메뉴 건너뛰기




Volumn 82, Issue 1, 2012, Pages 83-89

Production of recombinant Rhizopus oryzae lipase by the yeast Yarrowia lipolytica results in increased enzymatic thermostability

Author keywords

Rhizopus oryzae lipase (ROL); Thermostability; Yarrowia lipolytica

Indexed keywords

RECOMBINANT PROTEIN; TRIACYLGLYCEROL LIPASE;

EID: 84855425112     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.11.014     Document Type: Article
Times cited : (15)

References (43)
  • 3
    • 0032852741 scopus 로고    scopus 로고
    • Recombinant microbial lipases for biotechnological applications
    • DOI 10.1016/S0968-0896(99)00141-8, PII S0968089699001418
    • C. Schmidt-Dannert Recombinant microbial lipases for biotechnological applications Bioorg. Med. Chem. 7 1999 2123 2130 (Pubitemid 29486570)
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , Issue.10 , pp. 2123-2130
    • Schmidt-Dannert, C.1
  • 4
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization, and applications of lipases
    • DOI 10.1016/S0734-9750(01)00086-6, PII S0734975001000866
    • R. Sharma, Y. Chisti, and U.C. Banerjee Production, Purification, characterization, and applications of lipases Biotechnol. Adv. 19 2001 627 662 (Pubitemid 34212866)
    • (2001) Biotechnology Advances , vol.19 , Issue.8 , pp. 627-662
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 7
    • 0025721113 scopus 로고
    • Cloning, expression and characterization of a cDNA encoding a lipase from Rhizopus delemar
    • M.J. Haas, J. Allen, and T.R. Berka Cloning, expression and characterization of a cDNA encoding a lipase from Rhizopus delemar Gene 109 1991 107 113
    • (1991) Gene , vol.109 , pp. 107-113
    • Haas, M.J.1    Allen, J.2    Berka, T.R.3
  • 9
    • 0027582185 scopus 로고
    • Molecular characterization of an extracellular acid-resistant lipase produced by Rhizopus javanicus
    • W. Uyttenbroeck, D. Hendriks, G. Vriend, I. De Baere, L. Moens, and S. Scharpe Molecular characterization of an extracellular acid-resistant lipase produced by Rhizopus javanicus Biol. Chem. 374 1993 245 254
    • (1993) Biol. Chem. , vol.374 , pp. 245-254
    • Uyttenbroeck, W.1    Hendriks, D.2    Vriend, G.3    De Baere, I.4    Moens, L.5    Scharpe, S.6
  • 10
    • 0028448470 scopus 로고
    • Purification, characterization, and crystallization of two types of lipase from Rhizopus niveus
    • M. Kohno, W. Kugimiya, Y. Hashimoto, and Y. Morita Purification, characterization, and crystallization of two types of lipase from Rhizopus niveus Biosci. Biotechnol. Biochem. 58 1994 1007 1012 (Pubitemid 2118865)
    • (1994) Bioscience, Biotechnology and Biochemistry , vol.58 , Issue.6 , pp. 1007-1012
    • Kohno, M.1    Kugimiya, W.2    Hashimoto, Y.3    Morita, Y.4
  • 11
    • 13844278305 scopus 로고    scopus 로고
    • N-terminal peptide of Rhizopus oryzae lipase is important for its catalytic properties
    • DOI 10.1016/j.febslet.2004.12.068
    • A. Sayari, F. Frikha, N. Miled, H. Mtibaa, Y. Ben Ali, R. Verger, and Y. Gargouri N-terminal peptide of Rhizopus oryzae lipase is important for its catalytic properties FEBS Lett. 579 2005 976 982 (Pubitemid 40248656)
    • (2005) FEBS Letters , vol.579 , Issue.5 , pp. 976-982
    • Sayari, A.1    Frikha, F.2    Miled, N.3    Mtibaa, H.4    Ali, Y.B.5    Verger, R.6    Gargouri, Y.7
  • 12
    • 0033117564 scopus 로고    scopus 로고
    • High-level expression of Rhizopus niveus lipase in the yeast Saccharomyces cerevisiae and structural properties of the expressed enzyme
    • DOI 10.1006/prep.1999.1029
    • M. Kohno, M. Enatsu, M. Yoshiizumi, and W. Kugimiya High-level expression of Rhizopus niveus lipase in the yeast Saccharomyces cerevisiae and structural properties of the expressed enzyme Protein Expr. Purif. 15 1999 327 335 (Pubitemid 29326380)
    • (1999) Protein Expression and Purification , vol.15 , Issue.3 , pp. 327-335
    • Kohno, M.1    Enatsu, M.2    Yoshiizumi, M.3    Kugimiya, W.4
  • 14
    • 0029744652 scopus 로고    scopus 로고
    • Analysis of the catalytic mechanism of a fungal lipase using computer-aided design and structural mutants
    • H.D. Beer, G. Wohlfahrt, J.E. McCarthy, D. Schomburg, and R.D. Schmid Analysis of the catalytic mechanism of a fungal lipase using computer-aided design and structural mutants Protein Eng. 9 1996 507 517 (Pubitemid 26261292)
    • (1996) Protein Engineering , vol.9 , Issue.6 , pp. 507-517
    • Beer, H.D.1    Wohlfahrt, G.2    McCarthy, J.E.G.3    Schomburg, D.4    Schmid, R.D.5
  • 15
    • 1842530437 scopus 로고    scopus 로고
    • Expression of a Rhizopus oryzae lipase in Pichia pastoris under control of the nitrogen source-regulated formaldehyde dehydrogenase promoter
    • DOI 10.1016/j.jbiotec.2003.10.029, PII S016816560400029X
    • D. Resina, A. Serrano, F. Valero, and P. Ferrer Expression of a Rhizopus oryzae lipase in Pichia pastoris under control of the nitrogen source-regulated formaldehyde dehydrogenase promoter J. Biotechnol. 109 2004 103 113 (Pubitemid 38452575)
    • (2004) Journal of Biotechnology , vol.109 , Issue.1-2 , pp. 103-113
    • Resina, D.1    Serrano, A.2    Valero, F.3    Ferrer, P.4
  • 16
    • 0344404412 scopus 로고    scopus 로고
    • Functional expression of Rhizopus oryzae lipase in Pichia pastoris: High-level production and some properties
    • DOI 10.1016/S0168-1656(98)00142-4, PII S0168165698001424
    • S. Minning, C. Schmidt-Dannert, and R.D. Schmid Functional expression of Rhizopus oryzae lipase in Pichia pastoris: high-level production and some properties J. Biotechnol. 66 1998 147 156 (Pubitemid 28544956)
    • (1998) Journal of Biotechnology , vol.66 , Issue.2-3 , pp. 147-156
    • Minning, S.1    Schmidt-Dannert, C.2    Schmid, R.D.3
  • 17
    • 70350547284 scopus 로고    scopus 로고
    • Engineering of bottlenecks in Rhizopus oryzae lipase production in Pichia pastoris using the nitrogen source-regulated FLD1 promoter
    • D. Resina, M. Maurer, O. Cos, C. Arnau, M. Carnicer, H. Marx, B. Gasser, F. Valero, D. Mattanovich, and P. Ferrer Engineering of bottlenecks in Rhizopus oryzae lipase production in Pichia pastoris using the nitrogen source-regulated FLD1 promoter N Biotechnol. 25 2009 396 403
    • (2009) N Biotechnol. , vol.25 , pp. 396-403
    • Resina, D.1    Maurer, M.2    Cos, O.3    Arnau, C.4    Carnicer, M.5    Marx, H.6    Gasser, B.7    Valero, F.8    Mattanovich, D.9    Ferrer, P.10
  • 18
    • 0032739524 scopus 로고    scopus 로고
    • Independent production of two molecular forms of a recombinant Rhizopus oryzae lipase by KEX2-engineered strains of Saccharomyces cerevisiae
    • DOI 10.1007/s002530051556
    • S. Takahashi, M. Ueda, and A. Tanaka Independent production of two molecular forms of a recombinant Rhizopus oryzae lipase by KEX2-engineered strains of Saccharomyces cerevisiae Appl. Microbiol. Biotechnol. 52 1999 534 540 (Pubitemid 29513333)
    • (1999) Applied Microbiology and Biotechnology , vol.52 , Issue.4 , pp. 534-540
    • Takahashi, S.1    Ueda, M.2    Tanaka, A.3
  • 19
    • 46149109460 scopus 로고    scopus 로고
    • Role of N-terminal 28-amino-acid region of Rhizopus oryzae lipase in directing proteins to secretory pathway of Aspergillus oryzae
    • S. Hama, S. Tamalampudi, N. Shindo, T. Numata, H. Yamaji, H. Fukuda, and A. Kondo Role of N-terminal 28-amino-acid region of Rhizopus oryzae lipase in directing proteins to secretory pathway of Aspergillus oryzae Appl. Microbiol. Biotechnol. 79 2008 1009 1018
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 1009-1018
    • Hama, S.1    Tamalampudi, S.2    Shindo, N.3    Numata, T.4    Yamaji, H.5    Fukuda, H.6    Kondo, A.7
  • 20
    • 0029824790 scopus 로고    scopus 로고
    • The folding and activity of the extracellular lipase of Rhizopus oryzae are modulated by a prosequence
    • H.D. Beer, G. Wohlfahrt, R.D. Schmid, and J.E. McCarthy The folding and activity of the extracellular lipase of Rhizopus oryzae are modulated by a prosequence Biochem. J. 319 Pt. 2 1996 351 359
    • (1996) Biochem. J. , vol.319 , Issue.PART 2 , pp. 351-359
    • Beer, H.D.1    Wohlfahrt, G.2    Schmid, R.D.3    McCarthy, J.E.4
  • 21
    • 0035003618 scopus 로고    scopus 로고
    • Function of the prosequence for in vivo folding and secretion of active Rhizopus oryzae lipase in Saccharomyces cerevisiae
    • DOI 10.1007/s002530000537
    • S. Takahashi, M. Ueda, and A. Tanaka Function of the prosequence for in vivo folding and secretion of active Rhizopus oryzae lipase in Saccharomyces cerevisiae Appl. Microbiol. Biotechnol. 55 2001 454 462 (Pubitemid 32417844)
    • (2001) Applied Microbiology and Biotechnology , vol.55 , Issue.4 , pp. 454-462
    • Takahashi, S.1    Ueda, M.2    Tanaka, A.3
  • 23
    • 0034714127 scopus 로고    scopus 로고
    • Thermal stability of Rhizopus niveus lipase expressed in a kex2 mutant yeast
    • M. Kohno, M. Enatsu, R. Takee, and W. Kugimiya Thermal stability of Rhizopus niveus lipase expressed in a kex2 mutant yeast J. Biotechnol. 81 2000 141 150
    • (2000) J. Biotechnol. , vol.81 , pp. 141-150
    • Kohno, M.1    Enatsu, M.2    Takee, R.3    Kugimiya, W.4
  • 24
    • 0035907159 scopus 로고    scopus 로고
    • Improvement of the optimum temperature of lipase activity for Rhizopus niveus by random mutagenesis and its structural interpretation
    • DOI 10.1016/S0168-1656(01)00243-7, PII S0168165601002437
    • M. Kohno, M. Enatsu, J. Funatsu, M. Yoshiizumi, and W. Kugimiya Improvement of the optimum temperature of lipase activity for Rhizopus niveus by random mutagenesis and its structural interpretation J. Biotechnol. 87 2001 203 210 (Pubitemid 32378754)
    • (2001) Journal of Biotechnology , vol.87 , Issue.3 , pp. 203-210
    • Kohno, M.1    Enatsu, M.2    Funatsu, J.3    Yoshiizumi, M.4    Kugimiya, W.5
  • 25
    • 0034000128 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit
    • DOI 10.1016/S0141-0229(99)00173-8, PII S0141022999001738
    • A. Hiol, M.D. Jonzo, N. Rugani, D. Druet, L. Sarda, and L.C. Comeau Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit Enzyme Microb. Technol. 26 2000 421 430 (Pubitemid 30122411)
    • (2000) Enzyme and Microbial Technology , vol.26 , Issue.5-6 , pp. 421-430
    • Hiol, A.1    Jonzo, M.D.2    Rugani, N.3    Druet, D.4    Sarda, L.5    Comeau, L.C.6
  • 26
    • 1842530397 scopus 로고    scopus 로고
    • Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: A review
    • DOI 10.1016/j.jbiotec.2003.10.027, PII S0168165604000264
    • C. Madzak, C. Gaillardin, and J.M. Beckerich Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review J. Biotechnol. 109 2004 63 81 (Pubitemid 38452572)
    • (2004) Journal of Biotechnology , vol.109 , Issue.1-2 , pp. 63-81
    • Madzak, C.1    Gaillardin, C.2    Beckerich, J.-M.3
  • 27
    • 0028287703 scopus 로고
    • Multiple-copy integration in the yeast Yarrowia lipolytica
    • DOI 10.1007/BF00326302
    • M.T. Le Dall, J.M. Nicaud, and C. Gaillardin Multiple-copy integration in the yeast Yarrowia lipolytica Curr. Genet. 26 1994 38 44 (Pubitemid 24192847)
    • (1994) Current Genetics , vol.26 , Issue.1 , pp. 38-44
    • Le Dall, M.-T.1    Nicaud, J.-M.2    Gaillardin, C.3
  • 28
    • 0344002683 scopus 로고    scopus 로고
    • Strong hybrid promoters and integrative expression/secretion vectors for quasi-constitutive expression of heterologous proteins in the yeast Yarrowia lipolytica
    • C. Madzak, B. Treton, and S. Blanchin-Roland Strong hybrid promoters and integrative expression/secretion vectors for quasi-constitutive expression of heterologous proteins in the yeast Yarrowia lipolytica J. Mol. Microbiol. Biotechnol. 2 2000 207 216 (Pubitemid 30218822)
    • (2000) Journal of Molecular Microbiology and Biotechnology , vol.2 , Issue.2 , pp. 207-216
    • Madzak, C.1    Treton, B.2    Blanchin-Roland, S.3
  • 29
  • 33
    • 0028012040 scopus 로고
    • Two upstream activation sequences control the expression of the XPR2 gene in the yeast Yarrowia lipolytica
    • S. Blanchin-Roland, R.R. Cordero Otero, and C. Gaillardin Two upstream activation sequences control the expression of the XPR2 gene in the yeast Yarrowia lipolytica Mol. Cell. Biol. 14 1994 327 338
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 327-338
    • Blanchin-Roland, S.1    Cordero Otero, R.R.2    Gaillardin, C.3
  • 34
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • E. Alani, L. Cao, and N. Kleckner A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains Genetics 116 1987 541 545
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 35
    • 85032069466 scopus 로고    scopus 로고
    • A simple method for extraction of fungal genomic DNA
    • T.H. Al-Samarrai, and J. Schmid A simple method for extraction of fungal genomic DNA Lett. Appl. Microbiol. 30 2000 53 56 (Pubitemid 30128904)
    • (2000) Letters in Applied Microbiology , vol.30 , Issue.1 , pp. 53-56
    • Al-Samarrai, T.H.1    Schmid, J.2
  • 37
    • 79960733229 scopus 로고    scopus 로고
    • Efficient cell surface display of Lip2 lipase using C-domains of glycosylphosphatidylinositol-anchored cell wall proteins of Yarrowia lipolytica
    • E.Y. Yuzbasheva, T.V. Yuzbashev, I.A. Laptev, T.K. Konstantinova, and S.P. Sineoky Efficient cell surface display of Lip2 lipase using C-domains of glycosylphosphatidylinositol-anchored cell wall proteins of Yarrowia lipolytica Appl. Microbiol. Biotechnol. 91 2011 645 654
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 645-654
    • Yuzbasheva, E.Y.1    Yuzbashev, T.V.2    Laptev, I.A.3    Konstantinova, T.K.4    Sineoky, S.P.5
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0032898514 scopus 로고    scopus 로고
    • Functional analysis of upstream regulating regions from the Yarrowia lipolytica XPR2 promoter
    • C. Madzak, S. Blanchin-Roland, R.R. Cordero Otero, and C. Gaillardin Functional analysis of upstream regulating regions from the Yarrowia lipolytica XPR2 promoter Microbiology 145 Pt. 1 1999 75 87 (Pubitemid 29043579)
    • (1999) Microbiology , vol.145 , Issue.1 , pp. 75-87
    • Madzak, C.1    Blanchin-Roland, S.2    Cordero Otero, R.R.3    Gaillardin, C.4
  • 43
    • 0028012081 scopus 로고
    • Cloning, nucleotide sequence and functions of XPR6, which codes for a dibasic processing endoprotease from the yeast Yarrowia lipolytica
    • C.S. Enderlin, and D.M. Ogrydziak Cloning, nucleotide sequence and functions of XPR6, which codes for a dibasic processing endoprotease from the yeast Yarrowia lipolytica Yeast 10 1994 67 79 (Pubitemid 24052950)
    • (1994) Yeast , vol.10 , Issue.1 , pp. 67-79
    • Enderlin, C.S.1    Ogrydziak, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.