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Volumn 61, Issue 4, 2009, Pages 581-586

Glycosylation and pH stability of Penicillin G acylase from Providencia rettgeri produced in Pichia pastoris

Author keywords

Glycosylation; Penicillin acylase; pH stability; Pichia pastoris

Indexed keywords


EID: 77949907121     PISSN: 03544664     EISSN: None     Source Type: Journal    
DOI: 10.2298/ABS0904581S     Document Type: Article
Times cited : (4)

References (21)
  • 1
    • 0031604266 scopus 로고    scopus 로고
    • Secretion of recombinant human insulinlike growth factor I (IGF-1)
    • Brierley, R. A. (1998). Secretion of recombinant human insulinlike growth factor I (IGF-1). Methods Mol. Biol. 103, 149- 177.
    • (1998) Methods Mol. Biol. , vol.103 , pp. 149-177
    • Brierley, R.A.1
  • 2
    • 0019551730 scopus 로고
    • " Western blotting" : electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. (1981). " Western blotting" : electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 3
    • 0034129596 scopus 로고    scopus 로고
    • An aproach for enhancing heterologous production of Providencia rettgeri penicillin acylase in Escherichia coli
    • Chou, P. C., Wang, W.-C., and M.-I. Lin (2000). An aproach for enhancing heterologous production of Providencia rettgeri penicillin acylase in Escherichia coli. Biotechnol. Prog. 16, 315-318.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 315-318
    • Chou, P.C.1    Wang, W.-C.2    Lin, M.-I.3
  • 4
    • 0021930011 scopus 로고
    • Role of protein subunits in Proteus rettgeri penicillin G acylase
    • Daumy, G. O., Danley, D., and A. S. McColl (1985). Role of protein subunits in Proteus rettgeri penicillin G acylase. J. Bacteriol. 163, 1279-1281.
    • (1985) J. Bacteriol. , vol.163 , pp. 1279-1281
    • Daumy, G.O.1    Danley, D.2    McColl, A.S.3
  • 5
    • 0022450984 scopus 로고
    • Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli
    • Daumy, G. O., Williams, J. A., Mc Coll, A. S., and T. J. Zuzel (1986). Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli. J. Bacteriol. 168, 431-433.
    • (1986) J. Bacteriol. , vol.168 , pp. 431-433
    • Daumy, G.O.1    Williams, J.A.2    Mc Coll, A.S.3    Zuzel, T.J.4
  • 8
    • 0031172410 scopus 로고    scopus 로고
    • Expression in Pichia pastoris and purification of Aspergillus awamori glucoamylase catalytic domain
    • Heimo, H., Palmu, K., and I. Suominen (1997). Expression in Pichia pastoris and purification of Aspergillus awamori glucoamylase catalytic domain. Protein Expr. Purif. 10, 70-79.
    • (1997) Protein Expr. Purif. , vol.10 , pp. 70-79
    • Heimo, H.1    Palmu, K.2    Suominen, I.3
  • 9
    • 0030250653 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of recombinant barley alpha-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris
    • Juge, N., Andersen, J. S., Tull, D., Roepstorff, P., and B. Svensson (1996). Overexpression, purification, and characterization of recombinant barley alpha-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 8, 204-214.
    • (1996) Protein Expr. Purif. , vol.8 , pp. 204-214
    • Juge, N.1    Andersen, J.S.2    Tull, D.3    Roepstorff, P.4    Svensson, B.5
  • 10
    • 0030484089 scopus 로고    scopus 로고
    • Influence of polyhydric compounds on the pH stability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105
    • Kazan, D., and A. Erarslan (1996). Influence of polyhydric compounds on the pH stability of penicillin G acylase obtained from a mutant of Escherichia coli ATCC 11105. Process Biochem. 31, 691.
    • (1996) Process Biochem , vol.31 , pp. 691
    • Kazan, D.1    Erarslan, A.2
  • 11
    • 0015956266 scopus 로고
    • Preparation and general properties of crystalline penicillin acylase from Escherichia coli ATCC 11105
    • Kutzbach, M., and E. Rauenbusch (1974). Preparation and general properties of crystalline penicillin acylase from Escherichia coli ATCC 11105. Hoppe-Seylers Z. Physiol. Chem. 354, 45-53.
    • (1974) Hoppe-Seylers Z. Physiol. Chem. , vol.354 , pp. 45-53
    • Kutzbach, M.1    Rauenbusch, E.2
  • 12
    • 0036010287 scopus 로고    scopus 로고
    • High-level secretory expression of penicillin amidase from Providencia rettgeri in Saccharomyces cerevisiae: purification and characterization
    • Ljubijankić, G., Gvozdenović, J., Ševo, M., and G. Degrassi (2002). High-level secretory expression of penicillin amidase from Providencia rettgeri in Saccharomyces cerevisiae: purification and characterization. Biotechnol. Progr. 18, 330-336.
    • (2002) Biotechnol. Progr. , vol.18 , pp. 330-336
    • Ljubijankić, G.1    Gvozdenović, J.2    Ševo, M.3    Degrassi, G.4
  • 13
    • 0033522191 scopus 로고    scopus 로고
    • Synthesis and secretion of Providencia rettgeri and Escherichia coli heterodimeric penicillin amidases in Saccharomyces cerevisiae
    • Ljubijankić, G., Storici, F., Glišin, V., and C. V. Bruschi (1999). Synthesis and secretion of Providencia rettgeri and Escherichia coli heterodimeric penicillin amidases in Saccharomyces cerevisiae. Gene 228, 225-232.
    • (1999) Gene , vol.228 , pp. 225-232
    • Ljubijankić, G.1    Storici, F.2    Glišin, V.3    Bruschi, C.V.4
  • 14
    • 0034769575 scopus 로고    scopus 로고
    • Stability enhancement of Escherichia coli penicillin G acylase by glycosylation with yeast manan
    • Masárová, J., Mislovičová, D., Gemeiner, P., and E. Michalková (2001). Stability enhancement of Escherichia coli penicillin G acylase by glycosylation with yeast manan. Biotechnol. Appl. Biochem. 34, 127-133.
    • (2001) Biotechnol. Appl. Biochem. , vol.34 , pp. 127-133
    • Masárová, J.1    Mislovičová, D.2    Gemeiner, P.3    Michalková, E.4
  • 15
    • 0032211383 scopus 로고    scopus 로고
    • Variation in N-linked oligosaccharide structures on heterologous proteins secreted by the methylotrophic yeast Pichia pastoris
    • Montesino, R., Garcia, R., Quintero, O., and J. A. Cremata (1998). Variation in N-linked oligosaccharide structures on heterologous proteins secreted by the methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 14, 197-207.
    • (1998) Protein Expr. Purif. , vol.14 , pp. 197-207
    • Montesino, R.1    Garcia, R.2    Quintero, O.3    Cremata, J.A.4
  • 17
    • 0026111220 scopus 로고
    • Studies on stabilization of amylase by covalent coupling to soluble polysaccharides
    • Srivastava, R. A. K. (1991). Studies on stabilization of amylase by covalent coupling to soluble polysaccharides. Enzyme Microb. Technol. 13, 164-171.
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 164-171
    • Srivastava, R.A.K.1
  • 18
    • 33645557358 scopus 로고    scopus 로고
    • Higghh-lleevveell production and covalent immobilization of Providencia rettgeri penicillin Gacylase (PAC) from recombinant Pichia pastoris for the development of a novel and stable biocatalyst of industrial applicability
    • Šenerović, L., Stanković, N., Spizo, P., Basso, A., Gardosi, L., Vasiljević, BBB., Ljubijankić, G., Tisminetzky, S., and G. Degrassi (2006). High-level production and covalent immobilization of Providencia rettgeri penicillin Gacylase (PAC) from recombinant Pichia pastoris for the development of a novel and stable biocatalyst of industrial applicability. Biotechnol. Bioeng. 93, 344-354.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 344-354
    • Šenerović, L.1    Stanković, N.2    Spizo, P.3    Basso, A.4    Gardosi, L.5    Vasiljević, B.B.B.6    Ljubijankić, G.7    Tisminetzky, S.8    Degrassi, G.9
  • 19
    • 0036231497 scopus 로고    scopus 로고
    • Production of glycosylated thermostable Providencia rettgeri penicillin G amidase in Pichia pastoris
    • Ševo, M., Degrassi, G., Skoko, N., Venturi, V., and G. Ljubijankić (2002). Production of glycosylated thermostable Providencia rettgeri penicillin G amidase in Pichia pastoris. FEMS Yeast Res. 1, 271-277.
    • (2002) FEMS Yeast Res , vol.1 , pp. 271-277
    • Ševo, M.1    Degrassi, G.2    Skoko, N.3    Venturi, V.4    Ljubijankić, G.5
  • 20
    • 0029990729 scopus 로고    scopus 로고
    • Secretion of a variant of human single-chain urokinase-type plasminogen activator without an N-glycosylation site in the methylotrophic yeast Pichia pastoris and characterization of the secreted product
    • Tsujikawa, M., Okabayashi, K., Morita, M., and T. Tanabe (1996). Secretion of a variant of human single-chain urokinase-type plasminogen activator without an N-glycosylation site in the methylotrophic yeast Pichia pastoris and characterization of the secreted product. Yeast 12, 541- 553.
    • (1996) Yeast , vol.12 , pp. 541-553
    • Tsujikawa, M.1    Okabayashi, K.2    Morita, M.3    Tanabe, T.4
  • 21


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.