메뉴 건너뛰기




Volumn 74, Issue 13, 2008, Pages 4210-4217

Purification and characterization of a new family 45 endoglucanase, STCE1, from Staphylotrichum coccosporum and its overproduction in Humicola insolens

Author keywords

[No Author keywords available]

Indexed keywords

AGENTS; AMINES; AMINO ACIDS; ARSENIC COMPOUNDS; BIOPHYSICS; CARBOHYDRATES; CLEANING; DETERGENTS; FABRICS; FOOD ADDITIVES; GENE ENCODING; HEALTH; ORGANIC ACIDS; ORGANIC COMPOUNDS; OXIDATION; PORT TERMINALS; PURIFICATION; REUSABILITY; SOAPS (DETERGENTS); SODIUM CHLORIDE; SUGARS; SURFACE ACTIVE AGENTS;

EID: 46949111816     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02747-07     Document Type: Article
Times cited : (22)

References (39)
  • 1
    • 0034255675 scopus 로고    scopus 로고
    • Effects of agitation level on the adsorption, desorption, and activities on cotton fabrics of full-length and core domains of EGV (Humicola insolens) and CenA (Cellulomonas fimi)
    • Azevedo, H., D. Bishop, and A. Cavaco-Paulo. 2000. Effects of agitation level on the adsorption, desorption, and activities on cotton fabrics of full-length and core domains of EGV (Humicola insolens) and CenA (Cellulomonas fimi). Enzyme Microb. Technol. 27:325-329.
    • (2000) Enzyme Microb. Technol , vol.27 , pp. 325-329
    • Azevedo, H.1    Bishop, D.2    Cavaco-Paulo, A.3
  • 2
    • 17644417083 scopus 로고    scopus 로고
    • Alternative splicing produces two endoglucanases with one or two carbohydrate-binding modules in Mucor circinelloides
    • Baba, Y., A. Shimonaka, J. Koga, H. Kubota, and T. Kono. 2005. Alternative splicing produces two endoglucanases with one or two carbohydrate-binding modules in Mucor circinelloides. J. Bacteriol. 187:3045-3051.
    • (2005) J. Bacteriol , vol.187 , pp. 3045-3051
    • Baba, Y.1    Shimonaka, A.2    Koga, J.3    Kubota, H.4    Kono, T.5
  • 3
    • 22444432914 scopus 로고    scopus 로고
    • Purification and characterization of a new endo-1,4-β- D-glucanase from Beltraniella portoricensis
    • Baba, Y., A. Shimonaka, J. Koga, K. Murashima, H. Kubota, and T. Kono. 2005. Purification and characterization of a new endo-1,4-β- D-glucanase from Beltraniella portoricensis. Biosci. Biotechnol. Biochem. 69:1198-1201.
    • (2005) Biosci. Biotechnol. Biochem , vol.69 , pp. 1198-1201
    • Baba, Y.1    Shimonaka, A.2    Koga, J.3    Murashima, K.4    Kubota, H.5    Kono, T.6
  • 5
    • 0034253208 scopus 로고    scopus 로고
    • Cellulases and related enzymes in biotechnology
    • Bhat, M. K. 2000. Cellulases and related enzymes in biotechnology. Biotechnol. Adv. 18:355-383.
    • (2000) Biotechnol. Adv , vol.18 , pp. 355-383
    • Bhat, M.K.1
  • 6
    • 0031295876 scopus 로고    scopus 로고
    • Cellulose degrading enzymes and their potential industrial applications
    • Bhat, M. K., and S. Bhat. 1997. Cellulose degrading enzymes and their potential industrial applications. Biotechnol. Adv. 15:583-620.
    • (1997) Biotechnol. Adv , vol.15 , pp. 583-620
    • Bhat, M.K.1    Bhat, S.2
  • 7
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston, A. B., D. N. Bolam, H. J. Gilbert, and G. J. Davies. 2004. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382:769-781.
    • (2004) Biochem. J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 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
  • 9
    • 0032204689 scopus 로고    scopus 로고
    • Mechanism of cellulase action in textile processes
    • Cavaco-Paulo, A. 1998. Mechanism of cellulase action in textile processes. Carbohydr. Polym. 37:273-277.
    • (1998) Carbohydr. Polym , vol.37 , pp. 273-277
    • Cavaco-Paulo, A.1
  • 10
    • 0034657160 scopus 로고    scopus 로고
    • Structure and function of Humicola insolens family 6 cellulases: Structure of the endoglucanase, Cel6B, at 1.6 A resolution
    • Davies, G. J., A. M. Brzozowski, M. Dauter, A. Varrot, and M. Schulein. 2000. Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution. Biochem. J. 348:201-207.
    • (2000) Biochem. J , vol.348 , pp. 201-207
    • Davies, G.J.1    Brzozowski, A.M.2    Dauter, M.3    Varrot, A.4    Schulein, M.5
  • 12
    • 0026349480 scopus 로고
    • Non-hydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase
    • Din, N., N. R. Gilkes, B. Tekant, R. C. J. Miller, R. A. J. Warren, and D. G. Kilburn. 1991. Non-hydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase. Bio/Technology 9:1096-1099.
    • (1991) Bio/Technology , vol.9 , pp. 1096-1099
    • Din, N.1    Gilkes, N.R.2    Tekant, B.3    Miller, R.C.J.4    Warren, R.A.J.5    Kilburn, D.G.6
  • 13
    • 0005648062 scopus 로고    scopus 로고
    • Steady growth for industrial enzyme market
    • Glaser, V. 2000. Steady growth for industrial enzyme market. Genet. Eng. News 20:8-36.
    • (2000) Genet. Eng. News , vol.20 , pp. 8-36
    • Glaser, V.1
  • 14
    • 0024419181 scopus 로고
    • Cellulase families revealed by hydrophobic cluster analysis
    • Henrissat, B., M. Claeyssens, P. Tomme, L. Lemesle, and J. P. Mornon. 1989. Cellulase families revealed by hydrophobic cluster analysis. Gene 81:83-95.
    • (1989) Gene , vol.81 , pp. 83-95
    • Henrissat, B.1    Claeyssens, M.2    Tomme, P.3    Lemesle, L.4    Mornon, J.P.5
  • 15
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in the degradation of cellulose
    • Henrissat, B., H. Driguez, C. Viet, and M. Schülein. 1985. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. Bio/Technology 3:722-726.
    • (1985) Bio/Technology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3    Schülein, M.4
  • 16
    • 0030806312 scopus 로고    scopus 로고
    • Cellulose and xylan utilization in the lower termite Reticulitermes speratus
    • Inoue, T., K. Murashima, J. Azuma, A. Sugimoto, and M. Slaytor. 1997. Cellulose and xylan utilization in the lower termite Reticulitermes speratus. J. Insect Physiol. 43:235-242.
    • (1997) J. Insect Physiol , vol.43 , pp. 235-242
    • Inoue, T.1    Murashima, K.2    Azuma, J.3    Sugimoto, A.4    Slaytor, M.5
  • 17
    • 0007196905 scopus 로고    scopus 로고
    • Color-care cellulases: Fabric color shield
    • Jakobsen, T. S., P. Lindegaard, and M. Chan. 1998. Color-care cellulases: fabric color shield. Inform 9:788-792.
    • (1998) Inform , vol.9 , pp. 788-792
    • Jakobsen, T.S.1    Lindegaard, P.2    Chan, M.3
  • 18
    • 46949111637 scopus 로고    scopus 로고
    • Endoglucanase STCE and cellulase preparation containing the same
    • September, European patent 1700917
    • Koga, J., Y. Baba, A. Nakane, S. Hamura, T. Nishimua, S. Gomi, H. Kubota, and T. Kono. September 2006. Endoglucanase STCE and cellulase preparation containing the same. European patent 1700917.
    • (2006)
    • Koga, J.1    Baba, Y.2    Nakane, A.3    Hamura, S.4    Nishimua, T.5    Gomi, S.6    Kubota, H.7    Kono, T.8
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 20
    • 84875213003 scopus 로고    scopus 로고
    • Miettinen-Oinonen, A. 2007. Cellulases in the textile industry, p. 51-63. In J. Polainoa and A. MacCabe, Industrial enzymes: structure, function and applications. Springer, Dordrecht, The Netherlands.
    • Miettinen-Oinonen, A. 2007. Cellulases in the textile industry, p. 51-63. In J. Polainoa and A. MacCabe, Industrial enzymes: structure, function and applications. Springer, Dordrecht, The Netherlands.
  • 21
    • 0036327466 scopus 로고    scopus 로고
    • Enhanced production of Trichoderma reesei endoglucanases and use of the new cellulase preparations in producing the stonewashed effect on denim fabric
    • Miettinen-Oinonen, A., and P. Suominen. 2002. Enhanced production of Trichoderma reesei endoglucanases and use of the new cellulase preparations in producing the stonewashed effect on denim fabric. Appl. Environ. Microbiol. 68:3956-3964.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 3956-3964
    • Miettinen-Oinonen, A.1    Suominen, P.2
  • 22
    • 33747333106 scopus 로고
    • Use of dinitrosalicyclic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicyclic acid reagent for determination of reducing sugar. Anal. Chem. 31:426-428.
    • (1959) Anal. Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 23
    • 0037373344 scopus 로고    scopus 로고
    • Molecular cloning of endo-β-D-1, 4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae
    • Moriya, T., K. Murashima, A. Nakane, K. Yanai, N. Sumida, J. Koga, T. Murakami, and T. Kono. 2003. Molecular cloning of endo-β-D-1, 4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae. J. Bacteriol. 185:1749-1756.
    • (2003) J. Bacteriol , vol.185 , pp. 1749-1756
    • Moriya, T.1    Murashima, K.2    Nakane, A.3    Yanai, K.4    Sumida, N.5    Koga, J.6    Murakami, T.7    Kono, T.8
  • 24
    • 46949093330 scopus 로고    scopus 로고
    • Enzyme endoglucanase and cellulase preparations containing the same
    • December, U.S. patent 6159720
    • Murashima, K., T. Moriya, T. Hamaya, J. Koga, N. Sumida, K. Aoyagi, T. Murakami, and T. Kono. December 2000. Enzyme endoglucanase and cellulase preparations containing the same. U.S. patent 6159720.
    • (2000)
    • Murashima, K.1    Moriya, T.2    Hamaya, T.3    Koga, J.4    Sumida, N.5    Aoyagi, K.6    Murakami, T.7    Kono, T.8
  • 26
    • 33749006205 scopus 로고    scopus 로고
    • Exploring amino acids responsible for the temperature profile of glycoside hydrolase family 45 endoglucanase EGL3 from Humicola grisea
    • Murashima, K., A. Shimonaka, T. Nishimura, Y. Baba, J. Koga, H. Kubota, and T. Kono. 2006. Exploring amino acids responsible for the temperature profile of glycoside hydrolase family 45 endoglucanase EGL3 from Humicola grisea. Biosci. Biotechnol. Biochem. 70:2205-2212.
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 2205-2212
    • Murashima, K.1    Shimonaka, A.2    Nishimura, T.3    Baba, Y.4    Koga, J.5    Kubota, H.6    Kono, T.7
  • 27
    • 46949083598 scopus 로고    scopus 로고
    • Endoglucanase enzyme NCE5 and cellulase preparations containing the same
    • November, U.S. patent 7138263
    • Murashima, K., N. Sumida, A. Nakane, K. Yanai, T. Nishimura, J. Koga, T. Murakami, and T. Kono. November 2006. Endoglucanase enzyme NCE5 and cellulase preparations containing the same. U.S. patent 7138263.
    • (2006)
    • Murashima, K.1    Sumida, N.2    Nakane, A.3    Yanai, K.4    Nishimura, T.5    Koga, J.6    Murakami, T.7    Kono, T.8
  • 29
    • 25444525116 scopus 로고    scopus 로고
    • Specific characteristics of an endoglucanase RCE1 from Rhizopus oryzae in the treatment of the dyed cotton fabrics
    • Nakane, A., J. Koga, H. Kubota, and T. Kono. 2005. Specific characteristics of an endoglucanase RCE1 from Rhizopus oryzae in the treatment of the dyed cotton fabrics. Sen'i Gakkaishi 61:229-233.
    • (2005) Sen'i Gakkaishi , vol.61 , pp. 229-233
    • Nakane, A.1    Koga, J.2    Kubota, H.3    Kono, T.4
  • 30
    • 0029310610 scopus 로고
    • Purification and properties of wall-bound endo-1,4-β-glucanase from suspension-cultured poplar cells
    • Ohmiya, Y., T. Takeda, S. Nakamura, F. Sakai, and T. Hayashi. 1995. Purification and properties of wall-bound endo-1,4-β-glucanase from suspension-cultured poplar cells. Plant Cell Physiol. 36:607-614.
    • (1995) Plant Cell Physiol , vol.36 , pp. 607-614
    • Ohmiya, Y.1    Takeda, T.2    Nakamura, S.3    Sakai, F.4    Hayashi, T.5
  • 31
    • 0032871869 scopus 로고    scopus 로고
    • A comparative study of the unfolding of the endoglucanase Cel45 from Humicola insolens in denaturant and surfactant
    • Otzen, D. E., L. Christiansen, and M. Schulein. 1999. A comparative study of the unfolding of the endoglucanase Cel45 from Humicola insolens in denaturant and surfactant. Protein Sci. 8:1878-1887.
    • (1999) Protein Sci , vol.8 , pp. 1878-1887
    • Otzen, D.E.1    Christiansen, L.2    Schulein, M.3
  • 34
    • 11144280580 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding endo-β-D-1,4- glucanase PCE1 from Phycomyces nitens
    • Shimonaka, A., Y. Baba, J. Koga, A. Nakane, H. Kubota, and T. Kono. 2004. Molecular cloning of a gene encoding endo-β-D-1,4- glucanase PCE1 from Phycomyces nitens. Biosci. Biotechnol. Biochem. 68:2299-2305.
    • (2004) Biosci. Biotechnol. Biochem , vol.68 , pp. 2299-2305
    • Shimonaka, A.1    Baba, Y.2    Koga, J.3    Nakane, A.4    Kubota, H.5    Kono, T.6
  • 36
    • 33750462747 scopus 로고    scopus 로고
    • Amino acid regions of family 45 endoglucanases involved in cotton defibrillation and in resistance to anionic surfactants and oxidizing agents
    • Shimonaka, A., K. Murashima, J. Koga, Y. Baba, T. Nishimura, H. Kubota, and T. Kono. 2006. Amino acid regions of family 45 endoglucanases involved in cotton defibrillation and in resistance to anionic surfactants and oxidizing agents. Biosci. Biotechnol. Biochem. 70:2460-2466.
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 2460-2466
    • Shimonaka, A.1    Murashima, K.2    Koga, J.3    Baba, Y.4    Nishimura, T.5    Kubota, H.6    Kono, T.7
  • 37
    • 0017802798 scopus 로고    scopus 로고
    • Shoemaker, S. P., and R. D. Brown, Jr. 1978. Characterization of endo-1,4-β-D-glucanases purified from Trichoderma viride. Biochim. Biophys. Acta 523:147-161.
    • Shoemaker, S. P., and R. D. Brown, Jr. 1978. Characterization of endo-1,4-β-D-glucanases purified from Trichoderma viride. Biochim. Biophys. Acta 523:147-161.
  • 38
    • 0032926666 scopus 로고    scopus 로고
    • Comparison of gene structures and enzymatic properties between two endoglucanases from Humicola grisea
    • Takashima, S., H. Iikura, A. Nakamura, M. Hidaka, H. Masaki, and T. Uozumi. 1999. Comparison of gene structures and enzymatic properties between two endoglucanases from Humicola grisea. J. Biotechnol. 67:85-97.
    • (1999) J. Biotechnol , vol.67 , pp. 85-97
    • Takashima, S.1    Iikura, H.2    Nakamura, A.3    Hidaka, M.4    Masaki, H.5    Uozumi, T.6
  • 39
    • 0026586210 scopus 로고
    • Fungal cellulases
    • Wood, T. M. 1992. Fungal cellulases. Biochem. Soc. Trans. 20:46-53.
    • (1992) Biochem. Soc. Trans , vol.20 , pp. 46-53
    • Wood, T.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.