메뉴 건너뛰기




Volumn 34, Issue 5, 1997, Pages 273-279

Characterization of cloned endoxylanase from Cellulomonas sp. NCIM 2353 expressed in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0030890729     PISSN: 03438651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002849900181     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0001719868 scopus 로고
    • Xylan structure, microbial xylanases, and their mode of action
    • Bastawade KB (1992) Xylan structure, microbial xylanases, and their mode of action. World J Microbiol Biotechnol 8:353-368
    • (1992) World J Microbiol Biotechnol , vol.8 , pp. 353-368
    • Bastawade, K.B.1
  • 3
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in PAGE gels
    • Blum H, Beier H, Gross HJ (1987) Improved silver staining of plant proteins, RNA and DNA in PAGE gels. Electophoresis 8:93-99
    • (1987) Electophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 5
    • 0021865554 scopus 로고
    • The role of carboxyl groups in the function of endo beta-1,4 glucanase from Schizophyllum commune
    • Clarke AJ, Yaguchi M (1985) The role of carboxyl groups in the function of endo beta-1,4 glucanase from Schizophyllum commune. Eur J Biochem 149:223-238
    • (1985) Eur J Biochem , vol.149 , pp. 223-238
    • Clarke, A.J.1    Yaguchi, M.2
  • 7
    • 0025107503 scopus 로고
    • Chemical modification of xylanase: Evidence for essential tryptophan and cysteine residues at the active site
    • Deshpande V, Hinge J, Rao M (1990) Chemical modification of xylanase: evidence for essential tryptophan and cysteine residues at the active site. Biochim Biophys Acta 1041:172-177
    • (1990) Biochim Biophys Acta , vol.1041 , pp. 172-177
    • Deshpande, V.1    Hinge, J.2    Rao, M.3
  • 8
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 11
    • 0009581494 scopus 로고
    • Differential expression of xylanases and endoglucanases in the hybrid derived from intergeneric protoplast fusion between a Cellulomonas species and B. subtilis
    • Gokhale DV, Deobagkar DN (1989) Differential expression of xylanases and endoglucanases in the hybrid derived from intergeneric protoplast fusion between a Cellulomonas species and B. subtilis. Appl Environ Microbiol 55:2675-2680
    • (1989) Appl Environ Microbiol , vol.55 , pp. 2675-2680
    • Gokhale, D.V.1    Deobagkar, D.N.2
  • 13
    • 1842319649 scopus 로고
    • Alkalophilic Bacillus xylanase A, a secretable protein through outer membrane of E. coli
    • Hamamoto T, Horikoshi K (1987) Alkalophilic Bacillus xylanase A, a secretable protein through outer membrane of E. coli. Agric Biol Chem 51:3133-3139
    • (1987) Agric Biol Chem , vol.51 , pp. 3133-3139
    • Hamamoto, T.1    Horikoshi, K.2
  • 14
    • 0014322072 scopus 로고
    • Isolation and characterization of a cellulose-utilising bacterium
    • Han YW, Srinivasan VR (1968) Isolation and characterization of a cellulose-utilising bacterium. Appl Microbiol 16:1140-1145
    • (1968) Appl Microbiol , vol.16 , pp. 1140-1145
    • Han, Y.W.1    Srinivasan, V.R.2
  • 15
    • 0024335334 scopus 로고
    • Chemical modification of a xylanase from a thermotolerant Streptomyces. Evidence for essential tryptophan and cysteine residues at the active site
    • Keskar SS, Srinivasan MC, Deshpande VV (1989) Chemical modification of a xylanase from a thermotolerant Streptomyces. Evidence for essential tryptophan and cysteine residues at the active site. Biochem J 261:49-55
    • (1989) Biochem J , vol.261 , pp. 49-55
    • Keskar, S.S.1    Srinivasan, M.C.2    Deshpande, V.V.3
  • 16
    • 0026542662 scopus 로고
    • Characterization and sequencing of an active-site cysteine containing peptide from the xylanase of a thermotolerant Streptomyces
    • Keskar SS, Rao MB, Deshpande VV (1992) Characterization and sequencing of an active-site cysteine containing peptide from the xylanase of a thermotolerant Streptomyces. Biochem J 281:601-605
    • (1992) Biochem J , vol.281 , pp. 601-605
    • Keskar, S.S.1    Rao, M.B.2    Deshpande, V.V.3
  • 17
    • 0027703676 scopus 로고
    • Regulation, purification and properties of xylanase from Cellulomonas fimi
    • Khanna S, Gauri (1993) Regulation, purification and properties of xylanase from Cellulomonas fimi. Enzyme Microb Technol 15:990-995
    • (1993) Enzyme Microb Technol , vol.15 , pp. 990-995
    • Khanna, S.1    Gauri2
  • 18
    • 0022435206 scopus 로고
    • An active center tryptophan residue in liquefying alpha amylase from Bacillus
    • Kochhar S, Dua RD (1985) An active center tryptophan residue in liquefying alpha amylase from Bacillus. Biochem Biophys Res Commun 126:966-973
    • (1985) Biochem Biophys Res Commun , vol.126 , pp. 966-973
    • Kochhar, S.1    Dua, R.D.2
  • 20
    • 0029082723 scopus 로고
    • Presence of multiple amylases encoded by independent genes in Cellulomonas sp. NCIM 2353
    • Kumar NN, Deobagkar DN (1995) Presence of multiple amylases encoded by independent genes in Cellulomonas sp. NCIM 2353. Biotechnol Lett 17:797-802
    • (1995) Biotechnol Lett , vol.17 , pp. 797-802
    • Kumar, N.N.1    Deobagkar, D.N.2
  • 21
    • 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
  • 22
    • 0024077054 scopus 로고
    • B. subtilis beta-1,4-endoglucanase genes from intact and truncated genes are secreted into the extracellular medium by E. coli
    • Lo AC, McKay RM, Seligy VL, Willick GE (1988) B. subtilis beta-1,4-endoglucanase genes from intact and truncated genes are secreted into the extracellular medium by E. coli. Appl Environ Microbiol 54:2287-2292
    • (1988) Appl Environ Microbiol , vol.54 , pp. 2287-2292
    • Lo, A.C.1    McKay, R.M.2    Seligy, V.L.3    Willick, G.E.4
  • 24
    • 84954941286 scopus 로고
    • Immunological properties and constituent amino acids of three xylanases produced inductively from Streptomyces sp.
    • Marui M, Nakanishi K, Yasui T (1985) Immunological properties and constituent amino acids of three xylanases produced inductively from Streptomyces sp. Agric Biol Chem 49:3409-3413
    • (1985) Agric Biol Chem , vol.49 , pp. 3409-3413
    • Marui, M.1    Nakanishi, K.2    Yasui, T.3
  • 25
    • 0028214219 scopus 로고
    • Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases
    • Millward-Sadler SJ, Poole DM, Henrissat B, Hazelwood GP, Clarke JH, Gilbert HJ (1994) Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases. Mol Microbiol 11:375-382
    • (1994) Mol Microbiol , vol.11 , pp. 375-382
    • Millward-Sadler, S.J.1    Poole, D.M.2    Henrissat, B.3    Hazelwood, G.P.4    Clarke, J.H.5    Gilbert, H.J.6
  • 26
    • 0022446556 scopus 로고
    • Isolation and partial primary sequence of a xylanase from the yeast Cryptococcus albidus
    • Morosoli R, Roy C, Yaguchi M (1986) Isolation and partial primary sequence of a xylanase from the yeast Cryptococcus albidus. Biochim Biophys Acta 870:473-478
    • (1986) Biochim Biophys Acta , vol.870 , pp. 473-478
    • Morosoli, R.1    Roy, C.2    Yaguchi, M.3
  • 27
    • 0011852227 scopus 로고
    • Purification and some properties of an endo 1,4-beta-D-xylanase from Streptomyces sp
    • Nakajima T, Tsukamoto K, Watanabe T, Kainuma K, Matsuda K (1984) Purification and some properties of an endo 1,4-beta-D-xylanase from Streptomyces sp. J Ferment Technol 62:269-276
    • (1984) J Ferment Technol , vol.62 , pp. 269-276
    • Nakajima, T.1    Tsukamoto, K.2    Watanabe, T.3    Kainuma, K.4    Matsuda, K.5
  • 28
    • 0039825170 scopus 로고
    • Purification of three types of xylanases from an alkalophilic Aeromonas sp.
    • Ohkoshi A, Kudo T, Mase T, Horikoshi K (1985) Purification of three types of xylanases from an alkalophilic Aeromonas sp. Agric Biol Chem 49:3037-3038
    • (1985) Agric Biol Chem , vol.49 , pp. 3037-3038
    • Ohkoshi, A.1    Kudo, T.2    Mase, T.3    Horikoshi, K.4
  • 29
    • 0019972097 scopus 로고
    • Comparison of the xylanolytic and cellulolytic activities of Cellulomonas
    • Peins SP, Rickard PAD, Dunn NW (1982) Comparison of the xylanolytic and cellulolytic activities of Cellulomonas. Eur J Appl Microbiol Biotechnol 14:169-173
    • (1982) Eur J Appl Microbiol Biotechnol , vol.14 , pp. 169-173
    • Peins, S.P.1    Rickard, P.A.D.2    Dunn, N.W.3
  • 30
    • 0028905198 scopus 로고
    • Purification and characterisation of a cellulose binding endoxylanase from Cellulomonas flavigena
    • Pembroke JT, McMohan M, Sweeney B (1995) Purification and characterisation of a cellulose binding endoxylanase from Cellulomonas flavigena. Biotechnol Lett 17:331-334
    • (1995) Biotechnol Lett , vol.17 , pp. 331-334
    • Pembroke, J.T.1    McMohan, M.2    Sweeney, B.3
  • 31
    • 0021739999 scopus 로고
    • Cellulase and hemicellulase production by Cellulomonas flavigena NIAB 441
    • Rajoka MI, Malik KA (1984) Cellulase and hemicellulase production by Cellulomonas flavigena NIAB 441. Biotechnol Lett 6:597-600
    • (1984) Biotechnol Lett , vol.6 , pp. 597-600
    • Rajoka, M.I.1    Malik, K.A.2
  • 32
    • 0001077278 scopus 로고
    • Comparison of different strains of Cellulomonas for production of cellulolytic and xylanolytic enzymes from biomass produced on saline lands
    • Rajoka MI, Malik KA (1986) Comparison of different strains of Cellulomonas for production of cellulolytic and xylanolytic enzymes from biomass produced on saline lands. Biotechnol Lett 8:753-756
    • (1986) Biotechnol Lett , vol.8 , pp. 753-756
    • Rajoka, M.I.1    Malik, K.A.2
  • 33
    • 0028979231 scopus 로고
    • Chemical modification of xylanase from Chainia NCL 82.5.1
    • Rao M, Khadilkar S, Deshpande V (1995) Chemical modification of xylanase from Chainia NCL 82.5.1. Biotechnol Lett 17:589-592
    • (1995) Biotechnol Lett , vol.17 , pp. 589-592
    • Rao, M.1    Khadilkar, S.2    Deshpande, V.3
  • 34
    • 0022627851 scopus 로고
    • Production and properties of xylan-degrading enzymes from Cellulomonas uda
    • Rapp P, Wagner F (1986) Production and properties of xylan-degrading enzymes from Cellulomonas uda. Appl Environ Microbiol 51:746-752
    • (1986) Appl Environ Microbiol , vol.51 , pp. 746-752
    • Rapp, P.1    Wagner, F.2
  • 35
    • 0015242051 scopus 로고
    • Isoelectric focusing in polyacrylamide gel electrophoresis
    • Righetti P, Drysdale JW (1971) Isoelectric focusing in polyacrylamide gel electrophoresis. Biochim Biophys Acta 236:17-23
    • (1971) Biochim Biophys Acta , vol.236 , pp. 17-23
    • Righetti, P.1    Drysdale, J.W.2
  • 36
    • 0027410681 scopus 로고
    • Cloning and extracellular expression in E. coli of xylanases from an alkaliphilic thermophilic Bacillus sp. NCIM 59
    • Shendye A, Rao M (1993) Cloning and extracellular expression in E. coli of xylanases from an alkaliphilic thermophilic Bacillus sp. NCIM 59. FEMS Microbiol Lett 108:297-302
    • (1993) FEMS Microbiol Lett , vol.108 , pp. 297-302
    • Shendye, A.1    Rao, M.2
  • 37
    • 0027345153 scopus 로고
    • Molecular biology of xylan degradation
    • Thomson JA (1993) Molecular biology of xylan degradation. FEMS Microbiol Rev 104:65-82
    • (1993) FEMS Microbiol Rev , vol.104 , pp. 65-82
    • Thomson, J.A.1
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordan J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4351
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4351
    • Towbin, H.1    Staehelin, T.2    Gordan, J.3
  • 39
  • 40
    • 84910447165 scopus 로고
    • Precipitation analysis by diffusion gels
    • Academic Press
    • Williams CA, Chase MW (1971) Precipitation analysis by diffusion gels. In: Methods Immunol Immunochem. Academic Press, pp 146-160
    • (1971) Methods Immunol Immunochem , pp. 146-160
    • Williams, C.A.1    Chase, M.W.2
  • 41
    • 0024087074 scopus 로고
    • Multiplicity of beta-1,4-xylanase in micro-organisms: Functions and applications
    • Wong KKY, Tan LUL, Saddler JN (1988) Multiplicity of beta-1,4-xylanase in micro-organisms: functions and applications. Microbiol Rev 52:305-317
    • (1988) Microbiol Rev , vol.52 , pp. 305-317
    • Wong, K.K.Y.1    Tan, L.U.L.2    Saddler, J.N.3
  • 42
    • 0028332196 scopus 로고
    • Enzymatic specificities and modes of action of the two catalytic domains of the XynC xylanase from Fibrobacter succinogenes 85
    • Zhu H, Paradis FW, Krell PJ, Phillips JP, Forsberg CW (1994) Enzymatic specificities and modes of action of the two catalytic domains of the XynC xylanase from Fibrobacter succinogenes 85. J Bacteriol 176:3885-3894
    • (1994) J Bacteriol , vol.176 , pp. 3885-3894
    • Zhu, H.1    Paradis, F.W.2    Krell, P.J.3    Phillips, J.P.4    Forsberg, C.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.