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Volumn 11, Issue , 2012, Pages

Enhanced thermostability of a Rhizopus chinensis lipase by in vivo recombination in Pichia pastoris

Author keywords

Directed evolution; Lipase; Mutant library construction; Pichia pastoris; Thermostability

Indexed keywords

TRIACYLGLYCEROL LIPASE;

EID: 84864518283     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-11-102     Document Type: Article
Times cited : (52)

References (49)
  • 1
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization, and applications of lipases
    • Sharma R, Chisti Y, Banerjee UC. Production, purification, characterization, and applications of lipases. Biotechnol Adv 2001, 19:627-662.
    • (2001) Biotechnol Adv , vol.19 , pp. 627-662
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 2
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • Hasan F, Shah AA, Hameed A. Industrial applications of microbial lipases. Enzyme Microb Technol 2006, 39:235-251.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 235-251
    • Hasan, F.1    Shah, A.A.2    Hameed, A.3
  • 4
    • 84907036382 scopus 로고
    • Lipase-catalyzed reactions for modification of fats and other lipids
    • Mukherjee KD. Lipase-catalyzed reactions for modification of fats and other lipids. Biocatal Biotransfor 1990, 3:277-293.
    • (1990) Biocatal Biotransfor , vol.3 , pp. 277-293
    • Mukherjee, K.D.1
  • 5
    • 0031162606 scopus 로고    scopus 로고
    • Applications of lipase
    • Gandhi NN. Applications of lipase. J Am Oil Chem Soc 1997, 74:621-634.
    • (1997) J Am Oil Chem Soc , vol.74 , pp. 621-634
    • Gandhi, N.N.1
  • 6
    • 0034788695 scopus 로고    scopus 로고
    • Enhancement of apparent thermostability of lipase from Rhizopus sp. by the treatment with a microbial transglutaminase
    • Kamiya N, Ogawa T, Nagamune T. Enhancement of apparent thermostability of lipase from Rhizopus sp. by the treatment with a microbial transglutaminase. Biotechnol Lett 2001, 23:1629-1632.
    • (2001) Biotechnol Lett , vol.23 , pp. 1629-1632
    • Kamiya, N.1    Ogawa, T.2    Nagamune, T.3
  • 7
    • 29644442942 scopus 로고    scopus 로고
    • Secretion of pro-and mature Rhizopus arrhizus lipases by Pichia pastoris and properties of the proteins
    • Niu W, Li Z, Tan T. Secretion of pro-and mature Rhizopus arrhizus lipases by Pichia pastoris and properties of the proteins. Mol Biotechnol 2006, 32:73-81.
    • (2006) Mol Biotechnol , vol.32 , pp. 73-81
    • Niu, W.1    Li, Z.2    Tan, T.3
  • 8
    • 0034000128 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit
    • Hiol A, Jonzo MD, Rugani N, Druet D, Sarda L, Comeau LC. Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit. Enzyme Microb Technol 2000, 26:421-430.
    • (2000) Enzyme Microb Technol , vol.26 , pp. 421-430
    • Hiol, A.1    Jonzo, M.D.2    Rugani, N.3    Druet, D.4    Sarda, L.5    Comeau, L.C.6
  • 9
    • 0344074507 scopus 로고    scopus 로고
    • Cloning, expression, characterization and role of the leader sequence of a lipase from Rhizopus oryzae
    • Beer HD, McCarthy JEG, Bornscheuer UT, Schmid RD. Cloning, expression, characterization and role of the leader sequence of a lipase from Rhizopus oryzae. Biochimica et Biophysica Acta 1998, 1399:173-180.
    • (1998) Biochimica et Biophysica Acta , vol.1399 , pp. 173-180
    • Beer, H.D.1    McCarthy, J.E.G.2    Bornscheuer, U.T.3    Schmid, R.D.4
  • 10
    • 68649091229 scopus 로고    scopus 로고
    • Rhizopus chinensis lipase: gene cloning, expression in Pichia pastoris and properties
    • Yu XW, Wang LL, Xu Y. Rhizopus chinensis lipase: gene cloning, expression in Pichia pastoris and properties. J Mol Catal B: Enzym 2009, 57:304-311.
    • (2009) J Mol Catal B: Enzym , vol.57 , pp. 304-311
    • Yu, X.W.1    Wang, L.L.2    Xu, Y.3
  • 11
    • 0037072996 scopus 로고    scopus 로고
    • Biosynthesis of ethyl esters of short-chain fatty acids using whole-cell lipase from Rhizopus chinensis CCTCC M201021 in non-aqueous phase
    • Xu Y, Wang D, Mu XQ, Zhao GA, Zhang KC. Biosynthesis of ethyl esters of short-chain fatty acids using whole-cell lipase from Rhizopus chinensis CCTCC M201021 in non-aqueous phase. J Mol Catal B: Enzym 2002, 18:29-37.
    • (2002) J Mol Catal B: Enzym , vol.18 , pp. 29-37
    • Xu, Y.1    Wang, D.2    Mu, X.Q.3    Zhao, G.A.4    Zhang, K.C.5
  • 12
    • 0042388350 scopus 로고    scopus 로고
    • Efficient esterification of sorbitan oleate by lipase in a solvent-free system
    • Xu Y, Wang D, Mu XQ, Ni YQ. Efficient esterification of sorbitan oleate by lipase in a solvent-free system. J Am Oil Chem Soc 2003, 80:647-651.
    • (2003) J Am Oil Chem Soc , vol.80 , pp. 647-651
    • Xu, Y.1    Wang, D.2    Mu, X.Q.3    Ni, Y.Q.4
  • 13
    • 66149124499 scopus 로고    scopus 로고
    • Purification and biochemical characterization of an intracellular lipase by Rhizopus chinensis under solid-state fermentation and its potential application in the production of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA)
    • Sun SY, Xu Y, Wang D. Purification and biochemical characterization of an intracellular lipase by Rhizopus chinensis under solid-state fermentation and its potential application in the production of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA). J Chem Technol Biotechnol 2009, 84:435-441.
    • (2009) J Chem Technol Biotechnol , vol.84 , pp. 435-441
    • Sun, S.Y.1    Xu, Y.2    Wang, D.3
  • 14
    • 59649122602 scopus 로고    scopus 로고
    • Novel minor lipase from Rhizopus chinensis during solid-state fermentation: Biochemical characterization and its esterification potential for ester synthesis
    • Sun SY, Xu Y, Wang D. Novel minor lipase from Rhizopus chinensis during solid-state fermentation: Biochemical characterization and its esterification potential for ester synthesis. Bioresource Technol 2009, 100:2607-2612.
    • (2009) Bioresource Technol , vol.100 , pp. 2607-2612
    • Sun, S.Y.1    Xu, Y.2    Wang, D.3
  • 15
    • 83755169013 scopus 로고    scopus 로고
    • Rheology, microstructure, and baking characteristics of frozen dough containing Rhizopus chinensis lipase and transglutaminase
    • Li Z, Tang X, Huang W, Liu JG, Tilley M, Yao Y. Rheology, microstructure, and baking characteristics of frozen dough containing Rhizopus chinensis lipase and transglutaminase. Cereal Chem 2011, 88:596-601.
    • (2011) Cereal Chem , vol.88 , pp. 596-601
    • Li, Z.1    Tang, X.2    Huang, W.3    Liu, J.G.4    Tilley, M.5    Yao, Y.6
  • 16
    • 33645781503 scopus 로고    scopus 로고
    • Directed evolution strategies for improved enzymatic performance
    • Hibbert EG, Dalby PA. Directed evolution strategies for improved enzymatic performance. Microb Cell Fact 2005, 4:29-34.
    • (2005) Microb Cell Fact , vol.4 , pp. 29-34
    • Hibbert, E.G.1    Dalby, P.A.2
  • 17
    • 0035907159 scopus 로고    scopus 로고
    • Improvement of the optimum temperature of lipase activity for Rhizopus niveus by random mutagenesis and its structural interpretation
    • Kohno M, Enatsu M, Funatsu J, Yoshiizumi M, Kugimiya W. Improvement of the optimum temperature of lipase activity for Rhizopus niveus by random mutagenesis and its structural interpretation. J Biotechnol 2001, 87:203-210.
    • (2001) J Biotechnol , vol.87 , pp. 203-210
    • Kohno, M.1    Enatsu, M.2    Funatsu, J.3    Yoshiizumi, M.4    Kugimiya, W.5
  • 18
    • 29144524951 scopus 로고    scopus 로고
    • Heterologous production of functional forms of Rhizopus oryzae lipase in Escherichia coli
    • Di Lorenzo M, Hidalgo A, Haas M, Bornscheuer UT. Heterologous production of functional forms of Rhizopus oryzae lipase in Escherichia coli. Appl Environ Microbiol 2005, 71:8974-8977.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8974-8977
    • Di Lorenzo, M.1    Hidalgo, A.2    Haas, M.3    Bornscheuer, U.T.4
  • 20
    • 0035831305 scopus 로고    scopus 로고
    • Optimization of the high-level production of Rhizopus oryzae lipase in Pichia pastoris
    • Minning S, Serrano A, Ferrer P, Sola C, Schmid RD, Valero F. Optimization of the high-level production of Rhizopus oryzae lipase in Pichia pastoris. J Biotechnol 2001, 86:59-70.
    • (2001) J Biotechnol , vol.86 , pp. 59-70
    • Minning, S.1    Serrano, A.2    Ferrer, P.3    Sola, C.4    Schmid, R.D.5    Valero, F.6
  • 21
    • 1842530437 scopus 로고    scopus 로고
    • Expression of a Rhizopus oryzae lipase in Pichia pastoris under control of the nitrogen source-regulated formaldehyde dehydrogenase promoter
    • Resina D, Serrano A, Valero F, Ferrer P. Expression of a Rhizopus oryzae lipase in Pichia pastoris under control of the nitrogen source-regulated formaldehyde dehydrogenase promoter. J Biotechnol 2004, 109:103-113.
    • (2004) J Biotechnol , vol.109 , pp. 103-113
    • Resina, D.1    Serrano, A.2    Valero, F.3    Ferrer, P.4
  • 22
    • 34548175274 scopus 로고    scopus 로고
    • Transcriptional response of P. pastoris in fed-batch cultivations to Rhizopus oryzae lipase production reveals UPR induction
    • Resina D, Bollok M, Khatri N, Valero F, Neubauer P, Ferrer P. Transcriptional response of P. pastoris in fed-batch cultivations to Rhizopus oryzae lipase production reveals UPR induction. Microb Cell Fact 2007, 6:21-31.
    • (2007) Microb Cell Fact , vol.6 , pp. 21-31
    • Resina, D.1    Bollok, M.2    Khatri, N.3    Valero, F.4    Neubauer, P.5    Ferrer, P.6
  • 23
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S, Fazenda ML, McNeil B, Harvey LM. Heterologous protein production using the Pichia pastoris expression system. Yeast 2005, 22:249-270.
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 24
    • 84856790732 scopus 로고    scopus 로고
    • Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway
    • Krainer FW, Dietzsch C, Hajek T, Herwig C, Spadiut O, Glieder A. Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway. Microb Cell Fact 2012, 11:22-35.
    • (2012) Microb Cell Fact , vol.11 , pp. 22-35
    • Krainer, F.W.1    Dietzsch, C.2    Hajek, T.3    Herwig, C.4    Spadiut, O.5    Glieder, A.6
  • 25
    • 33750608896 scopus 로고    scopus 로고
    • Improved thermostability and the optimum temperature of Rhizopus arrhizus lipase by directed evolution
    • Niu WN, Li ZP, Zhang DW, Yu MR, Tan TW. Improved thermostability and the optimum temperature of Rhizopus arrhizus lipase by directed evolution. J Mol Catal B: Enzym 2006, 43:33-39.
    • (2006) J Mol Catal B: Enzym , vol.43 , pp. 33-39
    • Niu, W.N.1    Li, Z.P.2    Zhang, D.W.3    Yu, M.R.4    Tan, T.W.5
  • 27
    • 0030873221 scopus 로고    scopus 로고
    • Recombination-mediated PCR-directed plasmid construction in vivo in yeast
    • Oldenburg KR, Vo KT, Michaelis S, Paddon C. Recombination-mediated PCR-directed plasmid construction in vivo in yeast. Nucleic acids Res 1997, 25:451-452.
    • (1997) Nucleic acids Res , vol.25 , pp. 451-452
    • Oldenburg, K.R.1    Vo, K.T.2    Michaelis, S.3    Paddon, C.4
  • 28
    • 1442335000 scopus 로고    scopus 로고
    • Recombinant porcine intestinal carboxylesterase: cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization
    • Musidlowska-Persson A, Bornscheuer UT. Recombinant porcine intestinal carboxylesterase: cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization. Protein Eng 2003, 16:1139-1145.
    • (2003) Protein Eng , vol.16 , pp. 1139-1145
    • Musidlowska-Persson, A.1    Bornscheuer, U.T.2
  • 29
    • 11144334584 scopus 로고    scopus 로고
    • Expression of manganese lipoxygenase in Pichia pastoris and site-directed mutagenesis of putative metal ligands
    • Cristea M, Engström T, Su C, Hörnsten L, Oliw EH. Expression of manganese lipoxygenase in Pichia pastoris and site-directed mutagenesis of putative metal ligands. Arch Biochem Biophys 2005, 434:201-211.
    • (2005) Arch Biochem Biophys , vol.434 , pp. 201-211
    • Cristea, M.1    Engström, T.2    Su, C.3    Hörnsten, L.4    Oliw, E.H.5
  • 34
    • 77951174887 scopus 로고    scopus 로고
    • Evolving thermostability in mutant libraries of ligninolytic oxidoreductases expressed in yeast
    • García-Ruiz E, Maté D, Ballesteros A, Martinez AT, Alcalde M. Evolving thermostability in mutant libraries of ligninolytic oxidoreductases expressed in yeast. Microb Cell Fact 2010, 9:17.
    • (2010) Microb Cell Fact , vol.9 , pp. 17
    • García-Ruiz, E.1    Maté, D.2    Ballesteros, A.3    Martinez, A.T.4    Alcalde, M.5
  • 36
    • 26844523510 scopus 로고    scopus 로고
    • Directed evolution of a thermostable phosphite dehydrogenase for NAD (P) H regeneration
    • Johannes TW, Woodyer RD, Zhao H. Directed evolution of a thermostable phosphite dehydrogenase for NAD (P) H regeneration. Appl Environ Microbiol 2005, 71:5728-5734.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 5728-5734
    • Johannes, T.W.1    Woodyer, R.D.2    Zhao, H.3
  • 37
    • 17644365489 scopus 로고    scopus 로고
    • Structural features of thermozymes
    • Li W, Zhou X, Lu P. Structural features of thermozymes. Biotechnol Adv 2005, 23:271-281.
    • (2005) Biotechnol Adv , vol.23 , pp. 271-281
    • Li, W.1    Zhou, X.2    Lu, P.3
  • 38
    • 0040003315 scopus 로고    scopus 로고
    • Structural and functional properties of low molecular weight endo-1, 4-β-xylanases
    • Törrönen A, Rouvinen J. Structural and functional properties of low molecular weight endo-1, 4-β-xylanases. J Biotechnol 1997, 57:137-149.
    • (1997) J Biotechnol , vol.57 , pp. 137-149
    • Törrönen, A.1    Rouvinen, J.2
  • 39
    • 0036217687 scopus 로고    scopus 로고
    • Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1, 4-β-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH
    • Turunen O, Vuorio M, Fenel F, Leisola M. Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1, 4-β-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH. Protein Eng 2002, 15:141-145.
    • (2002) Protein Eng , vol.15 , pp. 141-145
    • Turunen, O.1    Vuorio, M.2    Fenel, F.3    Leisola, M.4
  • 40
    • 0035827175 scopus 로고    scopus 로고
    • In-vitro selection of highly stabilized protein variants with optimized surface
    • Martin A, Sieber V, Schmid FX. In-vitro selection of highly stabilized protein variants with optimized surface. J Mol Biol 2001, 309:717-726.
    • (2001) J Mol Biol , vol.309 , pp. 717-726
    • Martin, A.1    Sieber, V.2    Schmid, F.X.3
  • 41
    • 0036310988 scopus 로고    scopus 로고
    • Origins of the high stability of an in vitro-selected cold-shock protein
    • Martin A, Kather I, Schmid FX. Origins of the high stability of an in vitro-selected cold-shock protein. J Mol Biol 2002, 318:1341-1349.
    • (2002) J Mol Biol , vol.318 , pp. 1341-1349
    • Martin, A.1    Kather, I.2    Schmid, F.X.3
  • 42
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 2001, 65:1-43.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 43
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin E into a functional equivalent of thermitase
    • Zhao H, Arnold FH. Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng 1999, 12:47-53.
    • (1999) Protein Eng , vol.12 , pp. 47-53
    • Zhao, H.1    Arnold, F.H.2
  • 44
    • 0030754926 scopus 로고    scopus 로고
    • Optimization of DNA shuffling for high fidelity recombination
    • Zhao H, Arnold FH. Optimization of DNA shuffling for high fidelity recombination. Nucleic Acids Res 1997, 25:1307-1308.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1307-1308
    • Zhao, H.1    Arnold, F.H.2
  • 45
    • 0347915684 scopus 로고    scopus 로고
    • High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol
    • Wu SX, Letchworth GJ. High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol. Biotechniques 2004, 36:152-154.
    • (2004) Biotechniques , vol.36 , pp. 152-154
    • Wu, S.X.1    Letchworth, G.J.2
  • 46
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones
    • Khalameyzer V, Fischer I, Bornscheuer U, Altenbuchner J. Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones. Appl Environ Microbiol 1999, 65:477-482.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 477-482
    • Khalameyzer, V.1    Fischer, I.2    Bornscheuer, U.3    Altenbuchner, J.4
  • 47
    • 0025914935 scopus 로고
    • Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X-Ray diffraction data
    • Kordel M, Hofmann B, Schomburg D, Schmid RD. Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X-Ray diffraction data. J Bacteriol 1991, 173:4836-4841.
    • (1991) J Bacteriol , vol.173 , pp. 4836-4841
    • Kordel, M.1    Hofmann, B.2    Schomburg, D.3    Schmid, R.D.4
  • 48
    • 84858126537 scopus 로고    scopus 로고
    • Automated protein structure modeling with SWISS-MODEL workspace and the protein model portal
    • Bordoli L, Schwede T. Automated protein structure modeling with SWISS-MODEL workspace and the protein model portal. Methods Mol Biol (Clifton, NJ) 2012, 857:107-136.
    • (2012) Methods Mol Biol (Clifton, NJ) , vol.857 , pp. 107-136
    • Bordoli, L.1    Schwede, T.2
  • 49
    • 0029771658 scopus 로고    scopus 로고
    • The crystal structure of lipase II from Rhizopus niveus at 2.2 Å resolution
    • Kohno M, Funatsu J, Mikami B, Kugimiya W, Matsuo T, Morita Y. The crystal structure of lipase II from Rhizopus niveus at 2.2 Å resolution. J Biochem 1996, 120:505-510.
    • (1996) J Biochem , vol.120 , pp. 505-510
    • Kohno, M.1    Funatsu, J.2    Mikami, B.3    Kugimiya, W.4    Matsuo, T.5    Morita, Y.6


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