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Volumn 373, Issue 1-2, 2013, Pages 149-159

Characterization and evolution of a metagenome-derived lipase towards enhanced enzyme activity and thermostability

Author keywords

Activity; Directed evolution; Lipase; Metagenomic; Thermostability

Indexed keywords

ENZYME VARIANT; LIPR1 PROTEIN; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 84871776493     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-012-1483-8     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 77049088269 scopus 로고    scopus 로고
    • Protein engineering and discovery of lipases
    • 10.1002/ejlt.200900143 1:CAS:528:DC%2BC3cXht12nurY%3D
    • Kourist R, Brundiek H, Bornscheuer UT (2010) Protein engineering and discovery of lipases. Eur J Lipid Sci Technol 112:64-74
    • (2010) Eur J Lipid Sci Technol , vol.112 , pp. 64-74
    • Kourist, R.1    Brundiek, H.2    Bornscheuer, U.T.3
  • 3
    • 0031023666 scopus 로고    scopus 로고
    • 'Interfacial activation' of lipases: Facts and artefacts
    • 10.1016/S0167-7799(96)10064-0 1:CAS:528:DyaK2sXhtFCiu7c%3D
    • Verger R (1997) 'Interfacial activation' of lipases: facts and artefacts. Trends Biotechnol 15:32-38
    • (1997) Trends Biotechnol , vol.15 , pp. 32-38
    • Verger, R.1
  • 4
    • 0032479388 scopus 로고    scopus 로고
    • Lipases - Interfacial enzymes with attractive applications
    • 10.1002/(SICI)1521-3773(19980703)37:12<1608: AID-ANIE1608>3.0.CO;2- V
    • Schmid RD, Verger R (1998) Lipases - interfacial enzymes with attractive applications. Angew Chem Int Ed 37:1608-1633
    • (1998) Angew Chem Int Ed , vol.37 , pp. 1608-1633
    • Schmid, R.D.1    Verger, R.2
  • 5
    • 0142107384 scopus 로고    scopus 로고
    • Rhizomucor miehei lipase: Differential scanning calorimetry and pressure/temperature stability studies in presence of soluble additives
    • 10.1016/S0141-0229(03)00123-6 1:CAS:528:DC%2BD3sXlvVWisLg%3D
    • Noel M, Combes D (2003) Rhizomucor miehei lipase: differential scanning calorimetry and pressure/temperature stability studies in presence of soluble additives. Enzyme Microb Technol 33:299-308
    • (2003) Enzyme Microb Technol , vol.33 , pp. 299-308
    • Noel, M.1    Combes, D.2
  • 6
    • 3142776374 scopus 로고    scopus 로고
    • Mono-thioesters and di-thioesters by lipase-catalyzed reactions of alpha, omega alkanedithiols with palmitic acid or its methyl ester
    • 15048592 10.1007/s00253-004-1604-8 1:CAS:528:DC%2BD2cXktlyrsro%3D
    • Weber N, Klein E, Vosmann K, Mukherjee KD (2004) Mono-thioesters and di-thioesters by lipase-catalyzed reactions of alpha, omega alkanedithiols with palmitic acid or its methyl ester. Appl Microbiol Biotechnol 64:800-805
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 800-805
    • Weber, N.1    Klein, E.2    Vosmann, K.3    Mukherjee, K.D.4
  • 7
    • 33644774786 scopus 로고    scopus 로고
    • Copolymeric polythioesters by lipase-catalyzed thioesterification and transthioesterification of alpha, omega-alkanedithiols
    • 16007456 10.1007/s00253-005-027-5 1:CAS:528:DC%2BD28XitV2qsbk%3D
    • Weber N, Bergander K, Fehling E, Klein E, Vosmann K, Mukherjee KD (2006) Copolymeric polythioesters by lipase-catalyzed thioesterification and transthioesterification of alpha, omega-alkanedithiols. Appl Microbiol Biotechnol 70:290-297
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 290-297
    • Weber, N.1    Bergander, K.2    Fehling, E.3    Klein, E.4    Vosmann, K.5    Mukherjee, K.D.6
  • 8
    • 43849091244 scopus 로고    scopus 로고
    • Scale-up synthesis of lipase-catalyzed palm esters in stirred-tank reactor
    • 18243690 10.1016/j.biortech.2007.12.049 1:CAS:528:DC%2BD1cXmtlCnsLg%3D
    • Keng PS, Basri M, Ariff AB, Abdul Rahman MB, Abdul Rahman RN, Salleh AB (2008) Scale-up synthesis of lipase-catalyzed palm esters in stirred-tank reactor. Bioresour Technol 99:6097-6104
    • (2008) Bioresour Technol , vol.99 , pp. 6097-6104
    • Keng, P.S.1    Basri, M.2    Ariff, A.B.3    Abdul Rahman, M.B.4    Abdul Rahman, R.N.5    Salleh, A.B.6
  • 9
    • 33847757782 scopus 로고    scopus 로고
    • The dependence of enzyme activity with temperature: Determination and validation of parameters
    • 17092210 10.1042/BJ20061143 1:CAS:528:DC%2BD2sXhslWntbY%3D
    • Peterson ME, Daniel RM, Danson MJ, Eisenthal R (2007) The dependence of enzyme activity with temperature: determination and validation of parameters. Biochem J. 402:331-337
    • (2007) Biochem J. , vol.402 , pp. 331-337
    • Peterson, M.E.1    Daniel, R.M.2    Danson, M.J.3    Eisenthal, R.4
  • 10
    • 70450242805 scopus 로고    scopus 로고
    • Exploring protein fitness landscapes by directed evolution
    • 10.1038/nrm2805 1:CAS:528:DC%2BD1MXhsVGlur%2FI
    • Romero PA, Arnold FH (2009) Exploring protein fitness landscapes by directed evolution. Nature Review Mol Cell Biol 10:866-876
    • (2009) Nature Review Mol Cell Biol , vol.10 , pp. 866-876
    • Romero, P.A.1    Arnold, F.H.2
  • 12
    • 1942503297 scopus 로고    scopus 로고
    • Controlling the enantioselectivity of enzymes by directed evolution: Practical and theoretical ramifications
    • 15079053 10.1073/pnas.0306866101 1:CAS:528:DC%2BD2cXjsFKgtbk%3D
    • Reetz MT (2004) Controlling the enantioselectivity of enzymes by directed evolution: practical and theoretical ramifications. Proc Natl Acad Sci USA 101:5716-5722
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5716-5722
    • Reetz, M.T.1
  • 13
    • 0034059496 scopus 로고    scopus 로고
    • Inverting enantioselectivity by directed evolution of hydantoinase for improved production of l-methionine
    • 10700149 10.1038/73773 1:CAS:528:DC%2BD3cXhvVyru7k%3D
    • May O, Nguyen PT, Arnold FH (2000) Inverting enantioselectivity by directed evolution of hydantoinase for improved production of l-methionine. Nat Biotechnol 18(3):317-320
    • (2000) Nat Biotechnol , vol.18 , Issue.3 , pp. 317-320
    • May, O.1    Nguyen, P.T.2    Arnold, F.H.3
  • 14
    • 20444401521 scopus 로고    scopus 로고
    • Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability
    • 15949807 10.1016/j.febslet.2005.05.016 1:CAS:528:DC%2BD2MXlt1KjsLs%3D
    • Choi WC, Kim MH, Ro HS, Sang RR, Oh TK, Lee JK (2005) Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability. FEBS Lett 579:3461-3466
    • (2005) FEBS Lett , vol.579 , pp. 3461-3466
    • Choi, W.C.1    Kim, M.H.2    Ro, H.S.3    Sang, R.R.4    Oh, T.K.5    Lee, J.K.6
  • 15
    • 0030070838 scopus 로고    scopus 로고
    • DNA recovery from soils of diverse composition
    • 8593035 1:CAS:528:DyaK28XovVCnsw%3D%3D
    • Zhou J, Bruns MA, Tiedje JM (1996) DNA recovery from soils of diverse composition. Appl Environ Microbiol 62:316-322
    • (1996) Appl Environ Microbiol , vol.62 , pp. 316-322
    • Zhou, J.1    Bruns, M.A.2    Tiedje, J.M.3
  • 16
    • 34848861111 scopus 로고    scopus 로고
    • An improved method for single step purification of metagenomic DNA
    • 17827539 10.1007/s12033-007-0015-3 1:CAS:528:DC%2BD2sXms1Ontbs%3D
    • Sharma PK, Capalsh N, Kaur J (2007) An improved method for single step purification of metagenomic DNA. Mol Biotechnol 36:61-63
    • (2007) Mol Biotechnol , vol.36 , pp. 61-63
    • Sharma, P.K.1    Capalsh, N.2    Kaur, J.3
  • 17
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 10.1107/S0021889892009944 1:CAS:528:DyaK3sXit12lurY%3D
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 18
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • 1538787 10.1038/356083a0 1:STN:280:DyaK387mvVWluw%3D%3D
    • Luthy R, Bowie JU, Eisenberg D (1992) Assessment of protein models with three-dimensional profiles. Nature 356:83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 19
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • 17517781 10.1093/nar/gkm290
    • Wiederstein, Sippl (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res 35:W407-W410
    • (2007) Nucleic Acids Res , vol.35
    • Wiederstein1    Sippl2
  • 20
    • 84871787529 scopus 로고    scopus 로고
    • CCP4 Newsletter (Number 42, Summer 2005)
    • CCP4 Newsletter (Number 42, Summer 2005)
  • 21
    • 0034013627 scopus 로고    scopus 로고
    • Purification, characterization and thermostability of lipase from a thermophilic Bacillus sp
    • 10839198 10.1023/A:1007047328301 1:CAS:528:DC%2BD3cXjtlKmsbk%3D
    • Nawani N, Kaur J (2000) Purification, characterization and thermostability of lipase from a thermophilic Bacillus sp. Mol Cell Biochem 206:91-96
    • (2000) Mol Cell Biochem , vol.206 , pp. 91-96
    • Nawani, N.1    Kaur, J.2
  • 23
    • 38349084443 scopus 로고    scopus 로고
    • Partial purification and biochemistry characterization of an extracellular lipase obtained from new Rhizopus sp. stream
    • 10.1590/S0101-20612003000200006 1:CAS:528:DC%2BD3sXnvVGjtL8%3D
    • Pastore GM, Costa VSR, Koblitz MGB (2003) Partial purification and biochemistry characterization of an extracellular lipase obtained from new Rhizopus sp. stream. Ciência e Tecnologia de Alimentos 23(2):135-140
    • (2003) Ciência e Tecnologia de Alimentos , vol.23 , Issue.2 , pp. 135-140
    • Pastore, G.M.1    Costa, V.S.R.2    Koblitz, M.G.B.3
  • 24
    • 0030152430 scopus 로고    scopus 로고
    • Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: A simple test for the determination of lipase activity in organic media
    • 10.1016/0141-0229(95)00120-4
    • Pencreac'h G, Barrati JC (1996) Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: a simple test for the determination of lipase activity in organic media. Enzym Microb Technol 18:417-422
    • (1996) Enzym Microb Technol , vol.18 , pp. 417-422
    • Pencreac'H, G.1    Barrati, J.C.2
  • 25
    • 84863851532 scopus 로고    scopus 로고
    • Characterization of thermostable lipase showing loss of secondary structure at ambient temperature
    • 21678056 10.1007/s11033-011-1038-1 1:CAS:528:DC%2BC38XhvVWmtbc%3D
    • Sharma PK, Singh K, Singh R, Capalash N, Ali A, Mohammad O, Kaur J (2012) Characterization of thermostable lipase showing loss of secondary structure at ambient temperature. Mol Biol Rep 39(3):2795-2804
    • (2012) Mol Biol Rep , vol.39 , Issue.3 , pp. 2795-2804
    • Sharma, P.K.1    Singh, K.2    Singh, R.3    Capalash, N.4    Ali, A.5    Mohammad, O.6    Kaur, J.7
  • 26
    • 81455154019 scopus 로고    scopus 로고
    • Engineering of a metagenome derived lipase toward thermal tolerance: Effect of asparagine to lysine mutation on the protein surface
    • 22001407 10.1016/j.gene.2011.09.028 1:CAS:528:DC%2BC3MXhsVymtL%2FP
    • Sharma PK, Kumar R, Kumar R, Mohammad O, Singh R, Kaur J (2012) Engineering of a metagenome derived lipase toward thermal tolerance: effect of asparagine to lysine mutation on the protein surface. Gene 491(2):264-271
    • (2012) Gene , vol.491 , Issue.2 , pp. 264-271
    • Sharma, P.K.1    Kumar, R.2    Kumar, R.3    Mohammad, O.4    Singh, R.5    Kaur, J.6
  • 27
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin e into a functional equivalent of thermitase
    • 10065710 10.1093/protein/12.1.47 1:CAS:528:DyaK1MXht1Kgsb0%3D
    • Zhao H, Arnold FH (1999) Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng 12(1):47-53
    • (1999) Protein Eng , vol.12 , Issue.1 , pp. 47-53
    • Zhao, H.1    Arnold, F.H.2
  • 28
    • 80051473563 scopus 로고    scopus 로고
    • Engineeering of Bacillus lipase by directed evolution for enhanced thermal stability: Effect of isoleucine to threonine mutation
    • 20127521 10.1007/s11033-010-9954-z
    • Khurana J, Singh R, Kaur J (2010) Engineeering of Bacillus lipase by directed evolution for enhanced thermal stability: effect of isoleucine to threonine mutation. Mol Biol Rep 38:2919-2926
    • (2010) Mol Biol Rep , vol.38 , pp. 2919-2926
    • Khurana, J.1    Singh, R.2    Kaur, J.3
  • 29
    • 69149097372 scopus 로고    scopus 로고
    • Gene cloning, expression and characterization of the Geobacillus thermoleovorans CCR11 thermoalkaliphilic Lipase
    • 10.1007/s12033-008-9136-6
    • Castro RQ, Diaz P, Alfaro GV, Gracia HS, Ros RO (2009) Gene cloning, expression and characterization of the Geobacillus thermoleovorans CCR11 thermoalkaliphilic Lipase. Mol Biotechnol 42:75-83
    • (2009) Mol Biotechnol , vol.42 , pp. 75-83
    • Castro, R.Q.1    Diaz, P.2    Alfaro, G.V.3    Gracia, H.S.4    Ros, R.O.5
  • 30
    • 0031613603 scopus 로고    scopus 로고
    • Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1
    • 9501519 10.1271/bbb.62.66 1:CAS:528:DyaK1cXpsVCrsg%3D%3D
    • Kim HK, Park SY, Lee JK, Oh TK (1998) Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1. Biosci Biotechnol Biochem 62:66-71
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 66-71
    • Kim, H.K.1    Park, S.Y.2    Lee, J.K.3    Oh, T.K.4
  • 31
    • 0034864538 scopus 로고    scopus 로고
    • Optimization of a thermostable lipase from Bacillus stearothermophilus P1; Overexpression, purification, and characterization
    • 11483000 10.1006/prep.2001.1456 1:CAS:528:DC%2BD3MXlsFynt7g%3D
    • Sinchaikul S, Sookkheo B, Phutrakul S, Pan FM, Chen ST (2001) Optimization of a thermostable lipase from Bacillus stearothermophilus P1; overexpression, purification, and characterization. Protein Expr Purif 22:388-398
    • (2001) Protein Expr Purif , vol.22 , pp. 388-398
    • Sinchaikul, S.1    Sookkheo, B.2    Phutrakul, S.3    Pan, F.M.4    Chen, S.T.5
  • 32
    • 26844523510 scopus 로고    scopus 로고
    • Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration
    • 10.1128/AEM.71.10.5728-5734.2005
    • Johannes TW, Woodyer RD, Zhao H (2005) Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration. Appl Environ Microbiol 71:5734-5756
    • (2005) Appl Environ Microbiol , vol.71 , pp. 5734-5756
    • Johannes, T.W.1    Woodyer, R.D.2    Zhao, H.3
  • 33
    • 34347206354 scopus 로고    scopus 로고
    • Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt
    • 10.1016/j.procbio.2007.05.005 1:CAS:528:DC%2BD2sXnsFKrsLY%3D
    • Soliman NA, Knoll M, Fattah YRA, Schmid RD, Lange S (2007) Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt. Process Biochem 42:1090-1100
    • (2007) Process Biochem , vol.42 , pp. 1090-1100
    • Soliman, N.A.1    Knoll, M.2    Fattah, Y.R.A.3    Schmid, R.D.4    Lange, S.5
  • 34
    • 20444408450 scopus 로고    scopus 로고
    • Characterization of thermostable lipase from thermophilllic Geobacillus sp
    • 15939301 10.1016/j.pep.2005.03.011
    • Li H, Zhang X (2005) Characterization of thermostable lipase from thermophilllic Geobacillus sp. Protein Expr Purif 42:153-159
    • (2005) Protein Expr Purif , vol.42 , pp. 153-159
    • Li, H.1    Zhang, X.2
  • 35
    • 0009580464 scopus 로고
    • Chemical inactivation of lipase in organic solvent: A lipase from Pseudomonas aeruginosa TE3285 is more like a typical serine enzyme in an organic solvent than in aqueous media
    • 10.1271/bbb.56.1118 1:CAS:528:DyaK38XlsVKjsbw%3D
    • Nakatani T, Hiratake J, Yoshikawa K, Nishioka T, Oda J (1992) Chemical inactivation of lipase in organic solvent: a lipase from Pseudomonas aeruginosa TE3285 is more like a typical serine enzyme in an organic solvent than in aqueous media. Biosci Biotechnol Biochem 56:1118-1123
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1118-1123
    • Nakatani, T.1    Hiratake, J.2    Yoshikawa, K.3    Nishioka, T.4    Oda, J.5
  • 36
    • 0028025693 scopus 로고
    • Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus
    • 10.1016/0005-2760(94)90008-6
    • Dannert CS, Sztajer H, Stocklein W, Menge U, Schmid RD (1994) Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochim Biophys Acta 1214:43-53
    • (1994) Biochim Biophys Acta , vol.1214 , pp. 43-53
    • Dannert, C.S.1    Sztajer, H.2    Stocklein, W.3    Menge, U.4    Schmid, R.D.5
  • 37
    • 78149450306 scopus 로고    scopus 로고
    • Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method
    • 10.1039/c0cc02657c 1:CAS:528:DC%2BC3cXhtl2ltbjI
    • Reetz M, Soni P, Ferna′ndez L, Gumulya Y, Carballeira J (2010) Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method. Chem Commun 46:8657-8658
    • (2010) Chem Commun , vol.46 , pp. 8657-8658
    • Reetz, M.1    Soni, P.2    Fernandez, L.3    Gumulya, Y.4    Carballeira, J.5
  • 38
    • 0037053282 scopus 로고    scopus 로고
    • Novel Zinc-binding Center and a Temperature Switch in the Bacillus stearothermophilus L1 Lipase
    • 11859083 10.1074/jbc.M200640200 1:CAS:528:DC%2BD38Xjslaitbs%3D
    • Jeong ST, Kim HK, Kim SJ, Chi SW, Pan JG, Oh TK, Ryu SE (2002) Novel Zinc-binding Center and a Temperature Switch in the Bacillus stearothermophilus L1 Lipase. J Biol Chem 277:17041-17047
    • (2002) J Biol Chem , vol.277 , pp. 17041-17047
    • Jeong, S.T.1    Kim, H.K.2    Kim, S.J.3    Chi, S.W.4    Pan, J.G.5    Oh, T.K.6    Ryu, S.E.7


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