메뉴 건너뛰기




Volumn 66, Issue 5, 2002, Pages 1075-1083

Chitinases a, b, and c1 of serratia marcescens 2170 produced by recombinant escherichia coli: Enzymatic properties and synergism on chitin degradation

Author keywords

Chitinase; Serratia marcescens; Synergism

Indexed keywords

CHITIN; CHITINASE; ISOENZYME; OLIGOSACCHARIDE; RECOMBINANT PROTEIN;

EID: 0036562588     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.1075     Document Type: Article
Times cited : (175)

References (33)
  • 1
    • 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, 309-316 (1991).
    • (1991) Biochem.J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 0029835188 scopus 로고    scopus 로고
    • A modular family 19 chitinase found in the prokaryotic organismStreptomyces griseusHUT 6037
    • Ohno, T., Armand, S., Hata, T., Nikaidou, N., Henrissat, B., Mitsutomi, M., and Watanabe, T., A modular family 19 chitinase found in the prokaryotic organismStreptomyces griseusHUT 6037.J. Bac-teriol,178, 5065-5070 (1996).
    • (1996) J. Bac-Teriol , vol.178 , pp. 5065-5070
    • Ohno, T.1    Armand, S.2    Hata, T.3    Nikaidou, N.4    Henrissat, B.5    Mitsutomi, M.6    Watanabe, T.7
  • 4
    • 0035116215 scopus 로고    scopus 로고
    • The bacteriumBurkholderia gladiolistrain CHB101 produces two different kinds of chitinases belonging to families 18 and 19 of the glycosyl hydrolases
    • Shimosaka, M., Fukumori, Y., Narita, T., Zhang, X., Kodaira, R., Nogawa, M., and Okazaki, M., The bacteriumBurkholderia gladiolistrain CHB101 produces two different kinds of chitinases belonging to families 18 and 19 of the glycosyl hydrolases.J. Biosci. Bioeng.,91, 103-105 (2001).
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 103-105
    • Shimosaka, M.1    Fukumori, Y.2    Narita, T.3    Zhang, X.4    Kodaira, R.5    Nogawa, M.6    Okazaki, M.7
  • 6
    • 0024316572 scopus 로고
    • Nucleotide sequence of the chitinase B gene ofSerratia marcescensQMB1466
    • Harpster, M. H. and Dunsmuir, P., Nucleotide sequence of the chitinase B gene ofSerratia marcescensQMB1466.Nucleic Acids Res.,17, 5395 (1989).
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5395
    • Harpster, M.H.1    Dunsmuir, P.2
  • 7
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes fromSerratia marcescens
    • Jones, J. D. G., Grady, K. L., Suslow, T. V., and Bedbrook, J. R., Isolation and characterization of genes encoding two chitinase enzymes fromSerratia marcescens. EMBOJ., 5, 467-473 (1986).
    • (1986) EMBO , vol.5 , pp. 467-473
    • Jones, J.D.G.1    Grady, K.L.2    Suslow, T.V.3    Bedbrook, J.R.4
  • 8
    • 0028815373 scopus 로고
    • Chitinase B fromSerratia marcescensBJL200 is exported to the periplasm without processing
    • Brurberg, M. B., Eijsink, V. G., Haandrikman, A. J., Venema, G., and Nes, I. F., Chitinase B fromSerratia marcescensBJL200 is exported to the periplasm without processing.Microbiology, 141, 123-131 (1995).
    • (1995) Microbiology , vol.141 , pp. 123-131
    • Brurberg, M.B.1    Eijsink, V.G.2    Haandrikman, A.J.3    Venema, G.4    Nes, I.F.5
  • 9
    • 0027973484 scopus 로고
    • Characterization of a chitinase gene(ChiA)fromSerratia marcescensBJL200 and one-step purification of the gene product
    • Brurberg, M. B., Eijsink, V. G., and Nes, I. F., Characterization of a chitinase gene(chiA)fromSerratia marcescensBJL200 and one-step purification of the gene product.FEMS Microbiol. Lett.,124, 399-404 (1994).
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 399-404
    • Brurberg, M.B.1    Eijsink, V.G.2    Nes, I.F.3
  • 10
    • 0141596730 scopus 로고    scopus 로고
    • Isolation and characterization of the 54-kDa and 22-kDa chitinase genes ofSerratia marcescensKCTC2172
    • Gal, S. W., Choi, J. Y., Kim, C. Y., Cheong, Y. H., Choi, Y. J., Bahk, J. D., Lee, S. Y., and Cho, M. J., Isolation and characterization of the 54-kDa and 22-kDa chitinase genes ofSerratia marcescensKCTC2172.FEMS Microbiol. Lett.,151, 197-204 (1997).
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 197-204
    • Gal, S.W.1    Choi, J.Y.2    Kim, C.Y.3    Cheong, Y.H.4    Choi, Y.J.5    Bahk, J.D.6    Lee, S.Y.7    Cho, M.J.8
  • 11
    • 0032031378 scopus 로고    scopus 로고
    • Cloning of the 52-kDa chitinase gene fromSerratia marcescensKCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme
    • Gal, S. W., Choi, J. Y., Kim, C. Y., Cheong, Y. H., Choi, Y. J., Lee, S. Y., Bahk, J. D., and Cho, M. J., Cloning of the 52-kDa chitinase gene fromSerratia marcescensKCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme.FEMS Microbiol. Lett.,160, 151-158 (1998).
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 151-158
    • Gal, S.W.1    Choi, J.Y.2    Kim, C.Y.3    Cheong, Y.H.4    Choi, Y.J.5    Lee, S.Y.6    Bahk, J.D.7    Cho, M.J.8
  • 13
  • 17
    • 0035798612 scopus 로고    scopus 로고
    • Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A fromSerratia marcescens2170
    • Uchiyama, T., Katouno, F., Nikaidou, N., Nonaka, T., Sugiyama, J., and Watanabe, T., Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A fromSerratia marcescens2170.J. Biol. Chem.,276, 41343-41349 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 41343-41349
    • Uchiyama, T.1    Katouno, F.2    Nikaidou, N.3    Nonaka, T.4    Sugiyama, J.5    Watanabe, T.6
  • 18
  • 19
    • 0029884662 scopus 로고    scopus 로고
    • Comparative studies of chitinases A and B fromSerratia marcescens
    • Brurberg, M. B., Nes, I. F., and Eijsink, V. G., Comparative studies of chitinases A and B fromSerratia marcescens. Microbiology,142, 1581-1589 (1996).
    • (1996) Microbiology , vol.142 , pp. 1581-1589
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.3
  • 20
    • 9444272215 scopus 로고    scopus 로고
    • Three chitinase genes (ChiA, chiC and chiD) comprise the chitinase system ofBacillus circulansWL-12
    • Alam, M. M., Mizutani, T., Isono, M., Nikaidou, N., and Watanabe, T., Three chitinase genes (chiA, chiC and chiD) comprise the chitinase system ofBacillus circulansWL-12.J. Ferment. Bioeng.,82, 28-36 (1996).
    • (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
  • 21
    • 0031041984 scopus 로고    scopus 로고
    • Nucleotide sequence and expression of a gene (ChiB) for a chitinase fromStreptomyces lividans
    • Miyashita, K., Fujii, T., Watanabe, A., and Ueno, H., Nucleotide sequence and expression of a gene (chiB) for a chitinase fromStreptomyces lividans. J. Ferment. Bioeng.,83, 26-31 (1997).
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 26-31
    • Miyashita, K.1    Fujii, T.2    Watanabe, A.3    Ueno, H.4
  • 22
    • 0030019860 scopus 로고    scopus 로고
    • Cloning of a cluster of chitinase genes fromAeromo-nassp. No. 10S-24
    • Shiro, M., Ueda, M., Kawaguchi, T., and Arai, M., Cloning of a cluster of chitinase genes fromAeromo-nassp. No. 10S-24.Biochimi. Biophysi. Acta,1305, 44-48 (1996).
    • (1996) Biochimi. Biophysi. Acta , vol.1305 , pp. 44-48
    • Shiro, M.1    Ueda, M.2    Kawaguchi, T.3    Arai, M.4
  • 23
    • 0032955632 scopus 로고    scopus 로고
    • Multiplengenes involved in chitin degradation from the marine bacteriumPseudomonassp. Strain S91
    • Techkarnjanaruk, S. and Goodman, A. E., Multiplengenes involved in chitin degradation from the marine bacteriumPseudomonassp. strain S91.Microbiology,145, 925-934 (1999).
    • (1999) Microbiology , vol.145 , pp. 925-934
    • Techkarnjanaruk, S.1    Goodman, A.E.2
  • 25
    • 0027534187 scopus 로고
    • Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Altermonassp. Strain O-7
    • Tsujibo, H., Orikoshi, H., Tanno, H., Fujimoto, K., Miyamoto, K., Imada, C., Okami, Y., and Inamori, Y., Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Altermonassp. strain O-7.J. Bacteriol.,175, 176-181 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 176-181
    • Tsujibo, H.1    Orikoshi, H.2    Tanno, H.3    Fujimoto, K.4    Miyamoto, K.5    Imada, C.6    Okami, Y.7    Inamori, Y.8
  • 27
    • 0019883721 scopus 로고
    • A convenient synthesis of glycolchitin, a substrate of lysozyme
    • Yamada, H. and Imoto, T., A convenient synthesis of glycolchitin, a substrate of lysozyme.Carbohydr. Res.,92, 160-162 (1981).
    • (1981) Carbohydr. Res. , vol.92 , pp. 160-162
    • Yamada, H.1    Imoto, T.2
  • 28
    • 0017610344 scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • Molano, J., Duran, A., and Cabib, E., A rapid and sensitive assay for chitinase using tritiated chitin.Anal. Biochem.,83, 648-656 (1977).
    • (1977) Anal. Biochem. , vol.83 , pp. 648-656
    • Molano, J.1    Duran, A.2    Cabib, E.3
  • 29
    • 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(London), 227, 680-685 (1970).
    • (1970) Nature(London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0025314392 scopus 로고
    • Chitinase system ofBacillus circulansWL-12 and importance of chitinase A1 in chitin degradation
    • Watanabe, T., Oyanagi, W., Suzuki, K., and Tanaka, H., Chitinase system ofBacillus circulansWL-12 and importance of chitinase A1 in chitin degradation.J. Bacteriol.,172, 4017-4022 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 4017-4022
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Tanaka, H.4
  • 31
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T. and Yagishita, K., A simple activity measurement of lysozyme.Agr. Biol. Chem.,35, 1154-1156 (1971).
    • (1971) Agr. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 33
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P., Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.J. Biol. Chem.,262, 10035-10038 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.