
    • Shevchik V.E., Hugouvieux-Cotte-Pattat N. Identification of a bacterial pectin acetyl esterase in Erwinia chrysanthemi 3937. Mol. Microbiol. 24:1997;1285-1301.
    • (1997) Mol. Microbiol. , vol.24 , pp. 1285-1301
    • Shevchik, V.E.1    Hugouvieux-Cotte-Pattat, N.2
  • 91
    • 0028266846 scopus 로고
    • Morphology and hydrolytic activity of A7, a typing phage of Pseudomonas syringae pv. morsprunorum
    • Smith A.R.W., Zamze S.E., Hignett R.C. Morphology and hydrolytic activity of A7, a typing phage of Pseudomonas syringae pv. morsprunorum. Microbiol. 140:1994;905-913.
    • (1994) Microbiol. , vol.140 , pp. 905-913
    • Smith, A.R.W.1    Zamze, S.E.2    Hignett, R.C.3
  • 92
    • 0028044970 scopus 로고
    • A new gene required for cellulose production and a gene encoding cellulolytic activity in Acetobacter xylinum are co-localized with the bcs operon
    • Standal R., Iversen T., Coucheron D.H., Fjaervik E., Blatny J., Valla S. A new gene required for cellulose production and a gene encoding cellulolytic activity in Acetobacter xylinum are co-localized with the bcs operon. J. Bacteriol. 176:1994;665-672.
    • (1994) J. Bacteriol. , vol.176 , pp. 665-672
    • Standal, R.1    Iversen, T.2    Coucheron, D.H.3    Fjaervik, E.4    Blatny, J.5    Valla, S.6
  • 93
    • 0031564610 scopus 로고    scopus 로고
    • Phage P22 tailspike protein - crystal structure of the head-binding domain at 2.3 angstrom, fully refined structure of the endorhamnosidase at 1.56 angstrom resolution and the molecular basis of O-antigen recognition and cleavage
    • Steinbacher S., Mille S., Baxa U., Budisa N., Weintraub A., Seckler R., Huber R. Phage P22 tailspike protein - crystal structure of the head-binding domain at 2.3 angstrom, fully refined structure of the endorhamnosidase at 1.56 angstrom resolution and the molecular basis of O-antigen recognition and cleavage. J. Mol. Biol. 267:1997;865-880.
    • (1997) J. Mol. Biol. , vol.267 , pp. 865-880
    • Steinbacher, S.1    Mille, S.2    Baxa, U.3    Budisa, N.4    Weintraub, A.5    Seckler, R.6    Huber, R.7
  • 94
    • 0345552585 scopus 로고
    • Examination of the repeating units of bacterial exopolysaccharides: Use of bacteriophage-associated enzymes
    • Stirm S. Examination of the repeating units of bacterial exopolysaccharides: use of bacteriophage-associated enzymes. Methods in Carbohydrate Chemistry. 10:1994;143-154.
    • (1994) Methods in Carbohydrate Chemistry , vol.10 , pp. 143-154
    • Stirm, S.1
  • 95
    • 0015118955 scopus 로고
    • Escherichia coli capsule bacteriophages. II. Morphology
    • Stirm S., Freund-Mölbert E. Escherichia coli capsule bacteriophages. II. Morphology. J. Virol. 8:1971;330-342.
    • (1971) J. Virol. , vol.8 , pp. 330-342
    • Stirm, S.1    Freund-Mölbert, E.2
  • 97
    • 0029922414 scopus 로고    scopus 로고
    • Polysaccharide lyases from gellan-producing Sphingomonas spp
    • Sutherland I.W., Kennedy L. Polysaccharide lyases from gellan-producing Sphingomonas spp. Microbiol. 142:1996;867-872.
    • (1996) Microbiol. , vol.142 , pp. 867-872
    • Sutherland, I.W.1    Kennedy, L.2
  • 98
    • 0017178281 scopus 로고
    • Highly specific bacteriophage associated polysaccharide hydrolases for Klebsiella aerogenes type 8
    • Sutherland I.W. Highly specific bacteriophage associated polysaccharide hydrolases for Klebsiella aerogenes type 8. J. Gen. Microbiol. 94:1976;211-216.
    • (1976) J. Gen. Microbiol. , vol.94 , pp. 211-216
    • Sutherland, I.W.1
  • 99
    • 0002873095 scopus 로고
    • Hydrolysis of unordered xanthan in solution by fungal cellulases
    • Sutherland I.W. Hydrolysis of unordered xanthan in solution by fungal cellulases. Carbohydr. Res. 131:1984;93-104.
    • (1984) Carbohydr. Res. , vol.131 , pp. 93-104
    • Sutherland, I.W.1
  • 100
    • 0023546896 scopus 로고
    • Xanthan lyases - novel enzymes found in various bacterial species
    • Sutherland I.W. Xanthan lyases - novel enzymes found in various bacterial species. J. Gen. Microbiol. 133:1987;3129-3134.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 3129-3134
    • Sutherland, I.W.1
  • 101
  • 102
    • 0000542948 scopus 로고    scopus 로고
    • Microbial exopolysaccharides - structural subtleties and their consequences
    • Sutherland I.W. Microbial exopolysaccharides - structural subtleties and their consequences. Pure Appl. Chem. 69:1997;1911-1917.
    • (1997) Pure Appl. Chem. , vol.69 , pp. 1911-1917
    • Sutherland, I.W.1
  • 103
    • 0029922414 scopus 로고    scopus 로고
    • Polysaccharide lyases from gellan-producing Sphingomonas spp
    • Sutherland .W., Kennedy . Polysaccharide lyases from gellan-producing Sphingomonas spp. Microbiol. 142:1996;867-872.
    • (1996) Microbiol. , vol.142 , pp. 867-872
    • Sutherland, W.1    Kennedy2
  • 104
    • 84985044930 scopus 로고
    • Synthesis and properties of a mutant type of xanthan
    • Tait M.I., Sutherland I.W. Synthesis and properties of a mutant type of xanthan. J. Appl. Bact. 66:1989;457-460.
    • (1989) J. Appl. Bact. , vol.66 , pp. 457-460
    • Tait, M.I.1    Sutherland, I.W.2
  • 105
    • 85007956438 scopus 로고
    • Promotion of barley root elongation under hypoxic conditions by alginate lyase lysate
    • Tomoda Y., Umemura K., Adachi T. Promotion of barley root elongation under hypoxic conditions by alginate lyase lysate. Biosci. Biotech. Biochem. 58:1993;202-203.
    • (1993) Biosci. Biotech. Biochem. , vol.58 , pp. 202-203
    • Tomoda, Y.1    Umemura, K.2    Adachi, T.3
  • 106
    • 0002030556 scopus 로고
    • Inducible polysaccharide depolymerases of Bacillus palustris
    • Torriani A., Pappenheimer A.M. Inducible polysaccharide depolymerases of Bacillus palustris. J. Biol. Chem. 237:1962;3-13.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3-13
    • Torriani, A.1    Pappenheimer, A.M.2
  • 108
    • 0025372219 scopus 로고
    • Formation of an extracellular energy reserve by Cellulomonas flavigena strain KU
    • Voepel K.C., Buller C.S. Formation of an extracellular energy reserve by Cellulomonas flavigena strain KU. J. Ind. Microbiol. 5:1990;131-138.
    • (1990) J. Ind. Microbiol. , vol.5 , pp. 131-138
    • Voepel, K.C.1    Buller, C.S.2
  • 109
    • 0029914954 scopus 로고    scopus 로고
    • Linkage of genes essential for synthesis of a polysaccharide capsule in Sphingomonas Strain S88
    • Yamazaki M., Thorne L., Mikolajczak M.J., Armentrout R.W., Pollock T.J. Linkage of genes essential for synthesis of a polysaccharide capsule in Sphingomonas Strain S88. J. Bacteriol. 178:1996;2676-2687.
    • (1996) J. Bacteriol. , vol.178 , pp. 2676-2687
    • Yamazaki, M.1    Thorne, L.2    Mikolajczak, M.J.3    Armentrout, R.W.4    Pollock, T.J.5
  • 110
    • 0031858627 scopus 로고    scopus 로고
    • The succinyl and acetyl modifications of succinoglycan influence susceptibility to cleavage by the Rhizobium meliloti glycanases ExoK, ExsH
    • York G.M., Walker G.C. The succinyl and acetyl modifications of succinoglycan influence susceptibility to cleavage by the Rhizobium meliloti glycanases ExoK, ExsH. J. Bacteriol. 180:1998;4184-4191.
    • (1998) J. Bacteriol. , vol.180 , pp. 4184-4191
    • York, G.M.1    Walker, G.C.2
  • 111
    • 0015240209 scopus 로고
    • Catalytic and molecular properties of a phage induced capsular polysaccharide depolymerase
    • Yurewicz E.C., Ghalambor M.A., Duckworth D.H., Heath E.C. Catalytic and molecular properties of a phage induced capsular polysaccharide depolymerase. J. Biol. Chem. 246:1971;5607-5616.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5607-5616
    • Yurewicz, E.C.1    Ghalambor, M.A.2    Duckworth, D.H.3    Heath, E.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.