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Volumn , Issue , 2010, Pages 295-324

Chitin/chitosan oligosaccharides: Effective substrates for functional analysis of chitinases/chitosanases

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EID: 84877021559     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/EBK1439816035     Document Type: Chapter
Times cited : (12)

References (67)
  • 1
    • 17044455396 scopus 로고    scopus 로고
    • Transglycosidase activity of chitotriosidase: Improved enzymatic assay for the human macrophage chitinase
    • Aguilera, B., Ghauharali-van der Vlugt, K., Helmond, M.T. et al. 2003. Transglycosidase activity of chitotriosidase: Improved enzymatic assay for the human macrophage chitinase. J. Biol. Chem. 278: 40911-40916.
    • (2003) J. Biol. Chem , vol.278 , pp. 40911-40916
    • Aguilera, B.1    Ghauharali-Van Der Vlugt, K.2    Helmond, M.T.3
  • 2
    • 0028648428 scopus 로고
    • Preparation of N-acetylchitooligosaccharides by hydrolysis of chitosan with chitinase followed by N-acetylation
    • Aiba, S. 1994. Preparation of N-acetylchitooligosaccharides by hydrolysis of chitosan with chitinase followed by N-acetylation. Carbohydr. Res. 265: 323-328.
    • (1994) Carbohydr. Res , vol.265 , pp. 323-328
    • Aiba, S.1
  • 3
    • 0028858320 scopus 로고
    • Molecular weight manipulation of chitosan. I: Kinetics of depolymerization by nitrous acid
    • Allan, G.G. and Peyron, M. 1995. Molecular weight manipulation of chitosan. I: Kinetics of depolymerization by nitrous acid. Carbohydr. Res. 277: 257-272.
    • (1995) Carbohydr. Res , vol.277 , pp. 257-272
    • Allan, G.G.1    Peyron, M.2
  • 4
    • 0030904072 scopus 로고    scopus 로고
    • Heterologous expression and characterization of wild-type and mutant forms of a 26 kDa endochitinase from barley (Hordeum vulgare L.)
    • Andersen, M.D., Jensen, A., Robertus, J.D., Leah, R., and Skriver, K. 1997. Heterologous expression and characterization of wild-type and mutant forms of a 26 kDa endochitinase from barley (Hordeum vulgare L.). Biochem. J. 322: 815-822.
    • (1997) Biochem. J , vol.322 , pp. 815-822
    • Andersen, M.D.1    Jensen, A.2    Robertus, J.D.3    Leah, R.4    Skriver, K.5
  • 5
    • 0036060518 scopus 로고    scopus 로고
    • Sequence analysis of chitooligosaccharides by matrix-assisted laser desorption ionization postsource decay mass spectrometry
    • Bahrke, S., Einarsson, J.M., Gislason, J. et al. 2002. Sequence analysis of chitooligosaccharides by matrix-assisted laser desorption ionization postsource decay mass spectrometry. Biomacromolecules 3: 696-704.
    • (2002) Biomacromolecules , vol.3 , pp. 696-704
    • Bahrke, S.1    Einarsson, J.M.2    Gislason, J.3
  • 6
    • 0015320975 scopus 로고
    • Preparation of 2-acetamido-2-deoxy-β-D-glucose oligosaccharides from acid hydrolyzates of chitin by electrolytic desalting and exclusion chromatography
    • Berkeley, R.C., Brewer, S.J., and Ortiz, J.M., 1972. Preparation of 2-acetamido-2-deoxy-β-D-glucose oligosaccharides from acid hydrolyzates of chitin by electrolytic desalting and exclusion chromatography. Anal. Biochem. 46: 687-690.
    • (1972) Anal. Biochem , vol.46 , pp. 687-690
    • Berkeley, R.C.1    Brewer, S.J.2    Ortiz, J.M.3
  • 7
    • 0029622470 scopus 로고
    • Site-directed mutagenesis of evolutionary conserved carboxylic amino acids in the chitosanase from Streptomyces sp. N174 reveals two residues essential for catalysis
    • Boucher, I., Fukamizo, T., Honda, Y., Willick, G.E., Neugebauer, W.A., and Brzezinski, R. 1995. Site-directed mutagenesis of evolutionary conserved carboxylic amino acids in the chitosanase from Streptomyces sp. N174 reveals two residues essential for catalysis. J. Biol. Chem. 270: 31077-31082.
    • (1995) J. Biol. Chem , vol.270 , pp. 31077-31082
    • Boucher, I.1    Fukamizo, T.2    Honda, Y.3    Willick, G.E.4    Neugebauer, W.A.5    Brzezinski, R.6
  • 8
    • 0018406452 scopus 로고
    • The use of an amino acid analyzer for the rapid identification and quantitative determination of chitosan oligosaccharides
    • Chang, J.J. and Hash, J.H. 1979. The use of an amino acid analyzer for the rapid identification and quantitative determination of chitosan oligosaccharides. Anal. Biochem. 95: 563-567.
    • (1979) Anal. Biochem , vol.95 , pp. 563-567
    • Chang, J.J.1    Hash, J.H.2
  • 9
    • 0034525137 scopus 로고    scopus 로고
    • An Aspergillus chitosanase with potential for large-scale preparation of chitosan oligosaccharides
    • Cheng, C.Y. and Li, Y.K. 2000. An Aspergillus chitosanase with potential for large-scale preparation of chitosan oligosaccharides. Biotechnol. Appl. Biochem. 32: 197-203.
    • (2000) Biotechnol. Appl. Biochem , vol.32 , pp. 197-203
    • Cheng, C.Y.1    Li, Y.K.2
  • 10
    • 4143127722 scopus 로고    scopus 로고
    • Purification and characterization of chitosanase from Bacillus sp. Strain KCTC 0377BP and its application for the production of chitosan oligosaccharides
    • Choi, Y.J., Kim, E.J., Piao, Z., Yun, Y.C., and Shin, Y.C. 2004. Purification and characterization of chitosanase from Bacillus sp. strain KCTC 0377BP and its application for the production of chitosan oligosaccharides. Appl. Environ. Microbiol. 70: 4522-4531.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 4522-4531
    • Choi, Y.J.1    Kim, E.J.2    Piao, Z.3    Yun, Y.C.4    Shin, Y.C.5
  • 11
    • 33645010330 scopus 로고    scopus 로고
    • Two exob- D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases
    • Côté, N., Fleury, A., Dumont-Blanchette, E., Fukamizo, T., Mitsutomi, M., and Brzezinski, R. 2006. Two exob- D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases. Biochem. J. 394: 675-686.
    • (2006) Biochem. J. , vol.394 , pp. 675-686
    • Côté, N.1    Fleury, A.2    Dumont-Blanchette, E.3    Fukamizo, T.4    Mitsutomi, M.5    Brzezinski, R.6
  • 12
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies, G.J., Wilson, K.S., and Henrissat, B. 1997. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321: 557-559.
    • (1997) Biochem. J , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 13
    • 0028485452 scopus 로고
    • A convenient access to β-(1→4)-linked 2-amino-2-deoxy- D-glucopyranosyl fluoride oligosaccharides and β-(1→4)-linked 2-amino-2-deoxy-D-glucopyranosyl oligosaccharides by fluorolysis and fluorohydrolysis of chitosan
    • Defaye, J., Gadelle, A., and Pedersen, C. 1994. A convenient access to β-(1→4)-linked 2-amino-2-deoxy- D-glucopyranosyl fluoride oligosaccharides and β-(1→4)-linked 2-amino-2-deoxy-D-glucopyranosyl oligosaccharides by fluorolysis and fluorohydrolysis of chitosan. Carbohydr. Res. 261: 267-277.
    • (1994) Carbohydr. Res , vol.261 , pp. 267-277
    • Defaye, J.1    Gadelle, A.2    Pedersen, C.3
  • 14
    • 41549102790 scopus 로고    scopus 로고
    • Oligosaccharide hydrolysis by chitosanase enzymes monitored by real-time electrospray ionization-mass spectrometry
    • Dennhart, N., Fukamizo, T., Brzezinski, R., Lacombe-Harvey, M.E., and Letzel, T. 2008. Oligosaccharide hydrolysis by chitosanase enzymes monitored by real-time electrospray ionization-mass spectrometry. J. Biotechnol. 134: 253-260.
    • (2008) J. Biotechnol , vol.134 , pp. 253-260
    • Dennhart, N.1    Fukamizo, T.2    Brzezinski, R.3    Lacombe-Harvey, M.E.4    Letzel, T.5
  • 15
    • 0024419609 scopus 로고
    • Glucosamine oligomers: 1. Preparation and characterization
    • Domard, A. and Cartier, N. 1989. Glucosamine oligomers: 1. Preparation and characterization. Int. J. Biol. Macromol. 11: 297-302.
    • (1989) Int. J. Biol. Macromol , vol.11 , pp. 297-302
    • Domard, A.1    Cartier, N.2
  • 16
    • 0017623908 scopus 로고
    • Analysis of the lysozyme-catalyzed hydrolysis and transglycosylation of N-acetyl-D-glucosamine oligomers by high-pressure liquid chromatography
    • Eikeren, P.V. and McLaughin, H. 1977. Analysis of the lysozyme-catalyzed hydrolysis and transglycosylation of N-acetyl-D-glucosamine oligomers by high-pressure liquid chromatography. Anal. Biochem. 77: 513-522.
    • (1977) Anal. Biochem , vol.77 , pp. 513-522
    • Eikeren, P.V.1    McLaughin, H.2
  • 17
    • 0034236249 scopus 로고    scopus 로고
    • Chitinolytic enzymes: Catalysis, substrate binding, and their application
    • Fukamizo, T. 2000. Chitinolytic enzymes: Catalysis, substrate binding, and their application. Curr. Protein Pept. Sci. 1: 105-124.
    • (2000) Curr. Protein Pept. Sci , vol.1 , pp. 105-124
    • Fukamizo, T.1
  • 18
    • 0020092071 scopus 로고
    • Separation and mutarotation of anomers of chitooligosaccharides
    • Fukamizo, T. and Hayashi, K. 1982. Separation and mutarotation of anomers of chitooligosaccharides. J. Biochem. 91: 619-626.
    • (1982) J. Biochem , vol.91 , pp. 619-626
    • Fukamizo, T.1    Hayashi, K.2
  • 19
    • 0031312196 scopus 로고    scopus 로고
    • Chitosanase from Streptomyces sp. Strain N174: A comparative review of its structure and function
    • Fukamizo, T. and Brzezinski, R. 1997. Chitosanase from Streptomyces sp. strain N174: A comparative review of its structure and function. Biochem. Cell Biol. 75: 687-696.
    • (1997) Biochem. Cell Biol , vol.75 , pp. 687-696
    • Fukamizo, T.1    Brzezinski, R.2
  • 21
    • 0023050064 scopus 로고
    • Analysis of chitin structure by nuclear magnetic resonance spectroscopy and chitinolytic enzyme digestion
    • Fukamizo, T., Krame, K.J., Mueller, D.D., Schaefer, J., Garbow, J., and Jacob, G.S. 1986b. Analysis of chitin structure by nuclear magnetic resonance spectroscopy and chitinolytic enzyme digestion. Arch. Biochem. Biophys. 249: 15-26.
    • (1986) Arch. Biochem. Biophys , vol.249 , pp. 15-26
    • Fukamizo, T.1    Krame, K.J.2    Mueller, D.D.3    Schaefer, J.4    Garbow, J.5    Jacob, G.S.6
  • 22
    • 0026236452 scopus 로고
    • NMR spectra of partially deacetylated chitotrisaccharides
    • Fukamizo, T., Ohtakara, A., Mitsutomi, M., and Goto, S. 1991. NMR spectra of partially deacetylated chitotrisaccharides. Agric. Biol. Chem. 55: 2653-2655.
    • (1991) Agric. Biol. Chem , vol.55 , pp. 2653-2655
    • Fukamizo, T.1    Ohtakara, A.2    Mitsutomi, M.3    Goto, S.4
  • 23
    • 0026613757 scopus 로고
    • 1H-NMR study on the chitotrisaccharide binding to hen egg white lysozyme
    • Fukamizo, T., Ikeda, Y., Ohkawa, T., and Goto, S. 1992. 1H-NMR study on the chitotrisaccharide binding to hen egg white lysozyme. Eur. J. Biochem. 210: 351-357.
    • (1992) Eur. J. Biochem , vol.210 , pp. 351-357
    • Fukamizo, T.1    Ikeda, Y.2    Ohkawa, T.3    Goto, S.4
  • 24
    • 0028827046 scopus 로고
    • Reaction mechanism of chitosanase from Streptomyces sp. N174
    • Fukamizo, T., Honda, Y., Goto, S., Boucher, I., and Brzezinski, R. 1995. Reaction mechanism of chitosanase from Streptomyces sp. N174. Biochem. J. 311: 377-383.
    • (1995) Biochem. J , vol.311 , pp. 377-383
    • Fukamizo, T.1    Honda, Y.2    Goto, S.3    Boucher, I.4    Brzezinski, R.5
  • 25
    • 0035957051 scopus 로고    scopus 로고
    • Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis
    • Fukamizo, T., Sasaki, C., Schelp, E., Bortone, K., and Robertus, J.D. 2001. Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis. Biochemistry 40: 2448-2454.
    • (2001) Biochemistry , vol.40 , pp. 2448-2454
    • Fukamizo, T.1    Sasaki, C.2    Schelp, E.3    Bortone, K.4    Robertus, J.D.5
  • 26
    • 30344445355 scopus 로고    scopus 로고
    • Bacillus circulans MH-K1 chitosanase: Amino acid residues responsible for substrate binding
    • Fukamizo, T., Amano, S., Yamaguchi, K. et al. 2005. Bacillus circulans MH-K1 chitosanase: Amino acid residues responsible for substrate binding. J. Biochem. 138: 563-569.
    • (2005) J. Biochem , vol.138 , pp. 563-569
    • Fukamizo, T.1    Amano, S.2    Yamaguchi, K.3
  • 27
    • 33749556013 scopus 로고    scopus 로고
    • Exo-b-D-glucosaminidase from Amycolatopsis orientalis: Catalytic residues, sugar recognition specificity, kinetics, and synergism
    • Fukamizo, T., Fleury, A., Côté, N., Mitsutomi, M., and Brzezinski, R. 2006. Exo-b-D-glucosaminidase from Amycolatopsis orientalis: Catalytic residues, sugar recognition specificity, kinetics, and synergism. Glycobiology 16: 1064-1072.
    • (2006) Glycobiology , vol.16 , pp. 1064-1072
    • Fukamizo, T.1    Fleury, A.2    Côté, N.3    Mitsutomi, M.4    Brzezinski, R.5
  • 29
    • 65249175634 scopus 로고    scopus 로고
    • Degradation of chitosans with chitinase G from Streptomyces coelicolor A3(2): Production of chito-oligosaccharides and insight into subsite specificities
    • Heggset, E.B., Hoell, I.A., Kristoffersen, M., Eijsink, V.G., and Vårum, K.M. 2009 Degradation of chitosans with chitinase G from Streptomyces coelicolor A3(2): Production of chito-oligosaccharides and insight into subsite specificities. Biomacromolecules 10: 892-899.
    • (2009) Biomacromolecules , vol.10 , pp. 892-899
    • Heggset, E.B.1    Hoell, I.A.2    Kristoffersen, M.3    Eijsink, V.G.4    Vårum, K.M.5
  • 31
    • 0032517353 scopus 로고    scopus 로고
    • Substrate binding subsites of chitinase from barley seeds and lysozyme from goose egg white
    • Honda, Y. and Fukamizo, T. 1998. Substrate binding subsites of chitinase from barley seeds and lysozyme from goose egg white. Biochim. Biophys. Acta. 1388: 53-65.
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 53-65
    • Honda, Y.1    Fukamizo, T.2
  • 32
    • 0031567585 scopus 로고    scopus 로고
    • Substrate binding to the inactive mutants of Streptomyces sp. N174 chitosanase: Indirect evaluation from the thermal unfolding experiments
    • Honda, Y., Fukamizo, T., Boucher, I., and Brzezinski, R. 1997. Substrate binding to the inactive mutants of Streptomyces sp. N174 chitosanase: Indirect evaluation from the thermal unfolding experiments. FEBS Lett. 411: 346-350.
    • (1997) FEBS Lett , vol.411 , pp. 346-350
    • Honda, Y.1    Fukamizo, T.2    Boucher, I.3    Brzezinski, R.4
  • 33
    • 33644935876 scopus 로고    scopus 로고
    • Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens
    • Horn, S.J., Sørbotten, A., Synstad, B. et al. 2006a. Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. FEBS J. 273: 491-503.
    • (2006) FEBS J , vol.273 , pp. 491-503
    • Horn, S.J.1    Sørbotten, A.2    Synstad, B.3
  • 34
    • 33845321374 scopus 로고    scopus 로고
    • Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides
    • Horn, S.J., Sikorski, P., Cederkvist, J.B. et al. 2006b. Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. Proc. Natl. Acad. Sci. U. S. A. 103: 18089-18094.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 18089-18094
    • Horn, S.J.1    Sikorski, P.2    Cederkvist, J.B.3
  • 36
    • 0026828080 scopus 로고
    • Action pattern of Bacillus sp. No. 7-M chitosanase on partially N-acetylated chitosan
    • Izume, M., Nagae, S., Kawagishi, H., Mitsutomi, M., and Ohtakara, A. 1992. Action pattern of Bacillus sp. no. 7-M chitosanase on partially N-acetylated chitosan. Biosci. Biotechnol. Biochem. 56: 448-453.
    • (1992) Biosci. Biotechnol. Biochem , vol.56 , pp. 448-453
    • Izume, M.1    Nagae, S.2    Kawagishi, H.3    Mitsutomi, M.4    Ohtakara, A.5
  • 37
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases—Regulation and function
    • Kasprzewska A. (2003) Plant chitinases—Regulation and function. Cell Mol. Biol. Lett. 8: 809-824.
    • (2003) Cell Mol. Biol. Lett , vol.8 , pp. 809-824
    • Kasprzewska, A.1
  • 38
  • 39
    • 0001199167 scopus 로고    scopus 로고
    • HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme
    • Koga, D., Yoshioka, T., and Arakane, Y. 1998. HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme. Biosci. Biotechnol. Biochem. 62: 1643-1646.
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , pp. 1643-1646
    • Koga, D.1    Yoshioka, T.2    Arakane, Y.3
  • 40
    • 0344110241 scopus 로고    scopus 로고
    • Insect chitinases: Molecular biology and potential use as biopesticides
    • Kramer, K.J. and Muthukrishnan, S. 1997. Insect chitinases: Molecular biology and potential use as biopesticides. Insect Biochem. Mol. Biol. 27: 887-900.
    • (1997) Insect Biochem. Mol. Biol , vol.27 , pp. 887-900
    • Kramer, K.J.1    Muthukrishnan, S.2
  • 41
    • 0020163235 scopus 로고
    • Estimation of the free energy change of substrate binding lysozyme-catalyzed reactions
    • Kuhara, S., Ezaki, E., Fukamizo, T., and Hayashi, K. 1982. Estimation of the free energy change of substrate binding lysozyme-catalyzed reactions. J. Biochem. 92: 121-127.
    • (1982) J. Biochem , vol.92 , pp. 121-127
    • Kuhara, S.1    Ezaki, E.2    Fukamizo, T.3    Hayashi, K.4
  • 42
    • 33750368039 scopus 로고    scopus 로고
    • Cloning, purification, and characterization of chitosanase from Bacillus sp. DAU101
    • Lee, Y.S., Yoo, J.S., Chung, S.Y., Lee, Y.C., Cho, Y.S., and Choi, Y.L. 2006. Cloning, purification, and characterization of chitosanase from Bacillus sp. DAU101. Appl. Microbiol. Biotechnol. 73: 113-121.
    • (2006) Appl. Microbiol. Biotechnol , vol.73 , pp. 113-121
    • Lee, Y.S.1    Yoo, J.S.2    Chung, S.Y.3    Lee, Y.C.4    Cho, Y.S.5    Choi, Y.L.6
  • 43
    • 0028999965 scopus 로고
    • Mass-spectrometric analysis of N-acetylchitooligosaccharides prepared through enzymatic hydrolysis of chitosan
    • Lopatin, S.A., Ilyin, M.M., Pustobaev, V.N., Bezchetnikova, Z.A., Varlamov, V.P., and Davankov, V.A. 1995. Mass-spectrometric analysis of N-acetylchitooligosaccharides prepared through enzymatic hydrolysis of chitosan. Anal. Biochem. 227: 285-288.
    • (1995) Anal. Biochem , vol.227 , pp. 285-288
    • Lopatin, S.A.1    Ilyin, M.M.2    Pustobaev, V.N.3    Bezchetnikova, Z.A.4    Varlamov, V.P.5    Davankov, V.A.6
  • 46
    • 0019631734 scopus 로고
    • Estimation of rate constants in lysozyme-catalyzed reaction of chitooligosaccharides
    • Masaki, A., Fukamizo, T., Otakara, A., Torikata, T., Hayashi, K., and Imoto, T. 1981b. Estimation of rate constants in lysozyme-catalyzed reaction of chitooligosaccharides. J. Biochem. 90: 1167-1175.
    • (1981) J. Biochem , vol.90 , pp. 1167-1175
    • Masaki, A.1    Fukamizo, T.2    Otakara, A.3    Torikata, T.4    Hayashi, K.5    Imoto, T.6
  • 47
    • 0025407307 scopus 로고
    • Action pattern of Aeromonas hydrophila chitinase on partially N-acetylated chitosan
    • Mitsutomi, M., Ohtakara, A., Fukamizo, T., and Goto, S. 1990. Action pattern of Aeromonas hydrophila chitinase on partially N-acetylated chitosan. Agric. Biol. Chem. 54: 871-877.
    • (1990) Agric. Biol. Chem , vol.54 , pp. 871-877
    • Mitsutomi, M.1    Ohtakara, A.2    Fukamizo, T.3    Goto, S.4
  • 48
    • 0029270304 scopus 로고
    • The action of Bacillus circulans WL-12 chitinases on partially N-acetylated chitosan
    • Mitsutomi, M., Kidoh, H., Tomita, H., and Watanabe, T. 1995. The action of Bacillus circulans WL-12 chitinases on partially N-acetylated chitosan. Biosci. Biotechnol. Biochem. 59: 529-531.
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 529-531
    • Mitsutomi, M.1    Kidoh, H.2    Tomita, H.3    Watanabe, T.4
  • 49
    • 0025656279 scopus 로고
    • Action pattern of Streptomyces griseus chitinase on partially N-acetylated chitosan
    • Ohtakara, A., Matsunaga, H., and Mitsutomi, M. 1990. Action pattern of Streptomyces griseus chitinase on partially N-acetylated chitosan. Agric. Biol. Chem. 54: 3191-3199.
    • (1990) Agric. Biol. Chem , vol.54 , pp. 3191-3199
    • Ohtakara, A.1    Matsunaga, H.2    Mitsutomi, M.3
  • 50
    • 0014110026 scopus 로고
    • Separation of chitin oligosaccharides by thin-layer chromatography
    • Powning, R.F. and Irzykiewicz, H. 1967. Separation of chitin oligosaccharides by thin-layer chromatography. J. Chromatogr. 29: 115-119.
    • (1967) J. Chromatogr , vol.29 , pp. 115-119
    • Powning, R.F.1    Irzykiewicz, H.2
  • 51
    • 0000269710 scopus 로고
    • The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of lowmolecular- weight substrates for lysozyme
    • Rupley, J.A. 1964. The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of lowmolecular- weight substrates for lysozyme. Biochim. Biophys. Acta. 83: 245-255.
    • (1964) Biochim. Biophys. Acta , vol.83 , pp. 245-255
    • Rupley, J.A.1
  • 52
    • 0030759788 scopus 로고    scopus 로고
    • Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coli
    • Samain, E., Drouillard, S., Heyraud, A., Driguez, H., and Geremia, R.A. 1997. Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coli. Carbohydr. Res. 302: 35-42.
    • (1997) Carbohydr. Res , vol.302 , pp. 35-42
    • Samain, E.1    Drouillard, S.2    Heyraud, A.3    Driguez, H.4    Geremia, R.A.5
  • 53
    • 0036232796 scopus 로고    scopus 로고
    • Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes
    • Sasaki, C., Yokoyama, A., Itoh, Y., Hashimoto, M., Watanabe, T., and Fukamizo, T. 2002. Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes. J. Biochem. 131: 557-564.
    • (2002) J. Biochem , vol.131 , pp. 557-564
    • Sasaki, C.1    Yokoyama, A.2    Itoh, Y.3    Hashimoto, M.4    Watanabe, T.5    Fukamizo, T.6
  • 54
    • 0037938666 scopus 로고    scopus 로고
    • Family 19 chitinase from rice (Oryza sativa L.): Substrate-binding subsites demonstrated by kinetic and molecular modeling studies
    • Sasaki, C., Itoh, Y., Takehara, H., Kuhara, S., and Fukamizo, T. 2003. Family 19 chitinase from rice (Oryza sativa L.): Substrate-binding subsites demonstrated by kinetic and molecular modeling studies. Plant Mol. Biol. 52: 43-52.
    • (2003) Plant Mol. Biol , vol.52 , pp. 43-52
    • Sasaki, C.1    Itoh, Y.2    Takehara, H.3    Kuhara, S.4    Fukamizo, T.5
  • 55
    • 33751352573 scopus 로고    scopus 로고
    • Rice chitinases: Sugar recognition specificities of the individual subsites
    • Sasaki, C., Vårum, K.M., Itoh, Y., Tamoi, M., and Fukamizo, T. 2006. Rice chitinases: Sugar recognition specificities of the individual subsites. Glycobiology 16: 1242-1250.
    • (2006) Glycobiology , vol.16 , pp. 1242-1250
    • Sasaki, C.1    Vårum, K.M.2    Itoh, Y.3    Tamoi, M.4    Fukamizo, T.5
  • 56
    • 33747088169 scopus 로고    scopus 로고
    • Serratia marcescens chitinases with tunnel-shaped substrate-binding grooves show endo activity and different degrees of processivity during enzymatic hydrolysis of chitosan
    • Sikorski, P., Sørbotten, A., Horn, S.J., Eijsink, V.G., and Vårum, K.M. 2006. Serratia marcescens chitinases with tunnel-shaped substrate-binding grooves show endo activity and different degrees of processivity during enzymatic hydrolysis of chitosan. Biochemistry 45: 9566-9574.
    • (2006) Biochemistry , vol.45 , pp. 9566-9574
    • Sikorski, P.1    Sørbotten, A.2    Horn, S.J.3    Eijsink, V.G.4    Vårum, K.M.5
  • 57
    • 12544256264 scopus 로고    scopus 로고
    • Degradation of chitosans with chitinase B from Serratia marcescens. Production of chito-oligosaccharides and insight into enzyme processivity
    • Sørbotten, A., Horn, S.J., Eijsink, V.G., and Vårum, K.M. 2005. Degradation of chitosans with chitinase B from Serratia marcescens. Production of chito-oligosaccharides and insight into enzyme processivity. FEBS J. 272: 538-549.
    • (2005) FEBS J , vol.272 , pp. 538-549
    • Sørbotten, A.1    Horn, S.J.2    Eijsink, V.G.3    Vårum, K.M.4
  • 58
    • 0042127130 scopus 로고    scopus 로고
    • Novel chitosanase from Streptomyces griseus HUT 6037 with transglycosylation activity
    • Tanabe, T., Morinaga, K., Fukamizo, T., and Mitsutomi, M. 2003. Novel chitosanase from Streptomyces griseus HUT 6037 with transglycosylation activity. Biosci. Biotechnol. Biochem. 67: 354-364.
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 354-364
    • Tanabe, T.1    Morinaga, K.2    Fukamizo, T.3    Mitsutomi, M.4
  • 59
    • 0345374008 scopus 로고    scopus 로고
    • Preparation and characterisation of oligosaccharides produced by nitrous acid depolymerisation of chitosans
    • Tømmeraas, K., Vårum, K.M., Christensen, B.E., and Smidsrød, O. 2001. Preparation and characterisation of oligosaccharides produced by nitrous acid depolymerisation of chitosans. Carbohydr. Res. 333: 137-144.
    • (2001) Carbohydr. Res , vol.333 , pp. 137-144
    • Tømmeraas, K.1    Vårum, K.M.2    Christensen, B.E.3    Smidsrød, O.4
  • 60
    • 0035202976 scopus 로고    scopus 로고
    • Mechanism of chitosanase-oligosaccharide interaction: Subsite structure of Streptomyces sp. N174 chitosanase and the role of Asp57 carboxylate
    • Tremblay, H., Yamaguchi, T., Fukamizo, T., and Brzezinski, R. 2001. Mechanism of chitosanase-oligosaccharide interaction: Subsite structure of Streptomyces sp. N174 chitosanase and the role of Asp57 carboxylate. J. Biochem. 130: 679-686.
    • (2001) J. Biochem , vol.130 , pp. 679-686
    • Tremblay, H.1    Yamaguchi, T.2    Fukamizo, T.3    Brzezinski, R.4
  • 61
    • 48449085799 scopus 로고    scopus 로고
    • Chemical preparation and structural characterization of a homogeneous series of chitin/chitosan oligomers
    • Trombotto, S., Ladavière, C., Delolme, F., and Domard, A. 2008. Chemical preparation and structural characterization of a homogeneous series of chitin/chitosan oligomers. Biomacromolecules 9: 1731-1738.
    • (2008) Biomacromolecules , vol.9 , pp. 1731-1738
    • Trombotto, S.1    Ladavière, C.2    Delolme, F.3    Domard, A.4
  • 62
    • 0025471599 scopus 로고
    • Enzymic synthesis of useful chito-oligosaccharides utilizing transglycosylation by chitinolytic enzymes in a buffer containing ammonium sulfate
    • Usui, T., Matsui, H., and Isobe, K. 1990. Enzymic synthesis of useful chito-oligosaccharides utilizing transglycosylation by chitinolytic enzymes in a buffer containing ammonium sulfate. Carbohydr. Res. 203: 65-77.
    • (1990) Carbohydr. Res , vol.203 , pp. 65-77
    • Usui, T.1    Matsui, H.2    Isobe, K.3
  • 63
    • 0030605966 scopus 로고    scopus 로고
    • Determination of enzymatic hydrolysis specificity of partially N-acetylated chitosans
    • Vårum, K.M., Holme, H.K., Izume, M., Stokke, B.T., and Smidsrød, O. 1996. Determination of enzymatic hydrolysis specificity of partially N-acetylated chitosans. Biochim. Biophys. Acta. 1291: 5-15.
    • (1996) Biochim. Biophys. Acta , vol.1291 , pp. 5-15
    • Vårum, K.M.1    Holme, H.K.2    Izume, M.3    Stokke, B.T.4    Smidsrød, O.5
  • 64
    • 0037339655 scopus 로고    scopus 로고
    • An extracellular Bacillus sp. Chitinase for the production of chitotriose as a major chitinolytic product
    • Woo, C.J. and Park, H.D. 2003. An extracellular Bacillus sp. chitinase for the production of chitotriose as a major chitinolytic product. Biotechnol. Lett. 25: 409-412.
    • (2003) Biotechnol. Lett , vol.25 , pp. 409-412
    • Woo, C.J.1    Park, H.D.2
  • 65
    • 0023654037 scopus 로고
    • Retention of anomeric form in lysozyme-catalyzed reaction
    • Yanase, Y., Fukamizo, T., Hayashi, K., and Goto, S. 1987. Retention of anomeric form in lysozyme-catalyzed reaction. Arch. Biochem. Biophys. 253: 168-175.
    • (1987) Arch. Biochem. Biophys , vol.253 , pp. 168-175
    • Yanase, Y.1    Fukamizo, T.2    Hayashi, K.3    Goto, S.4
  • 66
    • 0036560423 scopus 로고    scopus 로고
    • Gene cloning and biochemical analysis of thermostable chitosanase (TCH-2) from Bacillus coagulans CK108
    • Yoon, H.G., Lee, K.H., Kim, H.Y. et al. 2002. Gene cloning and biochemical analysis of thermostable chitosanase (TCH-2) from Bacillus coagulans CK108. Biosci. Biotechnol. Biochem. 66: 986-995.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 986-995
    • Yoon, H.G.1    Lee, K.H.2    Kim, H.Y.3
  • 67
    • 67449088829 scopus 로고    scopus 로고
    • Aromatic residues in the catalytic center of chitinase a from Serratia marcescens affect processivity, enzyme activity, and biomass-converting efficiency
    • Zakariassen, H., Aam, B.B., Horn, S.J., Vårum, K.M., Sørlie, M., and Eijsink, V.G. 2009. Aromatic residues in the catalytic center of chitinase a from Serratia marcescens affect processivity, enzyme activity, and biomass-converting efficiency. J. Biol. Chem. 284: 10610-10617.
    • (2009) J. Biol. Chem , vol.284 , pp. 10610-10617
    • Zakariassen, H.1    Aam, B.B.2    Horn, S.J.3    Vårum, K.M.4    Sørlie, M.5    Eijsink, V.G.6


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