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Volumn 65, Issue 2, 2009, Pages 244-250

Purification and properties of a chitinase from Penicillium sp. LYG 0704

Author keywords

Chitinase; Gene cloning; Penicillium sp.; Purification; RACE PCR

Indexed keywords

2 PROPANOL; CHITINASE; HYBRID PROTEIN;

EID: 61749102862     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.12.004     Document Type: Article
Times cited : (68)

References (29)
  • 1
    • 0000759564 scopus 로고
    • Physiology of microbiol degradation of chitin and chitosan
    • Gooday G.W. Physiology of microbiol degradation of chitin and chitosan. Biodegradation 1 (1994) 177-190
    • (1994) Biodegradation , vol.1 , pp. 177-190
    • Gooday, G.W.1
  • 2
    • 36249003867 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio cholerae: characterization of a unique chitin oligosaccharide deacetylase
    • Li X., Wang L.X., Wang X., and Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio cholerae: characterization of a unique chitin oligosaccharide deacetylase. Glycobiology 17 (2007) 1377-1387
    • (2007) Glycobiology , vol.17 , pp. 1377-1387
    • Li, X.1    Wang, L.X.2    Wang, X.3    Roseman, S.4
  • 3
    • 0030019860 scopus 로고    scopus 로고
    • Cloning of a cluster of chitinase genes from Aeromonas sp. no. 10S-24
    • Shiro M., Ueda M., Kawaguchi T., and Arai M. Cloning of a cluster of chitinase genes from Aeromonas sp. no. 10S-24. Biochim. Biophys. Acta 1305 (1996) 44-48
    • (1996) Biochim. Biophys. Acta , vol.1305 , pp. 44-48
    • Shiro, M.1    Ueda, M.2    Kawaguchi, T.3    Arai, M.4
  • 4
    • 0000269710 scopus 로고
    • The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular-weight substrates for lysozyme
    • Rupley J.A. The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular-weight substrates for lysozyme. Biochim. Biophys. Acta 83 (1964) 245-255
    • (1964) Biochim. Biophys. Acta , vol.83 , pp. 245-255
    • Rupley, J.A.1
  • 5
    • 0037123211 scopus 로고    scopus 로고
    • Production of N-acetyl-d-glucosamine from α-chitin by crude enzymes from Areomonas hydrophila H-2330
    • Muraki E., Hiraga K., Oda K., and Aiba S. Production of N-acetyl-d-glucosamine from α-chitin by crude enzymes from Areomonas hydrophila H-2330. Carbohydr. Res. 337 (2002) 761-763
    • (2002) Carbohydr. Res. , vol.337 , pp. 761-763
    • Muraki, E.1    Hiraga, K.2    Oda, K.3    Aiba, S.4
  • 7
    • 0035929579 scopus 로고    scopus 로고
    • Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka T., Fukui T., and Imanaka T. Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 276 (2001) 35629-35635
    • (2001) J. Biol. Chem. , vol.276 , pp. 35629-35635
    • Tanaka, T.1    Fukui, T.2    Imanaka, T.3
  • 8
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 (1991) 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 9
    • 0029835188 scopus 로고    scopus 로고
    • A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037
    • Ohno T., Armand S., Hata T., Mikaidou N., Henrissat B., Mitsutomi M., and Watanabe T. A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037. J. Bacteriol. 178 (1996) 5065-5070
    • (1996) J. Bacteriol. , vol.178 , pp. 5065-5070
    • Ohno, T.1    Armand, S.2    Hata, T.3    Mikaidou, N.4    Henrissat, B.5    Mitsutomi, M.6    Watanabe, T.7
  • 11
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Terwisscha van Scheltinga A.C., Kalk K.H., Beintema J.J., and Dijkstra B.W. Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 2 (1994) 1181-1189
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Terwisscha van Scheltinga, A.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 12
    • 0033014645 scopus 로고    scopus 로고
    • Analysis of fungal diversity in the wheat rhizosphere by sequencing of cloned PCR-amplified genes encoding 18S rRNA and temperature gradient gel electrophoresis
    • Smit E., Leeflang P., Glandorf B., Van Elsas J.D., and Wernars K. Analysis of fungal diversity in the wheat rhizosphere by sequencing of cloned PCR-amplified genes encoding 18S rRNA and temperature gradient gel electrophoresis. Appl. Environ. Microbiol. 65 (1999) 2614-2621
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2614-2621
    • Smit, E.1    Leeflang, P.2    Glandorf, B.3    Van Elsas, J.D.4    Wernars, K.5
  • 13
    • 0034791387 scopus 로고    scopus 로고
    • Multiplex PCR using internal transcribed spacer 1 and 2 regions for rapid detection and identification of yeast strains
    • Fujita S.-I., Senda Y., Nakaguchi S., and Hashimoto T. Multiplex PCR using internal transcribed spacer 1 and 2 regions for rapid detection and identification of yeast strains. J. Clin. Microbiol. 39 (2001) 3617-3622
    • (2001) J. Clin. Microbiol. , vol.39 , pp. 3617-3622
    • Fujita, S.-I.1    Senda, Y.2    Nakaguchi, S.3    Hashimoto, T.4
  • 14
    • 0016632309 scopus 로고
    • Powdered chitin agar as a selective medium for enumeration of actinomycetes in water and soil
    • Hsu S.C., and Lockwood J.L. Powdered chitin agar as a selective medium for enumeration of actinomycetes in water and soil. Appl. Microbiol. 29 (1975) 422-426
    • (1975) Appl. Microbiol. , vol.29 , pp. 422-426
    • Hsu, S.C.1    Lockwood, J.L.2
  • 15
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0010612922 scopus 로고
    • Purification and characterization of a chitinase from the hyperparasitic fungus Aphanocladium album
    • Kunz C., Sellam O., and Bertheau Y. Purification and characterization of a chitinase from the hyperparasitic fungus Aphanocladium album. Physiol. Mol. Plant Pathol. 40 (1992) 117-131
    • (1992) Physiol. Mol. Plant Pathol. , vol.40 , pp. 117-131
    • Kunz, C.1    Sellam, O.2    Bertheau, Y.3
  • 19
    • 0026832966 scopus 로고
    • Purification and some properties of the extracellular chitinase produced by Trichoderma harzianum
    • Ulhoa C.J., and Peberdy J.F. Purification and some properties of the extracellular chitinase produced by Trichoderma harzianum. Enzyme Microb. Technol. 14 (1992) 236-241
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 236-241
    • Ulhoa, C.J.1    Peberdy, J.F.2
  • 20
    • 0000439771 scopus 로고
    • Endochitinase from Gliocladium virens: isolation, characterization, and synergistic antifungal activity in combination with gliotoxin
    • di Pietro A., Lorito M., Hayes C.K., Broadway R.M., and Harman G.E. Endochitinase from Gliocladium virens: isolation, characterization, and synergistic antifungal activity in combination with gliotoxin. Phytopathology 83 (1993) 308-313
    • (1993) Phytopathology , vol.83 , pp. 308-313
    • di Pietro, A.1    Lorito, M.2    Hayes, C.K.3    Broadway, R.M.4    Harman, G.E.5
  • 22
    • 1942472042 scopus 로고    scopus 로고
    • Purification and partial characterization of a chitinase from the mycoparasitic fungus Trichothecium roseum
    • Li D.-C., Zhang S.-H., Liu K.-Q., and Lu J. Purification and partial characterization of a chitinase from the mycoparasitic fungus Trichothecium roseum. J. Gen. Appl. Microbiol. 50 (2004) 35-39
    • (2004) J. Gen. Appl. Microbiol. , vol.50 , pp. 35-39
    • Li, D.-C.1    Zhang, S.-H.2    Liu, K.-Q.3    Lu, J.4
  • 23
    • 18344387205 scopus 로고    scopus 로고
    • Purification and partial characterization of two chitinase from the mycoparasitic fungus Talaromyces flavus
    • Li D.-C., Chen S., and Lu J. Purification and partial characterization of two chitinase from the mycoparasitic fungus Talaromyces flavus. Mycopathologia 159 (2005) 223-229
    • (2005) Mycopathologia , vol.159 , pp. 223-229
    • Li, D.-C.1    Chen, S.2    Lu, J.3
  • 25
    • 0032478045 scopus 로고    scopus 로고
    • The purification and characterization of a Trichoderma harzianum exochitinase
    • Deane E.E., Whipps J.M., Lynch J.M., and Peberdy J.F. The purification and characterization of a Trichoderma harzianum exochitinase. Biochim. Biophys. Acta 1383 (1998) 101-110
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 101-110
    • Deane, E.E.1    Whipps, J.M.2    Lynch, J.M.3    Peberdy, J.F.4
  • 26
    • 0029880644 scopus 로고    scopus 로고
    • Purification and characteristics of cytosolic chitinase from Piromyces communis OTS1
    • Sakurada M., Morgavi D.P., Komatani K., Tomita T., and Onodera R. Purification and characteristics of cytosolic chitinase from Piromyces communis OTS1. FEMS Microbiol. Lett. 137 (1996) 75-78
    • (1996) FEMS Microbiol. Lett. , vol.137 , pp. 75-78
    • Sakurada, M.1    Morgavi, D.P.2    Komatani, K.3    Tomita, T.4    Onodera, R.5
  • 27
    • 0035720520 scopus 로고    scopus 로고
    • The chitinolytic activity of Penicillium janthinellum P9: purification, partial characterization and potential applications
    • di Giambattista R., Federici F., Petruccioli M., and Fenice M. The chitinolytic activity of Penicillium janthinellum P9: purification, partial characterization and potential applications. J. Appl. Microbiol. 91 (2001) 498-505
    • (2001) J. Appl. Microbiol. , vol.91 , pp. 498-505
    • di Giambattista, R.1    Federici, F.2    Petruccioli, M.3    Fenice, M.4
  • 28
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: their involvement in morphogenesis and host-parasite interaction
    • Sahai A.S., and Manocha M.S. Chitinases of fungi and plants: their involvement in morphogenesis and host-parasite interaction. FEMS Microbio. Rev. 11 (1993) 317-338
    • (1993) FEMS Microbio. Rev. , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 29
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C., Bissery V., Benchetrit T., and Mornon J.P. Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 224 (1987) 149-155
    • (1987) FEBS Lett. , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.