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Volumn , Issue , 2010, Pages 185-191

Enzymatic modifications of chitin and chitosan

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EID: 85052000980     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/EBK1439816035     Document Type: Chapter
Times cited : (5)

References (40)
  • 1
    • 33745509211 scopus 로고    scopus 로고
    • Optimum substrate size and specific anomer requirements for the reducing-end glycoside hydrolase di-N-acetylchitobiase
    • Aronson, N. N. and Halloran, B. A. 2006. Optimum substrate size and specific anomer requirements for the reducing-end glycoside hydrolase di-N-acetylchitobiase. Biosci Biotechnol Biochem 70:1537-1541.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1537-1541
    • Aronson, N.N.1    Halloran, B.A.2
  • 2
    • 28844479325 scopus 로고    scopus 로고
    • Peripheral enzymatic deacetylation of chitin and reprecipitated chitin particles
    • Aye, K. N., Karuppuswamy, R., Ahamed, T., and Stevens, W. F. 2006. Peripheral enzymatic deacetylation of chitin and reprecipitated chitin particles. Bioresour Technol 97:577-582.
    • (2006) Bioresour Technol , vol.97 , pp. 577-582
    • Aye, K.N.1    Karuppuswamy, R.2    Ahamed, T.3    Stevens, W.F.4
  • 3
    • 33645010330 scopus 로고    scopus 로고
    • Two exo-β-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases
    • Cote, N., Fleury, A., Dumont-Blanchette, E., Fukamizo, T., Mitsutomi, M., and Brzezinski, R. 2006. Two exo-β-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
    • Cote, N.1    Fleury, A.2    Dumont-Blanchette, E.3    Fukamizo, T.4    Mitsutomi, M.5    Brzezinski, R.6
  • 4
    • 0036788052 scopus 로고    scopus 로고
    • Developmentally regulated conversion of surface-exposed chitin to chitosan in cell walls of plant pathogenic fungi
    • El Gueddari, N. E., Rauchhaus, U., Moerschbacher, B. M., and Deising, H. B. 2002. Developmentally regulated conversion of surface-exposed chitin to chitosan in cell walls of plant pathogenic fungi. New Phytol 156:103-112.
    • (2002) New Phytol , vol.156 , pp. 103-112
    • El Gueddari, N.E.1    Rauchhaus, U.2    Moerschbacher, B.M.3    Deising, H.B.4
  • 5
    • 84900431724 scopus 로고    scopus 로고
    • Substrates and products of chitin-and chitosan-modifying enzymes
    • S. Şenel, K. M. Vårum, M. M. Şumnu, and A. A. Hincal (Eds.), Ankara, Turkey: Hacettepe University Press
    • El Gueddari, N. E., Schaaf, A., Koflhoff, M., Gorzelanny, C., Schneider, S. W., and Moerschbacher, B. M. 2007. Substrates and products of chitin-and chitosan-modifying enzymes. In S. Şenel, K. M. Vårum, M. M. Şumnu, and A. A. Hincal (Eds.), Advances in Chitin Science, Vol. 10, pp. 119-126. Ankara, Turkey: Hacettepe University Press.
    • (2007) Advances in Chitin Science , vol.10 , pp. 119-126
    • El Gueddari, N.E.1    Schaaf, A.2    Koflhoff, M.3    Gorzelanny, C.4    Schneider, S.W.5    Moerschbacher, B.M.6
  • 6
    • 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
  • 7
    • 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
  • 8
    • 39649084901 scopus 로고    scopus 로고
    • Purification and characterization of chitosanase from Bacillus cereus D-11
    • Gao, X. A., Ju, W. T., Jung, W. J., and Park, R. D. 2008. Purification and characterization of chitosanase from Bacillus cereus D-11. Carbohydr Polym 72:513-520.
    • (2008) Carbohydr Polym , vol.72 , pp. 513-520
    • Gao, X.A.1    Ju, W.T.2    Jung, W.J.3    Park, R.D.4
  • 9
    • 67649363872 scopus 로고    scopus 로고
    • Reaction pattern of Bacillus cereus D-11 chitosanase on chitooligosaccharide alcohols
    • Gao, X. A., Jung, W. J., Kuk, J. H., and Park, R. D. 2009. Reaction pattern of Bacillus cereus D-11 chitosanase on chitooligosaccharide alcohols. J Microbiol Biotechnol 19:358-361.
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 358-361
    • Gao, X.A.1    Jung, W.J.2    Kuk, J.H.3    Park, R.D.4
  • 10
    • 0042330067 scopus 로고    scopus 로고
    • Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: An investigation using steady-state kinetic analysis and MS
    • Hekmat, O., Tokuyasu, K., and Withers, S. G. 2003. Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: An investigation using steady-state kinetic analysis and MS. Biochem J 374:369-380.
    • (2003) Biochem J , vol.374 , pp. 369-380
    • Hekmat, O.1    Tokuyasu, K.2    Withers, S.G.3
  • 11
    • 40549140768 scopus 로고    scopus 로고
    • A reducing-end-acting chitinase from Vibrio proteolyticus belonging to glycoside hydrolase family 19
    • Honda, Y., Taniguchi, H., and Kitaoka, M. 2008. A reducing-end-acting chitinase from Vibrio proteolyticus belonging to glycoside hydrolase family 19. Appl Microbiol Biotechnol 78:627-634.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 627-634
    • Honda, Y.1    Taniguchi, H.2    Kitaoka, M.3
  • 12
    • 33644935876 scopus 로고    scopus 로고
    • Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens
    • Horn, S. J., Sorbotten, A., Synstad, B. et al. 2006. 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    Sorbotten, A.2    Synstad, B.3
  • 13
    • 37149008789 scopus 로고    scopus 로고
    • High degree polymerized chitooligosaccharides synthesis by chitosanase in the bulk aqueous system and reversed micellar microreactors
    • Hsiao, Y. C., Lin, Y. W., Su, C. K., and Chiang, B. H. 2008. High degree polymerized chitooligosaccharides synthesis by chitosanase in the bulk aqueous system and reversed micellar microreactors. Process Biochem 43:76-82.
    • (2008) Process Biochem , vol.43 , pp. 76-82
    • Hsiao, Y.C.1    Lin, Y.W.2    Su, C.K.3    Chiang, B.H.4
  • 14
    • 2842597093 scopus 로고    scopus 로고
    • Characterization and kinetics of 45 kDa chitosanase from Bacillus sp. P16
    • Jo, Y. Y., Jo, K. J., Jin, Y. L. et al. 2003. Characterization and kinetics of 45 kDa chitosanase from Bacillus sp. P16. Biosci Biotechnol Biochem 67:1875-1882.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 1875-1882
    • Jo, Y.Y.1    Jo, K.J.2    Jin, Y.L.3
  • 15
    • 0027531525 scopus 로고
    • Rhizobium NodB protein involved in nodulation signal synthesis is a chitooligosaccharide deacetylase
    • John, M., Rohrig, H., Schmidt, J., Wieneke, U., and Schell, J. 1993. Rhizobium NodB protein involved in nodulation signal synthesis is a chitooligosaccharide deacetylase. Proc Natl Acad Sci U S A 90:625-629.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 625-629
    • John, M.1    Rohrig, H.2    Schmidt, J.3    Wieneke, U.4    Schell, J.5
  • 16
    • 28844452208 scopus 로고    scopus 로고
    • Purification and characterization of exo-β-D-glucosaminidase from Aspergillus fumigatus S-26
    • Jung, W. J., Kuk, J. H., Kim, K. Y., Jung, K. C., and Park, R. D. 2006. Purification and characterization of exo-β-D-glucosaminidase from Aspergillus fumigatus S-26. Protein Expr Purif 45:125-131.
    • (2006) Protein Expr Purif , vol.45 , pp. 125-131
    • Jung, W.J.1    Kuk, J.H.2    Kim, K.Y.3    Jung, K.C.4    Park, R.D.5
  • 17
    • 18144384257 scopus 로고    scopus 로고
    • Purification and characterization of chitinase from Paenibacillus illinoisensis KJA-424
    • Jung, W. J., Kuk, J. H., Kim, K. Y., Kim, T. H., and Park, R. D. 2005. Purification and characterization of chitinase from Paenibacillus illinoisensis KJA-424. J Microbiol Biotechnol 15:274-280.
    • (2005) J Microbiol Biotechnol , vol.15 , pp. 274-280
    • Jung, W.J.1    Kuk, J.H.2    Kim, K.Y.3    Kim, T.H.4    Park, R.D.5
  • 18
    • 34249864385 scopus 로고    scopus 로고
    • Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin
    • Kadokura, K., Rokutani, A., Yamamoto, M. et al. 2007. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl Microbiol Biotechnol 75:357-365.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 357-365
    • Kadokura, K.1    Rokutani, A.2    Yamamoto, M.3
  • 19
    • 13844299839 scopus 로고    scopus 로고
    • Selective preparation of N-acetyl-D-glucosamine and N, N′-diacetylchitobiose from chitin using a crude enzyme preparation from Aeromonas sp
    • Kuk, J. H., Jung, W. J., Jo, G. H., Ahn, J. S., Kim, K. Y., and Park, R. D. 2005. Selective preparation of N-acetyl-D-glucosamine and N, N′-diacetylchitobiose from chitin using a crude enzyme preparation from Aeromonas sp. Biotechnol Lett 27:7-11.
    • (2005) Biotechnol Lett , vol.27 , pp. 7-11
    • Kuk, J.H.1    Jung, W.J.2    Jo, G.H.3    Ahn, J.S.4    Kim, K.Y.5    Park, R.D.6
  • 20
    • 51449115651 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation
    • Li, C., Huang, W., and Wang, L. X. 2008. Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation. Bioorg Med Chem 16:8366-8372.
    • (2008) Bioorg Med Chem , vol.16 , pp. 8366-8372
    • Li, C.1    Huang, W.2    Wang, L.X.3
  • 21
    • 0031683066 scopus 로고    scopus 로고
    • Mode of action of chitin deacetylase from Mucor rouxii on partially N-acetylated chitosans
    • Martinou, A., Bouriotis, V., Stokke, B. T., and Vårum, K. M. 1998. Mode of action of chitin deacetylase from Mucor rouxii on partially N-acetylated chitosans. Carbohydr Res 311:71-78.
    • (1998) Carbohydr Res , vol.311 , pp. 71-78
    • Martinou, A.1    Bouriotis, V.2    Stokke, B.T.3    Vårum, K.M.4
  • 22
    • 85055228293 scopus 로고    scopus 로고
    • Classification of chitosanases by hydrolytic specificity against N, N4-diacetylchitohexaose
    • Mitsutomi, M., Watanabe, M., Hirano, K., and Seki, K. 2008. Classification of chitosanases by hydrolytic specificity against N, N4-diacetylchitohexaose. Eur Chitin Soc News Lett 24:8-9.
    • (2008) Eur Chitin Soc News Lett , vol.24 , pp. 8-9
    • Mitsutomi, M.1    Watanabe, M.2    Hirano, K.3    Seki, K.4
  • 23
    • 0025329913 scopus 로고
    • Purification and characterization of an exo-β-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis
    • Nanjo, F., Katsumi, R., and Sakai, K. 1990. Purification and characterization of an exo-β-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis. J Biol Chem 265:10088-10094.
    • (1990) J Biol Chem , vol.265 , pp. 10088-10094
    • Nanjo, F.1    Katsumi, R.2    Sakai, K.3
  • 24
    • 0031951409 scopus 로고    scopus 로고
    • Purification and characterization of exo-β-D-glucosaminidase from a cellulolytic fungus, Trichoderma reesei PC-3-7
    • Nogawa, M., Takahashi, H., Kashiwagi, A., Ohshima, K., Okada, H., and Morikawa, Y. 1998. Purification and characterization of exo-β-D-glucosaminidase from a cellulolytic fungus, Trichoderma reesei PC-3-7. Appl Environ Microbiol 64:890-895.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 890-895
    • Nogawa, M.1    Takahashi, H.2    Kashiwagi, A.3    Ohshima, K.4    Okada, H.5    Morikawa, Y.6
  • 26
    • 0036562588 scopus 로고    scopus 로고
    • Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: Enzymatic properties and synergism on chitin degradation
    • Suzuki, K., Sugawara, N., Suzuki, M. et al. 2002. Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: Enzymatic properties and synergism on chitin degradation. Biosci Biotechnol Biochem 66:1075-1083.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1075-1083
    • Suzuki, K.1    Sugawara, N.2    Suzuki, M.3
  • 27
    • 3142721163 scopus 로고    scopus 로고
    • Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka, T., Fukui, T., Fujiwara, S., Atomi, H., and Imanaka, T. 2004. Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Biol Chem 279:30021-30027.
    • (2004) J Biol Chem , vol.279 , pp. 30021-30027
    • Tanaka, T.1    Fukui, T.2    Fujiwara, S.3    Atomi, H.4    Imanaka, T.5
  • 28
    • 0034254598 scopus 로고    scopus 로고
    • Recognition of chitooligosaccharides and their N-acetyl groups by putative subsites of chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum
    • Tokuyasu, K., Mitsutomi, M., Yamaguchi, I., Hayashi, K., and Mori, Y. 2000a. Recognition of chitooligosaccharides and their N-acetyl groups by putative subsites of chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum. Biochemistry 39:8837-8843.
    • (2000) Biochemistry , vol.39 , pp. 8837-8843
    • Tokuyasu, K.1    Mitsutomi, M.2    Yamaguchi, I.3    Hayashi, K.4    Mori, Y.5
  • 29
    • 0032750475 scopus 로고    scopus 로고
    • Reverse hydrolysis reaction of chitin deacetylase and enzymatic synthesis of β-D-GlcNAc-(1-4)-GlcN from chitobiose
    • Tokuyasu, K., Ono, H., Hayashi, K., and Mori, Y. 1999. Reverse hydrolysis reaction of chitin deacetylase and enzymatic synthesis of β-D-GlcNAc-(1-4)-GlcN from chitobiose. Carbohydr Res 322:26-31.
    • (1999) Carbohydr Res , vol.322 , pp. 26-31
    • Tokuyasu, K.1    Ono, H.2    Hayashi, K.3    Mori, Y.4
  • 30
    • 0034690169 scopus 로고    scopus 로고
    • Synthesis of a chitosan tetramer derivative, β-D-GlcNAc-(1-4)-β-D-GlcNAc-(1-4)-β-D-GlcNAc-(1-4)-D-GlcN through a partial N-acetylation reaction by chitin deacetylase
    • Tokuyasu, K., Ono, H., Mitsutomi, M., Hayashi, K., and Mori, Y. 2000b. Synthesis of a chitosan tetramer derivative, β-D-GlcNAc-(1-4)-β-D-GlcNAc-(1-4)-β-D-GlcNAc-(1-4)-D-GlcN through a partial N-acetylation reaction by chitin deacetylase. Carbohydr Res 325:211-215.
    • (2000) Carbohydr Res , vol.325 , pp. 211-215
    • Tokuyasu, K.1    Ono, H.2    Mitsutomi, M.3    Hayashi, K.4    Mori, Y.5
  • 31
    • 0030731624 scopus 로고    scopus 로고
    • Deacetylation of chitin oligosaccharides of dp 2-4 by chitin deacetylase from Colletotrichum lindemuthianum
    • Tokuyasu, K., Ono, H., Ohnishi-Kameyama, M., Hayashi, K., and Mori, Y. 1997. Deacetylation of chitin oligosaccharides of dp 2-4 by chitin deacetylase from Colletotrichum lindemuthianum. Carbohydr Res 303:353-358.
    • (1997) Carbohydr Res , vol.303 , pp. 353-358
    • Tokuyasu, K.1    Ono, H.2    Ohnishi-Kameyama, M.3    Hayashi, K.4    Mori, Y.5
  • 32
    • 0008363314 scopus 로고    scopus 로고
    • Mode of action of chitin deacetylase from Mucor rouxii on N-acetylchitooligosaccharides
    • Tsigos, I., Zydowicz, N., Martinou, A., Domard, A., and Bouriotis, V. 1999. Mode of action of chitin deacetylase from Mucor rouxii on N-acetylchitooligosaccharides. Eur J Biochem 261:698-705.
    • (1999) Eur J Biochem , vol.261 , pp. 698-705
    • Tsigos, I.1    Zydowicz, N.2    Martinou, A.3    Domard, A.4    Bouriotis, V.5
  • 33
    • 0023137199 scopus 로고
    • Transglycosylation reaction of a chitinase purified from Nocardia orientalis
    • Usui, T., Hayashi, Y., Nanjo, F., Sakai, K., and Ishido, Y. 1987. Transglycosylation reaction of a chitinase purified from Nocardia orientalis. Biochim Biophys Acta 923:302-309.
    • (1987) Biochim Biophys Acta , vol.923 , pp. 302-309
    • Usui, T.1    Hayashi, Y.2    Nanjo, F.3    Sakai, K.4    Ishido, Y.5
  • 34
    • 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
  • 35
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • Vaaje-Kolstad, G., Horn, S. J., van Aalten, D. M., Synstad, B., and Eijsink, V. G. 2005. The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem 280:28492-28497.
    • (2005) J Biol Chem , vol.280 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    Van Aalten, D.M.3    Synstad, B.4    Eijsink, V.G.5
  • 36
    • 0034617218 scopus 로고    scopus 로고
    • The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae
    • Vollmer, W. and Tomasz, A. 2000. The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae. J Biol Chem 275:20496-20501.
    • (2000) J Biol Chem , vol.275 , pp. 20496-20501
    • Vollmer, W.1    Tomasz, A.2
  • 37
    • 0034788748 scopus 로고    scopus 로고
    • Shrimp chitin as substrate for fungal chitin deacetylase
    • Win, N. N. and Stevens, W. F. 2001. Shrimp chitin as substrate for fungal chitin deacetylase. Appl Microbiol Biotechnol 57:334-341.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 334-341
    • Win, N.N.1    Stevens, W.F.2
  • 38
    • 49749137824 scopus 로고    scopus 로고
    • Structural simulation and protein engineering to convert an endo-chitosanase to an exo-chitosanase
    • Yao, Y. Y., Shrestha, K. L., Wu, Y. J. et al. 2008. Structural simulation and protein engineering to convert an endo-chitosanase to an exo-chitosanase. Protein Eng Des Sel 21:561-566.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 561-566
    • Yao, Y.Y.1    Shrestha, K.L.2    Wu, Y.J.3
  • 39
    • 0034279420 scopus 로고    scopus 로고
    • Purification and characterization of chitosanase and exo-β-D-glucosaminidase from a Koji mold, Aspergillus oryzae IAM2660
    • Zhang, X. Y., Dai, A. L., Zhang, X. K. et al. 2000. Purification and characterization of chitosanase and exo-β-D-glucosaminidase from a Koji mold, Aspergillus oryzae IAM2660. Biosci Biotechnol Biochem 64:1896-1902.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1896-1902
    • Zhang, X.Y.1    Dai, A.L.2    Zhang, X.K.3
  • 40
    • 76149085543 scopus 로고    scopus 로고
    • Chitin deacetylases: Properties and applications
    • Zhao, Y., Park, R. D., and Muzzarelli, R. A. A. 2010. Chitin deacetylases: Properties and applications. Marine Drugs 8:24-46.
    • (2010) Marine Drugs , vol.8 , pp. 24-46
    • Zhao, Y.1    Park, R.D.2    Muzzarelli, R.A.A.3


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