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Volumn 15, Issue 2, 2010, Pages 273-276

Effect of growth temperature, induction, and molecular chaperones on the solubilization of over-expressed cellobiose phosphorylase from cellvibrio gilvus under in vivo conditions

Author keywords

Cellobiose phosphorylase; Cellvibrio gilvus; Molecular chaperone; Over expression; Solubilization

Indexed keywords

CELLOBIOSE; CO-EXPRESSION; IN-VIVO; INCLUSION BODIES; LOW GROWTH TEMPERATURE; LOW LEVEL; LOW TEMPERATURES; MOLECULAR CHAPERONES; OVER-EXPRESSION; RECOMBINANT PROTEIN; SOLUBLE FRACTION; SYNERGISTIC EFFECT; TARGET GENES;

EID: 77953548934     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12257-009-0023-1     Document Type: Article
Times cited : (10)

References (15)
  • 1
    • 0028931975 scopus 로고
    • Purification and properties of cellobiose phosphorylase from Clostridium thermocellum
    • Tanaka, K., K. Kawaguchi, T. Imada, T. Ooi, and M. Arai (1995) Purification and properties of cellobiose phosphorylase from Clostridium thermocellum. J. Ferment. Bioeng. 79: 212-216.
    • (1995) J. Ferment. Bioeng. , vol.79 , pp. 212-216
    • Tanaka, K.1    Kawaguchi, K.2    Imada, T.3    Ooi, T.4    Arai, M.5
  • 2
    • 0031749615 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the cellobiose phosphorylase gene of Cellvibrio gilvus
    • Liu, A., H. Tomita, H. Li, H. Miyaki, C. Aoyagi, S. Kaneko, and K. Hayashi (1998) Cloning, sequencing, and expression of the cellobiose phosphorylase gene of Cellvibrio gilvus. J. Ferment. Bioeng. 85: 511-513.
    • (1998) J. Ferment. Bioeng. , vol.85 , pp. 511-513
    • Liu, A.1    Tomita, H.2    Li, H.3    Miyaki, H.4    Aoyagi, C.5    Kaneko, S.6    Hayashi, K.7
  • 3
    • 37849188954 scopus 로고    scopus 로고
    • Phosphorylase coupling as a tool to convert cellobiose into amylose
    • Ohdan, K., K. Fujii, M. Yanase, V. Takaha, and T. Kuriki (2007) Phosphorylase coupling as a tool to convert cellobiose into amylose. J. Biotechnol. 127: 496-502.
    • (2007) J. Biotechnol. , vol.127 , pp. 496-502
    • Ohdan, K.1    Fujii, K.2    Yanase, M.3    Takaha, V.4    Kuriki, T.5
  • 4
    • 34249742691 scopus 로고    scopus 로고
    • Cloning and expression of cyclodextrin glycosyltransferase Gene from Paenibacillus sp. T16 isolated from hot spring soil in northern Thailand
    • Charoensakdi, R., S. Murakami, K. Aoki, V. Rimphanitchayakit, and T. Limpaseni (2006) Cloning and expression of cyclodextrin glycosyltransferase Gene from Paenibacillus sp. T16 isolated from hot spring soil in northern Thailand. J. Biochem. Mol. Bio. 40: 333-340.
    • (2006) J. Biochem. Mol. Bio. , vol.40 , pp. 333-340
    • Charoensakdi, R.1    Murakami, S.2    Aoki, K.3    Rimphanitchayakit, V.4    Limpaseni, T.5
  • 5
    • 2442502648 scopus 로고    scopus 로고
    • Cellobiose phosphorylase from Cellulomonas uda: Gene cloning and expression in Escherichia coli, and application of the recombinant enzyme in a 'glycosynthase-type' reaction
    • Nidetzky, B., R. Griessler, A. Schwarz, and B. Splechtna (2004) Cellobiose phosphorylase from Cellulomonas uda: gene cloning and expression in Escherichia coli, and application of the recombinant enzyme in a 'glycosynthase-type' reaction. J. Mol. Cata. B: Enzymatic 29: 241-248.
    • (2004) J. Mol. Cata. B: Enzymatic , vol.29 , pp. 241-248
    • Nidetzky, B.1    Griessler, R.2    Schwarz, A.3    Splechtna, B.4
  • 7
    • 0032008243 scopus 로고    scopus 로고
    • Overproduction of β-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES
    • Machida, S., Y. Yu, S. P. Singh, J. D. Kim, K. Hayashi, and Y. Kawata (1998) Overproduction of β-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES. FEMS Microbiol. Lett. 159: 41-46.
    • (1998) FEMS Microbiol. Lett. , vol.159 , pp. 41-46
    • MacHida, S.1    Yu, Y.2    Singh, S.P.3    Kim, J.D.4    Hayashi, K.5    Kawata, Y.6
  • 8
    • 0011143920 scopus 로고    scopus 로고
    • Overexpression and protein folding of a chimeric β-glucosidase constructed from Agrobacterium tumefaciens and Cellvibrio gilvus
    • Singh, S. P., J. D. Kim, S. Machida, and K. Hayashi (2002) Overexpression and protein folding of a chimeric β-glucosidase constructed from Agrobacterium tumefaciens and Cellvibrio gilvus. Ind. J. Biochem. Biophys. 39: 235-239.
    • (2002) Ind. J. Biochem. Biophys. , vol.39 , pp. 235-239
    • Singh, S.P.1    Kim, J.D.2    MacHida, S.3    Hayashi, K.4
  • 9
    • 0006283489 scopus 로고    scopus 로고
    • Importance of five amino acid residues at Cterminal region for the folding and stability of β-Glucosidase of Cellvibrio gilvus
    • Kim, D., S. Singh, S. Machida, Y. Chika, Y. Kawata, and K. Hayashi (1998) Importance of five amino acid residues at Cterminal region for the folding and stability of β-Glucosidase of Cellvibrio gilvus. J. Ferment. Bioeng. 85: 433-435.
    • (1998) J. Ferment. Bioeng. , vol.85 , pp. 433-435
    • Kim, D.1    Singh, S.2    MacHida, S.3    Chika, Y.4    Kawata, Y.5    Hayashi, K.6
  • 10
    • 0034624223 scopus 로고    scopus 로고
    • Cycloamylose as an efficient artificial chaperone for protein refolding
    • Machida, S., S. Ogawa, S. Xiaohua, T. Takaha, K. Fujii, and K. Hayashi (2000) Cycloamylose as an efficient artificial chaperone for protein refolding. FEBS Lett. 486: 131-135.
    • (2000) FEBS Lett. , vol.486 , pp. 131-135
    • MacHida, S.1    Ogawa, S.2    Xiaohua, S.3    Takaha, T.4    Fujii, K.5    Hayashi, K.6
  • 11
    • 38049068849 scopus 로고    scopus 로고
    • Purification and stability characteristics of an alkaline serine protease from a newly isolated haloalkaliphilic bacterium sp. AH-6
    • Dodia, M. S., C. M. Rawal, H. G. Bhimani, R. H. Joshi, S. K. Khare, and S. P. Singh (2008) Purification and stability characteristics of an alkaline serine protease from a newly isolated haloalkaliphilic bacterium sp. AH-6. J. Ind. Microbiol. Biotechnol. 35: 121-131.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 121-131
    • Dodia, M.S.1    Rawal, C.M.2    Bhimani, H.G.3    Joshi, R.H.4    Khare, S.K.5    Singh, S.P.6
  • 12
    • 43849095922 scopus 로고    scopus 로고
    • Salt dependent resistance against chemical denaturation of alkaline protease from a newly isolated Haloalkaliphilic Bacillus sp
    • Dodia, M. S., H. G. Bhimani, C. M. Rawal, R. H. Joshi, and S. P. Singh (2008) Salt dependent resistance against chemical denaturation of alkaline protease from a newly isolated Haloalkaliphilic Bacillus sp. Bioresour. Technol. 99: 6223-6227.
    • (2008) Bioresour. Technol. , vol.99 , pp. 6223-6227
    • Dodia, M.S.1    Bhimani, H.G.2    Rawal, C.M.3    Joshi, R.H.4    Singh, S.P.5
  • 13
    • 34548412730 scopus 로고    scopus 로고
    • Recombinant expression, characterization, and pulp prebleaching property of a Phanerochaete chrysosporium endo-β-1,4-mannanase
    • Benech, R. O., X. Li, D. Patton, J. Powlowski, R. Storms, R. Bourbonnais, M. Paice, and A. Tsang (2007) Recombinant expression, characterization, and pulp prebleaching property of a Phanerochaete chrysosporium endo-β-1,4- mannanase. Enzy. Microb. Technol. 41: 740-747.
    • (2007) Enzy. Microb. Technol. , vol.41 , pp. 740-747
    • Benech, R.O.1    Li, X.2    Patton, D.3    Powlowski, J.4    Storms, R.5    Bourbonnais, R.6    Paice, M.7    Tsang, A.8
  • 14
    • 0028917544 scopus 로고
    • Effective renaturation of reduced lysozyme by gentle removal of urea
    • Maeda, Y., H. Koga, H. Yamada, T. Ueda, and T. Imoto (1995) Effective renaturation of reduced lysozyme by gentle removal of urea. Protein Eng. 8: 201-205.
    • (1995) Protein Eng. , vol.8 , pp. 201-205
    • Maeda, Y.1    Koga, H.2    Yamada, H.3    Ueda, T.4    Imoto, T.5
  • 15
    • 0029980026 scopus 로고    scopus 로고
    • Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea
    • Maeda, Y., H. Koga, H. Yamada, T. Ueda, and T. Imoto (1996) Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea. Protein Eng. 9: 461-465.
    • (1996) Protein Eng. , vol.9 , pp. 461-465
    • Maeda, Y.1    Koga, H.2    Yamada, H.3    Ueda, T.4    Imoto, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.