메뉴 건너뛰기




Volumn 16, Issue 6, 2011, Pages 1196-1200

Enhancing functional expression of β-glucosidase in Pichia pastoris by Co-expressing protein disulfide isomerase

Author keywords

Fermentation optimization; Pichia pastoris; Protein disulfide isomerase; Protein folding; Specific activity; glucosidase

Indexed keywords

COBALT COMPOUNDS; COVALENT BONDS; ENZYME ACTIVITY; FERMENTATION; PROTEIN FOLDING; SULFUR COMPOUNDS; YEAST;

EID: 84862956348     PISSN: 12268372     EISSN: 19763816     Source Type: Journal    
DOI: 10.1007/s12257-011-0136-1     Document Type: Article
Times cited : (21)

References (22)
  • 2
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • DOI 10.1016/S0168-6445(99)00029-7, PII S0168644599000297
    • Cereghino, J. L. and J. M. Cregg (2000) Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24:45-66. (Pubitemid 30047114)
    • (2000) FEMS Microbiology Reviews , vol.24 , Issue.1 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 4
    • 33747174562 scopus 로고    scopus 로고
    • Enhanced secretion of heterologous proteins in Pichia pastoris following overexpression of Saccharomyces cerevisiae chaperone proteins
    • DOI 10.1021/bp060019r
    • Zhang, W. (2006) Enhanced secretion of heterologous proteins in Pichia pastoris following overexpression of Saccharomyces cerevisiae chaperone proteins. Biotechnol. Prog. 22:1090-1095. (Pubitemid 44230696)
    • (2006) Biotechnology Progress , vol.22 , Issue.4 , pp. 1090-1095
    • Zhang, W.1    Zhao, H.-L.2    Xue, C.3    Xiong, X.-H.4    Yao, X.-Q.5    Li, X.-Y.6    Chen, H.-P.7    Liu, Z.-M.8
  • 5
    • 0442309687 scopus 로고    scopus 로고
    • Effects of Gene Dosage, Promoters, and Substrates on Unfolded Protein Stress of Recombinant Pichia pastoris
    • DOI 10.1002/bit.10904
    • Hohenblum, H. (2004) Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris. Biotechnol. Bioeng. 85:367-375. (Pubitemid 38186091)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.4 , pp. 367-375
    • Hohenblum, H.1    Gasser, B.2    Maurer, M.3    Borth, N.4    Mattanovich, D.5
  • 6
    • 0034487424 scopus 로고    scopus 로고
    • Roles of molecular chaperones in cytoplasmic protein folding
    • DOI 10.1006/scdb.1999.0347
    • Agashe, V. R. and F. U. Hartl (2000) Roles of molecular chaperones in cytoplasmic protein folding. Semin. Cell Dev. Biol. 11:15-25. (Pubitemid 32096090)
    • (2000) Seminars in Cell and Developmental Biology , vol.11 , Issue.1 , pp. 15-25
    • Agashe, V.R.1    Hartl, F.-U.2
  • 7
    • 77954518631 scopus 로고    scopus 로고
    • Effect of coexpressing protein disulfide isomerase on expression of IFNβ-HSA fusion protein in Pichia pastoris
    • Qu Lin, L. J.-Y. and Z. Qi (2010) Effect of coexpressing protein disulfide isomerase on expression of IFNβ-HSA fusion protein in Pichia pastoris. Chin. J. Biologicals. 23:346-349.
    • (2010) Chin. J. Biologicals. , vol.23 , pp. 346-349
    • Qu Lin, L.J.-Y.1    Qi, Z.2
  • 8
    • 24044505375 scopus 로고    scopus 로고
    • Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding
    • DOI 10.1016/j.ymben.2005.04.002, PII S1096717605000431
    • Xu, P. (2005) Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding. Metab. Eng. 7:269-279. (Pubitemid 41225444)
    • (2005) Metabolic Engineering , vol.7 , Issue.4 , pp. 269-279
    • Xu, P.1    Raden, D.2    Doyle III, F.J.3    Robinson, A.S.4
  • 9
    • 34247257335 scopus 로고    scopus 로고
    • PDI improves secretion of redox-inactive β-glucosidase
    • DOI 10.1021/bp060287p
    • Powers, S. L. and A. S. Robinson (2007) PDI improves secretion of redox-inactive beta-glucosidase. Biotechnol. Prog. 23:364-369. (Pubitemid 46626310)
    • (2007) Biotechnology Progress , vol.23 , Issue.2 , pp. 364-369
    • Powers, S.L.1    Robinson, A.S.2
  • 10
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott, M. L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. American Chem. Society 90:1171-1202.
    • (1990) American Chem. Society , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 11
    • 0029921130 scopus 로고    scopus 로고
    • Bioconversion of forest products industry waste cellulosics to fuel ethanol: A review
    • DOI 10.1016/0960-8524(95)00122-0
    • Duff, S. J. B. and W. D. Murray. (1996) Bioconversion of forest products industry waste cellulosics to fuel ethanol: A review. Bioresource Technol. 55:1-33. (Pubitemid 26139082)
    • (1996) Bioresource Technology , vol.55 , Issue.1 , pp. 1-33
    • Duff, S.J.B.1    Murray, W.D.2
  • 12
    • 0033199427 scopus 로고    scopus 로고
    • Enzymes, energy, and the environment: A strategic perspective on the U.S. Department of Energy's Research and Development Activities for Bioethanol
    • DOI 10.1021/bp990110d
    • Sheehan, J. and M. Himmel (1999) Enzymes, energy, and the environment: A strategic perspective on the US Department of Energy's research and development activities for bioethanol. Biotechnol. Prog. 15:817-827. (Pubitemid 29475620)
    • (1999) Biotechnology Progress , vol.15 , Issue.5 , pp. 817-827
    • Sheehan, J.1    Himmel, M.2
  • 13
    • 0025002206 scopus 로고
    • Alkyl-β-glucoside synthesis in a water-organic two-phase system
    • Vulfson, E. N., R. Patel, and B. Law (1990) Alkyl glucoside synthesis in a water-organic two-phase system. Biotechnol. Lett. 12:397-402. (Pubitemid 20331233)
    • (1990) Biotechnology Letters , vol.12 , Issue.6 , pp. 397-402
    • Vulfson, E.N.1    Patel, R.2    Law, B.A.3
  • 14
    • 17744362070 scopus 로고    scopus 로고
    • Transglusidic reactions of the Aspergillus niger Family 3 β-glucosidase Qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH
    • Heather, F. and R. E. H. Seidle (2005) Transglusidic reactions of the Aspergillus niger Family 3 β-glucosidase Qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH. Arch. Biochem. Biophys. 436:254-264.
    • (2005) Arch. Biochem. Biophys. , vol.436 , pp. 254-264
    • Heather, F.1    Seidle, R.E.H.2
  • 15
    • 70349243928 scopus 로고    scopus 로고
    • Production of gentiooligosaccharide by recombinant β-glucosidase
    • Lingling Liu, S. Z. (2009) Production of gentiooligosaccharide by recombinant β-glucosidase. Acta Mcrobiol. Sinica. 49:597-602.
    • (2009) Acta Mcrobiol. Sinica. , vol.49 , pp. 597-602
    • Lingling Liu, S.Z.1
  • 17
    • 0842300391 scopus 로고    scopus 로고
    • Protein Disulfide Isomerase, but Not Binding Protein, Overexpression Enhances Secretion of a Non-Disulfide-Bonded Protein in Yeast
    • DOI 10.1002/bit.10853
    • Jason, D., B. C. T. Smith, and A. S. Robinson (2003) Protein disulfide isomerase. But not binding protein, overexpression enhances secretion of a Non-disulfide-bonded protein in yeast. Biotechnol. Bioeng. 85:340-350. (Pubitemid 38182227)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.3 , pp. 340-350
    • Smith, J.D.1    Tang, B.C.2    Robinson, A.S.3
  • 19
    • 33748097812 scopus 로고    scopus 로고
    • Interactions between yeast, oxygen and polyphenols during alcoholic fermentations: Practical implications
    • DOI 10.1016/j.lwt.2005.11.005, PII S002364380500246X
    • Salmon, J.-M. (2006) Interactions between yeast, oxygen and polyphenols during alcoholic fermentations: Practical implications. Food Sci. Technol. 39:959-965. (Pubitemid 44304446)
    • (2006) LWT - Food Science and Technology , vol.39 , Issue.9 , pp. 959-965
    • Salmon, J.-M.1
  • 20
    • 46549088173 scopus 로고    scopus 로고
    • Reactive oxygen species and yeast apoptosis
    • Perrone, G. G., S. X. Tan, and I. W. Dawes (2008) Reactive oxygen species and yeast apoptosis. Biochim. Biophys. Acta 1783:1354-1368.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1354-1368
    • Perrone, G.G.1    Tan, S.X.2    Dawes, I.W.3
  • 21
    • 71549114849 scopus 로고    scopus 로고
    • Enhancement of cell viability and alkaline polygalacturonate lyase production by sorbitol co-feeding with methanol in Pichia pastoris fermentation
    • Wang, Z. (2009) Enhancement of cell viability and alkaline polygalacturonate lyase production by sorbitol co-feeding with methanol in Pichia pastoris fermentation. Bioresour. Technol. 101:1318-1323.
    • (2009) Bioresour. Technol. , vol.101 , pp. 1318-1323
    • Wang, Z.1
  • 22
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Joan Lin Cereghino, J. M. C. (2000) Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24:45-66.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Joan Lin Cereghino, J.M.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.