메뉴 건너뛰기




Volumn 63, Issue 4, 2004, Pages 398-406

A chitinase with high activity toward partially N-acetylated chitosan from a new, moderately thermophilic, chitin-degrading bacterium, Ralstonia sp. A-471

Author keywords

[No Author keywords available]

Indexed keywords

ALANYLASPARTYLPROLYLTYROSYLLEUCYLLYSYLVALYLALANYLTYROSYLTYROSYLPROLINE; AMINO ACID DERIVATIVE; CALCIUM ION; CHITIN; CHITINASE; CHITOSAN; COPPER ION; GLYCOSIDASE; ISOENZYME; MAGNESIUM ION; MANGANESE; OLIGOSACCHARIDE; PEPTIDE DERIVATIVE; RIBOSOME DNA; UNCLASSIFIED DRUG;

EID: 1642537660     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-003-1351-2     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 9444272215 scopus 로고    scopus 로고
    • Three chitinase genes (chiA, chiC, and chiD) comprise the chitinase system of Bacillus circulans WL-12
    • Alam MM, Mizutani T, Isono M, Nikaidou N, Watanabe T (1996) Three chitinase genes (chiA, chiC, and chiD) comprise the chitinase system of Bacillus circulans WL-12. J Ferment Bioeng 82:28-36
    • (1996) J Ferment Bioeng , vol.82 , pp. 28-36
    • Alam, M.M.1    Mizutani, T.2    Isono, M.3    Nikaidou, N.4    Watanabe, T.5
  • 2
    • 0028316274 scopus 로고
    • Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12
    • Armand S, Tomita H, Heyraud A, Gey C, Watanabe T, Henrissat B (1994) Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12. FEES Lett 343:177-180
    • (1994) FEES Lett , vol.343 , pp. 177-180
    • Armand, S.1    Tomita, H.2    Heyraud, A.3    Gey, C.4    Watanabe, T.5    Henrissat, B.6
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0023774771 scopus 로고
    • Genetic analysis of extracellular proteins of Serratia marcescens
    • Hines DA, Saurugger PN, Ihler GM, Benedik MJ (1988) Genetic analysis of extracellular proteins of Serratia marcescens. J Bacteriol 170:4141-4146
    • (1988) J Bacteriol , vol.170 , pp. 4141-4146
    • Hines, D.A.1    Saurugger, P.N.2    Ihler, G.M.3    Benedik, M.J.4
  • 7
    • 0000568294 scopus 로고
    • Effects of chitosan, pectic acid, lysozyme, and chitinase on the growth of several phytopathogens
    • Hirano S, Nagao N (1989) Effects of chitosan, pectic acid, lysozyme, and chitinase on the growth of several phytopathogens. Agric Biol Chem 53:3065-3066
    • (1989) Agric Biol Chem , vol.53 , pp. 3065-3066
    • Hirano, S.1    Nagao, N.2
  • 8
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto T, Yagishita K (1971) A simple activity measurement of lysozyme. Agric Biol Chem 35:1154-1156
    • (1971) Agric Biol Chem , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 10
    • 0001199167 scopus 로고    scopus 로고
    • HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme
    • Koga D, Yoshioka T, 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
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0029270304 scopus 로고
    • The action of Bacillus circulans WL-12 chitinases on partially N-acetylated chitosan
    • Mitsutomi M, Kidoh H, Tomita H, 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
  • 15
    • 0001039236 scopus 로고    scopus 로고
    • Action patterns of microbial chitinases and chitosanases on partially N-acetylated chitosan
    • Mitsutomi M, Ueda M, Arai M, Ando A, Watanabe T (1996) Action patterns of microbial chitinases and chitosanases on partially N-acetylated chitosan. Chitin Enzymol 2:273-284
    • (1996) Chitin Enzymol , vol.2 , pp. 273-284
    • Mitsutomi, M.1    Ueda, M.2    Arai, M.3    Ando, A.4    Watanabe, T.5
  • 16
    • 0033288483 scopus 로고    scopus 로고
    • Native, industrial and fossil chitins
    • Jolles P and Muzzareli RAA (eds). Birkhauser, Basel
    • Muzzarelli RAA (1999) Native, industrial and fossil chitins. In: Jolles P and Muzzareli RAA (eds) Chitin and chitinases. Birkhauser, Basel, pp 1-6
    • (1999) Chitin and Chitinases , pp. 1-6
    • Muzzarelli, R.A.A.1
  • 17
    • 0023901367 scopus 로고
    • Cloning and expression of Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli
    • Robbins PW, Albright C, Benfield B (1988) Cloning and expression of Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli J Biol Chem 263:443-447
    • (1988) J Biol Chem , vol.263 , pp. 443-447
    • Robbins, P.W.1    Albright, C.2    Benfield, B.3
  • 18
    • 0020392369 scopus 로고
    • Serratia marcescens chitinases: One-step purification and use for the determination of chitin
    • Roberts RL, Cabib E (1982) Serratia marcescens chitinases: one-step purification and use for the determination of chitin. Anal Biochem 127:402-412
    • (1982) Anal Biochem , vol.127 , pp. 402-412
    • Roberts, R.L.1    Cabib, E.2
  • 20
    • 77957071226 scopus 로고
    • Preparation of crustacean chitin
    • Shimahara K, Takiguchi Y (1988) Preparation of crustacean chitin. Methods Enzymol 161:417-423
    • (1988) Methods Enzymol , vol.161 , pp. 417-423
    • Shimahara, K.1    Takiguchi, Y.2
  • 21
    • 0030019860 scopus 로고    scopus 로고
    • Cloning of a cluster of chitinase genes from Aeromonas sp. no. 10S-24
    • Shiro M, Ueda M, Kawaguchi T, Arai M (1996) Cloning of a cluster of chitinase genes from Aeromonas sp. no. 10S-24. Biochim Biophys Acta 1305:44-48
    • (1996) Biochim Biophys Acta , vol.1305 , pp. 44-48
    • Shiro, M.1    Ueda, M.2    Kawaguchi, T.3    Arai, M.4
  • 22
    • 0034913834 scopus 로고    scopus 로고
    • Expression of a gene encoding chitinase (pCA8 ORF) from Aeromonas sp. no. 10S-24 in Escherichia coli and enzyme characterization
    • Sutrisno A, Ueda M, Inui H, Kawaguchi T, Nakano Y, Arai M, Miyatake K (2001) Expression of a gene encoding chitinase (pCA8 ORF) from Aeromonas sp. no. 10S-24 in Escherichia coli and enzyme characterization. J Biosci Bioeng 91:599-602
    • (2001) J Biosci Bioeng , vol.91 , pp. 599-602
    • Sutrisno, A.1    Ueda, M.2    Inui, H.3    Kawaguchi, T.4    Nakano, Y.5    Arai, M.6    Miyatake, K.7
  • 23
    • 0021796977 scopus 로고
    • Enhancing effects of N-acetyl chitooligosaccharides on the active oxygen-generating and microbial activities of peritoneal exudates cells in mice
    • Tokyo
    • Suzuki K, Tokoro A, Okawa Y, Suzuki S, Suzuki M (1985) Enhancing effects of N-acetyl chitooligosaccharides on the active oxygen-generating and microbial activities of peritoneal exudates cells in mice. Chem Pharm Bull (Tokyo) 33:886-888
    • (1985) Chem Pharm Bull , vol.33 , pp. 886-888
    • Suzuki, K.1    Tokoro, A.2    Okawa, Y.3    Suzuki, S.4    Suzuki, M.5
  • 24
    • 0032728411 scopus 로고    scopus 로고
    • A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • Tanaka T, Fujiwara S, Nishikori S, Fukui T, Takagi M, Imanaka T (1999) A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1. Appl Environ Microbiol 65:5338-5344
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5338-5344
    • Tanaka, T.1    Fujiwara, S.2    Nishikori, S.3    Fukui, T.4    Takagi, M.5    Imanaka, T.6
  • 25
    • 0023930633 scopus 로고
    • Growth-inhibitory effect of hexa-N-acetylchitohexaose and chitohexaose against meth-A solid tumor
    • Tokyo
    • Tokoro A, Tatewaki N, Suzuki K, Mikami T, Suzuki S, Suzuki M (1988) Growth-inhibitory effect of hexa-N-acetylchitohexaose and chitohexaose against meth-A solid tumor. Chem Pharm Bull (Tokyo) 36:784-790
    • (1988) Chem Pharm Bull , vol.36 , pp. 784-790
    • Tokoro, A.1    Tatewaki, N.2    Suzuki, K.3    Mikami, T.4    Suzuki, S.5    Suzuki, M.6
  • 26
    • 0033630884 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520 and cloning of the encoding gene
    • Tsujibo H, Hatano N, Endo H, Miyamoto K, Inamori Y (2000) Purification and characterization of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520 and cloning of the encoding gene. Biosci Biotechnol Biochem 64:96-102
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 96-102
    • Tsujibo, H.1    Hatano, N.2    Endo, H.3    Miyamoto, K.4    Inamori, Y.5
  • 27
    • 84950927639 scopus 로고
    • Purification and some properties of chitinases from Aeromonas sp. no. 10S-24
    • Ueda M, Arai M (1992) Purification and some properties of chitinases from Aeromonas sp. no. 10S-24. Biosci Biotechnol Biochem 56:460-464
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 460-464
    • Ueda, M.1    Arai, M.2
  • 28
    • 0029398751 scopus 로고
    • Purification and some properties of six chitinases from Aeromonas sp. no. 10S-24
    • Ueda M, Fujiwara A, Kawaguchi T, Arai M (1995) Purification and some properties of six chitinases from Aeromonas sp. no. 10S-24. Biosci Biotechnol Biochem 59:2162-2164
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 2162-2164
    • Ueda, M.1    Fujiwara, A.2    Kawaguchi, T.3    Arai, M.4
  • 29
    • 0025314392 scopus 로고
    • Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation
    • Watanabe T, Oyanagi W, Suzuki K, Tanaka H (1990) Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J Bacteriol 172:4017-4022
    • (1990) J Bacteriol , vol.172 , pp. 4017-4022
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Tanaka, H.4
  • 30
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase Al of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe T, Kobori K, Miyashita K, Fujii T, Sakai H, Uchida M, Tanaka H (1993) Identification of glutamic acid 204 and aspartic acid 200 in chitinase Al of Bacillus circulans WL-12 as essential residues for chitinase activity. J Biol Chem 268:18567-18572
    • (1993) J Biol Chem , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 33
    • 0028850433 scopus 로고
    • Transfer of two Burkholderia and an Alcaligenes species to Ralstonia gen. Nov.: Proposal of Ralstonia picketti (Ralston, Palleroni and Doudoroff 1973) comb. Nov., Ralstonia solanacearum (Smith 1896) comb. Nov., and Ralstonia eutropha (Davis 1969) comb. Nov
    • Yabuuchi E, Kosako Y, Yano I, Hotta H, Nishiuchi Y (1995) Transfer of two Burkholderia and an Alcaligenes species to Ralstonia gen. Nov.: proposal of Ralstonia picketti (Ralston, Palleroni and Doudoroff 1973) comb. Nov., Ralstonia solanacearum (Smith 1896) comb. Nov., and Ralstonia eutropha (Davis 1969) comb. Nov. Microbiol Immunol. 39:897-904
    • (1995) Microbiol Immunol. , vol.39 , pp. 897-904
    • Yabuuchi, E.1    Kosako, Y.2    Yano, I.3    Hotta, H.4    Nishiuchi, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.