메뉴 건너뛰기




Volumn 54, Issue 3, 2006, Pages 815-822

Codon optimization of Candida rugosa lip1 gene for improving expression in Pichia pastoris and biochemical characterization of the purified recombinant LIP1 lipase

Author keywords

Candida rugosa lipase; Codon optimization; Isoforms; Pichia pastoris

Indexed keywords

FUNGAL DNA; ISOENZYME; RECOMBINANT PROTEIN; TRIACYLGLYCEROL LIPASE;

EID: 33244490497     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1175/JAS3661.1     Document Type: Article
Times cited : (75)

References (30)
  • 1
    • 0002425020 scopus 로고
    • Multiple forms and functions of Candida rugosa lipase
    • Chang, R. C.; Chou, S. J.; Shaw, J. F. Multiple forms and functions of Candida rugosa lipase. Biotechnol. Appl. Biochem. 1994, 19, 93-97.
    • (1994) Biotechnol. Appl. Biochem. , vol.19 , pp. 93-97
    • Chang, R.C.1    Chou, S.J.2    Shaw, J.F.3
  • 2
    • 0036714663 scopus 로고    scopus 로고
    • Multiple mutagenesis of non-universal serine codons of the Candida rugosa LIP2 gene and biochemical characterization of purified recombinant LIP2 lipase overexpressed in Pichia pastoris
    • Lee, G. C.; Lee, L. C.; Sava, V.; Shaw, J. F. Multiple mutagenesis of non-universal serine codons of the Candida rugosa LIP2 gene and biochemical characterization of purified recombinant LIP2 lipase overexpressed in Pichia pastoris. Biochem. J. 2002, 366, 603-611.
    • (2002) Biochem. J. , vol.366 , pp. 603-611
    • Lee, G.C.1    Lee, L.C.2    Sava, V.3    Shaw, J.F.4
  • 3
    • 5644247368 scopus 로고    scopus 로고
    • Protein engineering and application of Candida rugosa lipase isoforms
    • Akoh, C. C.; Lee, G. C.; Shaw, J. F. Protein engineering and application of Candida rugosa lipase isoforms. Lipids 2004, 39, 513-526.
    • (2004) Lipids , vol.39 , pp. 513-526
    • Akoh, C.C.1    Lee, G.C.2    Shaw, J.F.3
  • 7
    • 0024805184 scopus 로고
    • Characterization of three distinct forms of lipolytic enzymes in a commercial Candida lipase
    • Shaw, J. F.; Chang, C. H. Characterization of three distinct forms of lipolytic enzymes in a commercial Candida lipase. Biotechnol. Lett. 1989, 11, 779-784.
    • (1989) Biotechnol. Lett. , vol.11 , pp. 779-784
    • Shaw, J.F.1    Chang, C.H.2
  • 10
    • 84998237581 scopus 로고
    • Oxidation of methanol by the yeast, Pichia pastoris, purification and properties of the alcohol oxidase
    • Couderc, R.; Baratti, J. Oxidation of methanol by the yeast, Pichia pastoris, purification and properties of the alcohol oxidase. Agric. Biol. Chem. 1980, 44, 2279-2289.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 2279-2289
    • Couderc, R.1    Baratti, J.2
  • 11
    • 0002721559 scopus 로고
    • Development of the methylotrophic yeast, Pichia pastoris, as a host system for the production of foreign protein
    • Pierce, G., Eds.; Elsevier Science: Amsterdam, The Netherlands
    • Cregg, J. M.; Madden, K. R. Development of the methylotrophic yeast, Pichia pastoris, as a host system for the production of foreign protein. In Development in Industrial Microbiology; Pierce, G., Eds.; Elsevier Science: Amsterdam, The Netherlands, 1988; pp 33-41.
    • (1988) Development in Industrial Microbiology , pp. 33-41
    • Cregg, J.M.1    Madden, K.R.2
  • 12
  • 13
    • 0034537455 scopus 로고    scopus 로고
    • Heterologous protein production in methylotrophic yeasts
    • Gellissen, G. Heterologous protein production in methylotrophic yeasts. Appl. Microbiol. Biotechnol. 2000, 54, 741-750.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 741-750
    • Gellissen, G.1
  • 15
    • 17844402756 scopus 로고    scopus 로고
    • Multiple mutagenesis of the Candida rugosa LIP1 gene and optimum production of recombinant LIP1 expressed in Pichia pastrois
    • Chang, S. W.; Shieh, C. J.; Lee, G. C.; Shaw, J. F. Multiple mutagenesis of the Candida rugosa LIP1 gene and optimum production of recombinant LIP1 expressed in Pichia pastrois. Appl. Microbiol. Biotechnol. 2005, 67, 215-224.
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , pp. 215-224
    • Chang, S.W.1    Shieh, C.J.2    Lee, G.C.3    Shaw, J.F.4
  • 16
    • 0034056247 scopus 로고    scopus 로고
    • Fermentation, purification and efficacy of a recombinant vaccine candidate against botulinum neurotoxin type F from Pichia pastoris
    • Byrne, M. P.; Titball, R. W.; Holley, J.; Smith, L. A. Fermentation, purification and efficacy of a recombinant vaccine candidate against botulinum neurotoxin type F from Pichia pastoris. Protein Expression Purif. 2000, 18, 327-337.
    • (2000) Protein Expression Purif. , vol.18 , pp. 327-337
    • Byrne, M.P.1    Titball, R.W.2    Holley, J.3    Smith, L.A.4
  • 17
    • 0025758727 scopus 로고
    • Expression of tetanus toxin fragment C in yeast: Gene synthesis is required to eliminate fortuitous polyadenylation sites in AT-rich DNA
    • Romanos, M. A.; Makoff, A. J.; Fairweather, N. F.; Beesley, K. M.; Slater, D. E.; Rayment, F. B.; Rayne, M. M.; Clare, J. J. Expression of tetanus toxin fragment C in yeast: gene synthesis is required to eliminate fortuitous polyadenylation sites in AT-rich DNA. Nucleic Acids Res. 1991, 19, 1461-1467.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1461-1467
    • Romanos, M.A.1    Makoff, A.J.2    Fairweather, N.F.3    Beesley, K.M.4    Slater, D.E.5    Rayment, F.B.6    Rayne, M.M.7    Clare, J.J.8
  • 18
    • 0033727599 scopus 로고    scopus 로고
    • High-level periplasmic expression in Escherichia coli using a eukaryotic signal peptide: Importance of codon usage at the 5′ end of the coding sequence
    • Humphreys, D. P.; Sehdev, M.; Chapman, A. P.; Ganesh, R.; Smith, B. J.; King, L. M.; Glover, D. J.; Reeks, D. G.; Stephens, P. E. High-level periplasmic expression in Escherichia coli using a eukaryotic signal peptide: importance of codon usage at the 5′ end of the coding sequence. Protein Expression Purif. 2000, 20, 252-264.
    • (2000) Protein Expression Purif. , vol.20 , pp. 252-264
    • Humphreys, D.P.1    Sehdev, M.2    Chapman, A.P.3    Ganesh, R.4    Smith, B.J.5    King, L.M.6    Glover, D.J.7    Reeks, D.G.8    Stephens, P.E.9
  • 19
    • 0034993922 scopus 로고    scopus 로고
    • High-level expression in mammalian cells of recombinant house dust mite allergen ProDer p 1 with optimized codon usage
    • Massaer, M.; Mazzu, P.; Haumont, M.; Magi, M.; Daminet, V.; Bollen, A.; Jacquet, A. High-level expression in mammalian cells of recombinant house dust mite allergen ProDer p 1 with optimized codon usage. Int. Arch. Allergy Immunol. 2001, 125, 32-43.
    • (2001) Int. Arch. Allergy Immunol. , vol.125 , pp. 32-43
    • Massaer, M.1    Mazzu, P.2    Haumont, M.3    Magi, M.4    Daminet, V.5    Bollen, A.6    Jacquet, A.7
  • 20
    • 0034283706 scopus 로고    scopus 로고
    • Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus Trichoderma reesei
    • Te'o, V. S.; Cziferszky, A. E.; Bergquist, P. L.; Nevalainen, K. M. Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus Trichoderma reesei. FEMS Microbiol. Lett. 2000, 190, 13-19.
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 13-19
    • Te'O, V.S.1    Cziferszky, A.E.2    Bergquist, P.L.3    Nevalainen, K.M.4
  • 21
    • 0034969734 scopus 로고    scopus 로고
    • Codon optimization markedly improves doxycycline regulated gene expression in the mouse heart
    • Valencik, M. L.; McDonald, J. A. Codon optimization markedly improves doxycycline regulated gene expression in the mouse heart. Transgenic Res. 2001, 10, 269-275.
    • (2001) Transgenic Res. , vol.10 , pp. 269-275
    • Valencik, M.L.1    McDonald, J.A.2
  • 22
    • 0031777548 scopus 로고    scopus 로고
    • Design, total synthesis, and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase
    • Brocca, S.; Schmidt-Dannert, C.; Lotti, M.; Alberghina, L.; Schmid, R. D. Design, total synthesis, and functional overexpression of the Candida rugosa lip1 gene coding for a major industrial lipase. Protein Sci. 1998, 7, 1415-1422.
    • (1998) Protein Sci. , vol.7 , pp. 1415-1422
    • Brocca, S.1    Schmidt-Dannert, C.2    Lotti, M.3    Alberghina, L.4    Schmid, R.D.5
  • 23
    • 0036425270 scopus 로고    scopus 로고
    • Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast
    • Sinclair, G.; Choy, F. Y. M. Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast. Pichia pastoris. Protein Expression Purif. 2002, 26, 96-105.
    • (2002) Pichia Pastoris. Protein Expression Purif. , vol.26 , pp. 96-105
    • Sinclair, G.1    Choy, F.Y.M.2
  • 24
    • 0031579445 scopus 로고    scopus 로고
    • Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter
    • Waterham, H. R.; Digan, M. E.; Koutz, P. J.; Lair, S. V.; Cregg, J. M. Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter. Gene 1997, 186, 37-44.
    • (1997) Gene , vol.186 , pp. 37-44
    • Waterham, H.R.1    Digan, M.E.2    Koutz, P.J.3    Lair, S.V.4    Cregg, J.M.5
  • 26
    • 5044236206 scopus 로고    scopus 로고
    • Reactivity of pure Candida rugosa lipase isoenzymes (Lip1 Lip2, and Lip3) in aqueous and organic media. Influence of the isoenzymatic profile on the lipase performance in organic media
    • López, N.; Pernas, M. A.; Pastrana, L. M.; Sánchez, A.; Valero, F.; Rúa, M. L. Reactivity of pure Candida rugosa lipase isoenzymes (Lip1 Lip2, and Lip3) in aqueous and organic media. Influence of the isoenzymatic profile on the lipase performance in organic media. Biotechnol. Prog. 2004, 20, 65-73.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 65-73
    • López, N.1    Pernas, M.A.2    Pastrana, L.M.3    Sánchez, A.4    Valero, F.5    Rúa, M.L.6
  • 27
    • 33244470227 scopus 로고    scopus 로고
    • Cheese ripening: Supporting the natural processes
    • Uhlig, H., Ed.; Wiley: Mississauga, Canada
    • Uhlig, H. Cheese ripening: supporting the natural processes. In Industrial Enzymes and Their Application; Uhlig, H., Ed.; Wiley: Mississauga, Canada, 1998; pp 328-329.
    • (1998) Industrial Enzymes and Their Application , pp. 328-329
    • Uhlig, H.1
  • 29
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • Jaeger, K.-E.; Reetz, M. T. Microbial lipases form versatile tools for biotechnology. Trends Biotechnol. 1998, 16, 396-403.
    • (1998) Trends Biotechnol. , vol.16 , pp. 396-403
    • Jaeger, K.-E.1    Reetz, M.T.2
  • 30
    • 0003388452 scopus 로고
    • Kinetics of lipolysis
    • Academic Press: New York
    • Brockerhoff, H.; Jensen, R. G., III. Kinetics of lipolysis. In Lipolytic Enzymes; Academic Press: New York, 1974; pp 10-24.
    • (1974) Lipolytic Enzymes , pp. 10-24
    • Brockerhoff, H.1    Jensen III, R.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.