메뉴 건너뛰기




Volumn 9, Issue , 2010, Pages

Isolation, characterization and heterologous expression of a novel chitosanase from Janthinobacterium sp. strain 4239

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHITOSANASE; GLYCOSIDASE; BACTERIAL PROTEIN;

EID: 77949541268     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-9-5     Document Type: Article
Times cited : (61)

References (40)
  • 1
    • 0019834317 scopus 로고
    • Purification and mode of action of a chitosanase from Penicillium islandicum
    • Fenton DM, Eveleigh DE. Purification and mode of action of a chitosanase from Penicillium islandicum. J Gen Microbiol 1981, 126:151-165.
    • (1981) J Gen Microbiol , vol.126 , pp. 151-165
    • Fenton, D.M.1    Eveleigh, D.E.2
  • 2
    • 0036308660 scopus 로고    scopus 로고
    • Fungal chitosan production and its characterization
    • 10.1046/j.1472-765X.2002.01118.x, 12081543
    • Pochanavanich P, Suntornsuk W. Fungal chitosan production and its characterization. Lett Appl Microbiol 2002, 35:17-21. 10.1046/j.1472-765X.2002.01118.x, 12081543.
    • (2002) Lett Appl Microbiol , vol.35 , pp. 17-21
    • Pochanavanich, P.1    Suntornsuk, W.2
  • 3
    • 0006889166 scopus 로고
    • Chitosanases: occurrence, production and immobilization
    • New York: Academic Press, Zikakis JP
    • Davis B, Eveleigh DE. Chitosanases: occurrence, production and immobilization. Chitin, Chitosan and Related Enzymes 1984, 161-179. New York: Academic Press, Zikakis JP.
    • (1984) Chitin, Chitosan and Related Enzymes , pp. 161-179
    • Davis, B.1    Eveleigh, D.E.2
  • 4
    • 77249109059 scopus 로고    scopus 로고
    • The relevance of chitin
    • Oxford, United Kingdom: Elsevier Science Ltd, Khor E, First
    • Khor E. The relevance of chitin. Chitin: Fulfilling a biomaterials promise 2001, 1-8. Oxford, United Kingdom: Elsevier Science Ltd, Khor E, First.
    • (2001) Chitin: Fulfilling a biomaterials promise , pp. 1-8
    • Khor, E.1
  • 5
    • 0000568294 scopus 로고
    • Effects of chitosan, pectic acid, lysozyme and chitinase on the growth of several phytopathogens
    • Hirano S, Nagao N. Effects of chitosan, pectic acid, lysozyme and chitinase on the growth of several phytopathogens. Agric Biol Chem 1989, 53:3065-3066.
    • (1989) Agric Biol Chem , vol.53 , pp. 3065-3066
    • Hirano, S.1    Nagao, N.2
  • 6
    • 0021189336 scopus 로고
    • Characterization of the smallest chitosan oligomer that is maximally antifungal to Fusarium solani and elicits pisatin formation in Pisum sativum
    • Kendra DF, Hadwiger LA. Characterization of the smallest chitosan oligomer that is maximally antifungal to Fusarium solani and elicits pisatin formation in Pisum sativum. Exp Mycol 1984, 8:276-281.
    • (1984) Exp Mycol , vol.8 , pp. 276-281
    • Kendra, D.F.1    Hadwiger, L.A.2
  • 7
    • 0023050036 scopus 로고
    • Antitumor effect of hexa-N-Acetylchitogexaose and chitohexose
    • 10.1016/S0008-6215(00)90359-8, 3768901
    • Suzuki K, Mikami T, Okawa Y, Tokoro A, Suzuki S, Suzuki M. Antitumor effect of hexa-N-Acetylchitogexaose and chitohexose. Carbohydr Res 1986, 151:403-408. 10.1016/S0008-6215(00)90359-8, 3768901.
    • (1986) Carbohydr Res , vol.151 , pp. 403-408
    • Suzuki, K.1    Mikami, T.2    Okawa, Y.3    Tokoro, A.4    Suzuki, S.5    Suzuki, M.6
  • 8
    • 0001874785 scopus 로고    scopus 로고
    • Studies on biological effects of water soluble lower homologous oligosaccharides of chitin and chitosan
    • Suzuki S. Studies on biological effects of water soluble lower homologous oligosaccharides of chitin and chitosan. Fragrance J 1996, 15:61-68.
    • (1996) Fragrance J , vol.15 , pp. 61-68
    • Suzuki, S.1
  • 9
    • 0024362928 scopus 로고
    • Protective effects of N-acetylchitohexaose of Listeria monocytogenes infection in mice
    • Tokoro A, Kobayashi M, Tatekawa N, Suzuki S, Suzuki M. Protective effects of N-acetylchitohexaose of Listeria monocytogenes infection in mice. Microbiol Immunol 1989, 33:357-367.
    • (1989) Microbiol Immunol , vol.33 , pp. 357-367
    • Tokoro, A.1    Kobayashi, M.2    Tatekawa, N.3    Suzuki, S.4    Suzuki, M.5
  • 10
    • 0025217197 scopus 로고
    • Antimetastatic and growth-inhibitory effects of N-acetylchitohexaose in mice bearing Lewis lung carcinoma
    • Tsukada K, Matsumoto T, Aizawa K, Tokoro A, Naruse R, Suzuki S, Suzuki M. Antimetastatic and growth-inhibitory effects of N-acetylchitohexaose in mice bearing Lewis lung carcinoma. Jpn J Cancer Res 1990, 81:259-265.
    • (1990) Jpn J Cancer Res , vol.81 , pp. 259-265
    • Tsukada, K.1    Matsumoto, T.2    Aizawa, K.3    Tokoro, A.4    Naruse, R.5    Suzuki, S.6    Suzuki, M.7
  • 11
    • 77949540051 scopus 로고    scopus 로고
    • The glycoside hydrolase family server; Carbohydrate Active enzymes, CAZy
    • The glycoside hydrolase family server; Carbohydrate Active enzymes, CAZy. , http://www.cazy.org/fam/acc_GH.html
  • 12
    • 0031312196 scopus 로고    scopus 로고
    • Chitosanase from Streptomyces sp. strain N174: a comparative review of its structure and function
    • Fukamizo T, Brzezinski R. Chitosanase from Streptomyces sp. strain N174: a comparative review of its structure and function. Biochem Cell Biol, Biochimie et Biologie Cellulaire 1997, 75:687-696.
    • (1997) Biochem Cell Biol, Biochimie et Biologie Cellulaire , vol.75 , pp. 687-696
    • Fukamizo, T.1    Brzezinski, R.2
  • 13
    • 0032928871 scopus 로고    scopus 로고
    • Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization
    • Honda Y, Fukamizo T, Okajima T, Goto S, Boucher I, Brzezinski R. Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. Biochim Biophys Acta 1999, 1429:365-376.
    • (1999) Biochim Biophys Acta , vol.1429 , pp. 365-376
    • Honda, Y.1    Fukamizo, T.2    Okajima, T.3    Goto, S.4    Boucher, I.5    Brzezinski, R.6
  • 15
    • 0032695475 scopus 로고    scopus 로고
    • Crystal structure of chitosanase from Bacillus circulans MH-K1 at, 1.6-Å resolution and its substrate recognition mechanism
    • 10.1074/jbc.274.43.30818, 10521473
    • Saito J-I, Kita A, Higuchi Y, Nagata Y, Ando A, Miki K. Crystal structure of chitosanase from Bacillus circulans MH-K1 at, 1.6-Å resolution and its substrate recognition mechanism. J Biol Chem 1999, 274:30818-30825. 10.1074/jbc.274.43.30818, 10521473.
    • (1999) J Biol Chem , vol.274 , pp. 30818-30825
    • Saito, J.-.I.1    Kita, A.2    Higuchi, Y.3    Nagata, Y.4    Ando, A.5    Miki, K.6
  • 16
    • 0028796234 scopus 로고
    • Production of two chitosanases from a chitosan-assimilating bacterium, Acinetobacter sp. strain CHB101
    • 1388345, 16534927
    • Shimosaka M, Nogawa M, Wang XY, Kumehara M, Okazaki M. Production of two chitosanases from a chitosan-assimilating bacterium, Acinetobacter sp. strain CHB101. Appl Environ Microbiol 1995, 61:438-442. 1388345, 16534927.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 438-442
    • Shimosaka, M.1    Nogawa, M.2    Wang, X.Y.3    Kumehara, M.4    Okazaki, M.5
  • 17
    • 0028341631 scopus 로고
    • Purification and characterization of an extracellular chitosanase produced by Amycolatopsis sp. CsO-2
    • Okajima S, Ando A, Shinoyama H, Fujii T. Purification and characterization of an extracellular chitosanase produced by Amycolatopsis sp. CsO-2. J Ferment Bioeng 1994, 77:617-620.
    • (1994) J Ferment Bioeng , vol.77 , pp. 617-620
    • Okajima, S.1    Ando, A.2    Shinoyama, H.3    Fujii, T.4
  • 18
    • 43049117464 scopus 로고    scopus 로고
    • Purification and characterization of a chitosanase from Serratia marcescens TKU011
    • 10.1016/j.carres.2008.03.030, 18420186
    • Wang SL, Peng JH, Liang TW, Liu KC. Purification and characterization of a chitosanase from Serratia marcescens TKU011. Carbohydr Res 2008, 343:1316-1323. 10.1016/j.carres.2008.03.030, 18420186.
    • (2008) Carbohydr Res , vol.343 , pp. 1316-1323
    • Wang, S.L.1    Peng, J.H.2    Liang, T.W.3    Liu, K.C.4
  • 20
    • 0028786960 scopus 로고
    • A new chitosanase gene from a Nocardioides sp. is a third member of glycosyl hydrolase family 46
    • 10.1099/13500872-141-10-2629, 7582023
    • Masson JY, Boucher I, Neugebauer WA, Ramotar D, Brzezinski R. A new chitosanase gene from a Nocardioides sp. is a third member of glycosyl hydrolase family 46. Microbiology 1995, 141:2629-2635. 10.1099/13500872-141-10-2629, 7582023.
    • (1995) Microbiology , vol.141 , pp. 2629-2635
    • Masson, J.Y.1    Boucher, I.2    Neugebauer, W.A.3    Ramotar, D.4    Brzezinski, R.5
  • 21
    • 34447126483 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of a chitosanase from Microbacterium sp
    • 10.1007/s10529-007-9373-y, 17563859
    • Zhang J, Sun Y. Molecular cloning, expression and characterization of a chitosanase from Microbacterium sp. Biotechnol Lett 2007, 29:1221-1225. 10.1007/s10529-007-9373-y, 17563859.
    • (2007) Biotechnol Lett , vol.29 , pp. 1221-1225
    • Zhang, J.1    Sun, Y.2
  • 22
    • 51249116887 scopus 로고    scopus 로고
    • Characterization of a novel fungal chitosanase Csn2 from Gongronella sp. JG
    • 10.1016/j.carres.2008.08.004, 18722595
    • Wang J, Zhou W, Yuan H, Wang Y. Characterization of a novel fungal chitosanase Csn2 from Gongronella sp. JG. Carbohydr Res 2008, 343:2583-2588. 10.1016/j.carres.2008.08.004, 18722595.
    • (2008) Carbohydr Res , vol.343 , pp. 2583-2588
    • Wang, J.1    Zhou, W.2    Yuan, H.3    Wang, Y.4
  • 23
    • 0034279420 scopus 로고    scopus 로고
    • Purification and characterization of chitosanase and exo-ß-D-glucosaminidase from a koji mold, Aspergillus oryzae IAM 2660
    • 10.1271/bbb.64.1896, 11055393
    • Zhang XY, Dai AL, Zhang XK, Kuroiwa K, Kodaira R, Shimosaka M, Okazaki M. Purification and characterization of chitosanase and exo-ß-D-glucosaminidase from a koji mold, Aspergillus oryzae IAM 2660. Biosci Biotechnol Biochem 2000, 64:1896-1902. 10.1271/bbb.64.1896, 11055393.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1896-1902
    • Zhang, X.Y.1    Dai, A.L.2    Zhang, X.K.3    Kuroiwa, K.4    Kodaira, R.5    Shimosaka, M.6    Okazaki, M.7
  • 24
    • 0030471612 scopus 로고    scopus 로고
    • Cloning and characterization of a chitosanase gene from the plant pathogenic fungus, Fusarium solani
    • Shimosaka M, Kumehara M, Zhang X-Y, Nogawa M, Okazaki M. Cloning and characterization of a chitosanase gene from the plant pathogenic fungus, Fusarium solani. J Ferment Bioeng 1996, 82:426-431.
    • (1996) J Ferment Bioeng , vol.82 , pp. 426-431
    • Shimosaka, M.1    Kumehara, M.2    Zhang, X.-.Y.3    Nogawa, M.4    Okazaki, M.5
  • 25
    • 11244281032 scopus 로고    scopus 로고
    • Chitosan-based particles as controlled drug delivery systems
    • 10.1080/10717540590889781, 15801720
    • Prabaharan M, Mano JF. Chitosan-based particles as controlled drug delivery systems. Drug Deliv 2005, 12:41-57. 10.1080/10717540590889781, 15801720.
    • (2005) Drug Deliv , vol.12 , pp. 41-57
    • Prabaharan, M.1    Mano, J.F.2
  • 26
    • 39549096259 scopus 로고    scopus 로고
    • Improved transfection efficiency of CS/DNA complex by co-transfected chitosanase gene
    • 10.1016/j.ijpharm.2007.10.042, 18065172
    • Zuo A, Sun P, Liang D, Liu W, Zhao R, Guo G, Cheng N, Zhang J, Yao K. Improved transfection efficiency of CS/DNA complex by co-transfected chitosanase gene. Int J Pharm 2008, 352:302-308. 10.1016/j.ijpharm.2007.10.042, 18065172.
    • (2008) Int J Pharm , vol.352 , pp. 302-308
    • Zuo, A.1    Sun, P.2    Liang, D.3    Liu, W.4    Zhao, R.5    Guo, G.6    Cheng, N.7    Zhang, J.8    Yao, K.9
  • 27
    • 0029150686 scopus 로고
    • Cloning and sequencing of a gene encoding the 69-kDa extracellular chitinase of Janthinobacterium lividum
    • 10.1111/j.1574-6968.1995.tb07788.x, 7557339
    • Gleave AP, Taylor RK, Morris BA, Greenwood DR. Cloning and sequencing of a gene encoding the 69-kDa extracellular chitinase of Janthinobacterium lividum. FEMS Microbiol Lett 1995, 131:279-288. 10.1111/j.1574-6968.1995.tb07788.x, 7557339.
    • (1995) FEMS Microbiol Lett , vol.131 , pp. 279-288
    • Gleave, A.P.1    Taylor, R.K.2    Morris, B.A.3    Greenwood, D.R.4
  • 28
    • 29144490893 scopus 로고    scopus 로고
    • Chitinase genes in lake sediments of Ardley Island, Antarctica
    • 10.1128/AEM.71.12.7904-7909.2005, 1317360, 16332766
    • Xiao X, Yin X, Lin J, Sun L, You Z, Wang P, Wang F. Chitinase genes in lake sediments of Ardley Island, Antarctica. Appl Environ Microbiol 2005, 71:7904-7909. 10.1128/AEM.71.12.7904-7909.2005, 1317360, 16332766.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 7904-7909
    • Xiao, X.1    Yin, X.2    Lin, J.3    Sun, L.4    You, Z.5    Wang, P.6    Wang, F.7
  • 30
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur J. A procedure for the isolation of deoxyribonucleic acid from microorganisms. J Mol Biol 1961, 3:208-218.
    • (1961) J Mol Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 31
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • 10.1093/nar/25.17.3389, 146917, 9254694
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25:3389-3402. 10.1093/nar/25.17.3389, 146917, 9254694.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 32
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • 10.1093/nar/25.24.4876, 147148, 9396791
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25:4876-4882. 10.1093/nar/25.24.4876, 147148, 9396791.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 33
    • 3042521098 scopus 로고    scopus 로고
    • Improved Prediction of Signal Peptides: SignalP 3.0
    • 10.1016/j.jmb.2004.05.028, 15223320
    • Bendtsen JD, Nielsen H, von Heijne G, Brunak S. Improved Prediction of Signal Peptides: SignalP 3.0. J Mol Biol 2004, 340:783-795. 10.1016/j.jmb.2004.05.028, 15223320.
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 34
    • 0035934280 scopus 로고    scopus 로고
    • ProBA complementation of an auxotrophic E. coli strain improves plasmid stability and expression yield during fermenter production of a recombinant antibody fragment
    • 10.1016/S0378-1119(01)00629-1, 11675003
    • Fiedler M, Skerra A. proBA complementation of an auxotrophic E. coli strain improves plasmid stability and expression yield during fermenter production of a recombinant antibody fragment. Gene 2001, 274:111-118. 10.1016/S0378-1119(01)00629-1, 11675003.
    • (2001) Gene , vol.274 , pp. 111-118
    • Fiedler, M.1    Skerra, A.2
  • 35
    • 0028555357 scopus 로고
    • Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli
    • 10.1016/0378-1119(94)90643-2, 7828861
    • Skerra A. Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene 1994, 151:131-135. 10.1016/0378-1119(94)90643-2, 7828861.
    • (1994) Gene , vol.151 , pp. 131-135
    • Skerra, A.1
  • 36
    • 55949102415 scopus 로고    scopus 로고
    • Flavobacterium sp. strain 4221 and Pedobacter sp. strain 4236 beta-1,3-glucanases that are active at low temperatures
    • Rasmussen MA, Madsen SM, Stougaard P, Johnsen MG. Flavobacterium sp. strain 4221 and Pedobacter sp. strain 4236 beta-1,3-glucanases that are active at low temperatures. Appl Environ Microbiol 2008, 22:7070-7072.
    • (2008) Appl Environ Microbiol , vol.22 , pp. 7070-7072
    • Rasmussen, M.A.1    Madsen, S.M.2    Stougaard, P.3    Johnsen, M.G.4
  • 37
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto T, Yagishita K. A simple activity measurement of lysozyme. Agric Biol Chem 1971, 35:1154-1156.
    • (1971) Agric Biol Chem , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 38
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • London, Academic Press, Purich DL
    • Keith KJ, Morrison JF. Buffers of constant ionic strength for studying pH-dependent processes. Methods in enzymology, vol 87 1982, 405-426. London, Academic Press, Purich DL.
    • (1982) Methods in enzymology, vol 87 , pp. 405-426
    • Keith, K.J.1    Morrison, J.F.2
  • 39
    • 0019135876 scopus 로고
    • Studies on the damage to Escherichia coli cell membrane caused by different rates of freeze-thawing
    • 10.1016/0005-2736(80)90387-9, 7004488
    • Souzu H. Studies on the damage to Escherichia coli cell membrane caused by different rates of freeze-thawing. Biochim Biophys Acta 1980, 603:13-26. 10.1016/0005-2736(80)90387-9, 7004488.
    • (1980) Biochim Biophys Acta , vol.603 , pp. 13-26
    • Souzu, H.1
  • 40
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • 10.1016/0378-1119(85)90120-9, 2985470
    • Yanisch-Perron C, Vieira J, Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 1985, 33:103-119. 10.1016/0378-1119(85)90120-9, 2985470.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.