메뉴 건너뛰기




Volumn 93, Issue 1-2, 1998, Pages 3-14

Overexpression, immobilization and biotechnological application of Pseudomonas lipases

Author keywords

Enantioselectivity; Immobilization; In vitro evolution; Lipase specific foldase; Overexpression; Pseudomonas lipase

Indexed keywords

BACTERIAL ENZYME; TRIACYLGLYCEROL LIPASE;

EID: 0032103762     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-3084(98)00033-4     Document Type: Conference Paper
Times cited : (84)

References (77)
  • 2
    • 0030830073 scopus 로고    scopus 로고
    • A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation required for recycling DsbA/DsbB and DsbC redox proteins
    • Andersen C.L., Matthey-Dupraz A., Missiakis D., Raina S. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation required for recycling DsbA/DsbB and DsbC redox proteins. Mol. Microbiol. 26:1997;121-132.
    • (1997) Mol. Microbiol. , vol.26 , pp. 121-132
    • Andersen, C.L.1    Matthey-Dupraz, A.2    Missiakis, D.3    Raina, S.4
  • 3
    • 43949175664 scopus 로고
    • Immobilization/stabilization on different hydroxylic supports of lipase from Candida rugosa
    • Arroyo M., Moreno J.M., Sinisterra J.V. Immobilization/stabilization on different hydroxylic supports of lipase from Candida rugosa. J. Mol. Catal. 83:1993;261-271.
    • (1993) J. Mol. Catal. , vol.83 , pp. 261-271
    • Arroyo, M.1    Moreno, J.M.2    Sinisterra, J.V.3
  • 4
    • 0000324041 scopus 로고
    • Organic chemistry within ceramic matrixes: Doped sol-gel materials
    • Avnir D. Organic chemistry within ceramic matrixes: doped sol-gel materials. Acc. Chem. Res. 28:1995;328-334.
    • (1995) Acc. Chem. Res. , vol.28 , pp. 328-334
    • Avnir, D.1
  • 5
    • 33751158445 scopus 로고
    • Enzymes and other proteins entrapped in sol-gel materials
    • Avnir D., Braun S., Lev O., Ottolenghi M. Enzymes and other proteins entrapped in sol-gel materials. Chem. Mater. 6:1994;1605-1614.
    • (1994) Chem. Mater. , vol.6 , pp. 1605-1614
    • Avnir, D.1    Braun, S.2    Lev, O.3    Ottolenghi, M.4
  • 6
    • 0010458253 scopus 로고
    • Resolution of optical isomers of tosyloxy-alkanols with lipase
    • 407
    • Bianchi D., Bosetti A., Cesti P., Spezia S. Resolution of optical isomers of tosyloxy-alkanols with lipase. Eur. Pat. Appl. EP. 490407:1992;2.
    • (1992) Eur. Pat. Appl. EP , vol.490 , pp. 2
    • Bianchi, D.1    Bosetti, A.2    Cesti, P.3    Spezia, S.4
  • 7
    • 0026356460 scopus 로고
    • Esterolytic and lipolytic enzymes in organic synthesis
    • Boland, W., Frößl, C. and Lorenz, M., 1991. Esterolytic and lipolytic enzymes in organic synthesis. Synthesis 1049-1072.
    • (1991) Synthesis , pp. 1049-1072
    • Boland, W.1    Frößl, C.2    Lorenz, M.3
  • 9
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • Chen K., Arnold F.H. Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc. Natl. Acad. Sci. USA. 90:1993;5618-5622.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 10
    • 0027530521 scopus 로고
    • Immobilization of lipase for effective interesterification of fats and oils in organic solvent
    • Cho S.-W., Rhee J.S. Immobilization of lipase for effective interesterification of fats and oils in organic solvent. Biotechnol. Bioeng. 41:1993;204-210.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 204-210
    • Cho, S.-W.1    Rhee, J.S.2
  • 11
    • 0010526190 scopus 로고    scopus 로고
    • Enzyme-catalyzed reactions
    • in Ahuja, S. (Ed.), American Chemical Society, Washington, DC
    • Coffen, D.L., 1997. Enzyme-catalyzed reactions, in Ahuja, S. (Ed.), Chiral Separations: Applications and Technology, American Chemical Society, Washington, DC, pp. 59-91.
    • (1997) Chiral Separations: Applications and Technology , pp. 59-91
    • Coffen, D.L.1
  • 12
    • 0000434975 scopus 로고    scopus 로고
    • Industrial enzyme technology
    • Cowan D. Industrial enzyme technology. Trends Biotechnol. 14:1996;177-178.
    • (1996) Trends Biotechnol. , vol.14 , pp. 177-178
    • Cowan, D.1
  • 15
    • 0028878079 scopus 로고
    • Enzymic resolution of alcohols via lipases immobilized in microemulsion-based gels
    • de Jesus P.C., Rezende M.C., da Graca Nascimento M. Enzymic resolution of alcohols via lipases immobilized in microemulsion-based gels. Tetrahedron: Asymmetry. 6:1995;63-66.
    • (1995) Tetrahedron: Asymmetry , vol.6 , pp. 63-66
    • De Jesus, P.C.1    Rezende, M.C.2    Da Graca Nascimento, M.3
  • 16
    • 0028240371 scopus 로고
    • The Pseudomonas fluorescens lipase has a C-terminal secretion signal and is secreted by a three-component bacterial ABC-exporter system
    • Duong F., Soscia A., Lazdunski A., Murgier M. The Pseudomonas fluorescens lipase has a C-terminal secretion signal and is secreted by a three-component bacterial ABC-exporter system. Mol. Microbiol. 11:1994;1117-1126.
    • (1994) Mol. Microbiol. , vol.11 , pp. 1117-1126
    • Duong, F.1    Soscia, A.2    Lazdunski, A.3    Murgier, M.4
  • 18
    • 0000853894 scopus 로고
    • Extremozymes for industry-from nature and by design
    • (London)
    • Govardhan, C.P. and Margolin, A.L., 1995. Extremozymes for industry-from nature and by design. Chem. Ind. (London) 689-693.
    • (1995) Chem. Ind. , pp. 689-693
    • Govardhan, C.P.1    Margolin, A.L.2
  • 20
    • 0028951433 scopus 로고
    • Lipase modulator protein (LimL) of Pseudomonas sp. Strain 109
    • Ihara F., Okamoto I., Akao K., Nihira T., Yamada Y. Lipase modulator protein (LimL) of Pseudomonas sp. Strain 109. J. Bacteriol. 177:1995;1254-1258.
    • (1995) J. Bacteriol. , vol.177 , pp. 1254-1258
    • Ihara, F.1    Okamoto, I.2    Akao, K.3    Nihira, T.4    Yamada, Y.5
  • 21
    • 0029778830 scopus 로고    scopus 로고
    • Biotechnological application of Pseudomonas aeruginosa lipase: Efficient kinetic resolution of amines and alcohols
    • Jaeger K.-E., Liebeton K., Zonta A., Schimossek K., Reetz M.T. Biotechnological application of Pseudomonas aeruginosa lipase: efficient kinetic resolution of amines and alcohols. Appl. Microbiol. Biotechnol. 46:1996;99-105.
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 99-105
    • Jaeger, K.-E.1    Liebeton, K.2    Zonta, A.3    Schimossek, K.4    Reetz, M.T.5
  • 23
    • 0027359783 scopus 로고
    • Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa
    • Jaeger K.-E., Ransac S., Koch H.B., Ferrato F., Dijkstra B.W. Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa. FEBS Lett. 332:1993;143-149.
    • (1993) FEBS Lett. , vol.332 , pp. 143-149
    • Jaeger, K.-E.1    Ransac, S.2    Koch, H.B.3    Ferrato, F.4    Dijkstra, B.W.5
  • 24
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases: versatile tools in biotechnology
    • (submitted).
    • Jaeger, K.-E. and Reetz, M.T., 1998. Microbial lipases: versatile tools in biotechnology. Trends Biotechnol. (submitted).
    • (1998) Trends Biotechnol.
    • Jaeger, K.-E.1    Reetz, M.T.2
  • 26
    • 0002644787 scopus 로고
    • Bakterielle Lipasen: Biochemie, Molekulargenetik und biotechnologische Bedeutung
    • Jaeger K.-E., Wohlfarth S. Bakterielle Lipasen: Biochemie, Molekulargenetik und biotechnologische Bedeutung. BioEng. (Graefelfing, Ger.). 9:1993;39-46.
    • (1993) BioEng. (Graefelfing, Ger.) , vol.9 , pp. 39-46
    • Jaeger, K.-E.1    Wohlfarth, S.2
  • 27
    • 0342754143 scopus 로고    scopus 로고
    • Quick E. A fast spectrophotometric method to measure the enantioselectivity of hydrolases
    • Janes L.E., Kazlauskas R.J. Quick E. A fast spectrophotometric method to measure the enantioselectivity of hydrolases. J. Org. Chem. 62:1997;4560-4561.
    • (1997) J. Org. Chem. , vol.62 , pp. 4560-4561
    • Janes, L.E.1    Kazlauskas, R.J.2
  • 28
    • 0000714772 scopus 로고
    • Enzymes in organic synthesis
    • Jones J.B. Enzymes in organic synthesis. Tetrahedron. 42:1986;3351-3403.
    • (1986) Tetrahedron , vol.42 , pp. 3351-3403
    • Jones, J.B.1
  • 29
    • 0029962076 scopus 로고    scopus 로고
    • Optical resolution of 2,2,2-trifluoro-1-(9-phenanthryl)ethanol via enzymic alcoholysis of its activated ester
    • Kato K., Katayama M., Fujii S., Fukaya H., Kimoto H. Optical resolution of 2,2,2-trifluoro-1-(9-phenanthryl)ethanol via enzymic alcoholysis of its activated ester. J. Ferment. Bioeng. 81:1996;206-211.
    • (1996) J. Ferment. Bioeng. , vol.81 , pp. 206-211
    • Kato, K.1    Katayama, M.2    Fujii, S.3    Fukaya, H.4    Kimoto, H.5
  • 30
    • 0030948567 scopus 로고    scopus 로고
    • Enzymatic resolution of 2,2,2-Trifluoro-1-(pyrenyl)ethanol with lipases
    • Kato K., Katayama M., Fujii S., Kimoto H. Enzymatic resolution of 2,2,2-Trifluoro-1-(pyrenyl)ethanol with lipases. Biosci., Biotechnol. Biochem. 61:1997;194-196.
    • (1997) Biosci., Biotechnol. Biochem. , vol.61 , pp. 194-196
    • Kato, K.1    Katayama, M.2    Fujii, S.3    Kimoto, H.4
  • 31
    • 0029399950 scopus 로고
    • Optical resolution of 1-arylethanols with a condensed aromatic ring by lipase from Pseudomonas aeruginosa
    • Kato K., Katayama M., Fujii S., Kimoto H. Optical resolution of 1-arylethanols with a condensed aromatic ring by lipase from Pseudomonas aeruginosa. Biosci., Biotechnol. Biochem. 59:1995;2178-2180.
    • (1995) Biosci., Biotechnol. Biochem. , vol.59 , pp. 2178-2180
    • Kato, K.1    Katayama, M.2    Fujii, S.3    Kimoto, H.4
  • 32
    • 84952948009 scopus 로고    scopus 로고
    • Biotranformations with Lipases
    • VCH, Weinheim (in press).
    • Kazlauskas, R.J. and Bornscheuer, U.T., 1998. Biotranformations with Lipases (Biotechnology, vol. 8), VCH, Weinheim (in press).
    • (1998) Biotechnology , vol.8
    • Kazlauskas, R.J.1    Bornscheuer, U.T.2
  • 34
    • 21144465745 scopus 로고
    • How to select a useful biocatalyst
    • Kieslich K. How to select a useful biocatalyst. Chimia. 47:1993;99-102.
    • (1993) Chimia , vol.47 , pp. 99-102
    • Kieslich, K.1
  • 36
    • 0002814433 scopus 로고    scopus 로고
    • The general secretion pathway in Pseudomonas aeruginosa: Molecular mechanisms and regulation
    • In: Nakazawa, T., Furukawa, K., Haas, D. and Silver, S. (Eds.), ASM Press, Washington, DC
    • Lazdunski, A., Filloux, A., Michel, G., Foglino, M., Murgier, M., Latifi, A., Chapon, V., Bléves, S. and Bally, M., 1996. The general secretion pathway in Pseudomonas aeruginosa: Molecular mechanisms and regulation. In: Nakazawa, T., Furukawa, K., Haas, D. and Silver, S. (Eds.), Molecular biology of Pseudomonads, ASM Press, Washington, DC, pp. 427-437.
    • (1996) Molecular Biology of Pseudomonads , pp. 427-437
    • Lazdunski, A.1    Filloux, A.2    Michel, G.3    Foglino, M.4    Murgier, M.5    Latifi, A.6    Chapon, V.7    Bléves, S.8    Bally, M.9
  • 40
    • 0030185060 scopus 로고    scopus 로고
    • Novel crystalline catalysts
    • Margolin A.L. Novel crystalline catalysts. Trends Biotechnol. 14:1996;223-230.
    • (1996) Trends Biotechnol. , vol.14 , pp. 223-230
    • Margolin, A.L.1
  • 41
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakis D., Raina S. Protein folding in the bacterial periplasm. J. Bacteriol. 179:1997;2465-2471.
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakis, D.1    Raina, S.2
  • 43
    • 0027435346 scopus 로고
    • The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
    • Noble M.E.M., Cleasby A., Johnson L.N., Egmond M.R., Frenken L.G.J. The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett. 331:1993;123-128.
    • (1993) FEBS Lett. , vol.331 , pp. 123-128
    • Noble, M.E.M.1    Cleasby, A.2    Johnson, L.N.3    Egmond, M.R.4    Frenken, L.G.J.5
  • 44
    • 0000339874 scopus 로고
    • Lipase immobilized by adsorption. Effect of support hydrophobicity on the reaction rate of ester synthesis in cyclohexane
    • Norin M., Boutelje J., Holmberg E., Hult K. Lipase immobilized by adsorption. Effect of support hydrophobicity on the reaction rate of ester synthesis in cyclohexane. Appl. Microbiol. Biotechnol. 28:1988;527-530.
    • (1988) Appl. Microbiol. Biotechnol. , vol.28 , pp. 527-530
    • Norin, M.1    Boutelje, J.2    Holmberg, E.3    Hult, K.4
  • 45
    • 0031081342 scopus 로고    scopus 로고
    • Lipid-coated enzymes as efficient catalysts in organic media
    • Okahata Y., Mori T. Lipid-coated enzymes as efficient catalysts in organic media. Trends Biotechnol. 15:1997;50-54.
    • (1997) Trends Biotechnol. , vol.15 , pp. 50-54
    • Okahata, Y.1    Mori, T.2
  • 46
    • 0030780084 scopus 로고    scopus 로고
    • Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase leads to partial pleiotropic deficiency in c-type cytochrome biogenesis
    • Page M.D., Saunders N.F.W., Ferguson S.J. Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase leads to partial pleiotropic deficiency in c-type cytochrome biogenesis. Microbiology (Reading, UK). 143:1997;3111-3122.
    • (1997) Microbiology (Reading, UK) , vol.143 , pp. 3111-3122
    • Page, M.D.1    Saunders, N.F.W.2    Ferguson, S.J.3
  • 47
    • 0028292641 scopus 로고
    • Synthesis of polymeric microcapsule arrays and their use for enzyme immobilization
    • Parthasarathy R.V., Martin C.R. Synthesis of polymeric microcapsule arrays and their use for enzyme immobilization. Nature (London). 369:1994;298-301.
    • (1994) Nature (London) , vol.369 , pp. 298-301
    • Parthasarathy, R.V.1    Martin, C.R.2
  • 49
    • 0031251298 scopus 로고    scopus 로고
    • Entrapment of biocatalysts in hydrophobic sol-gel materials for use in organic chemistry
    • Reetz M.T. Entrapment of biocatalysts in hydrophobic sol-gel materials for use in organic chemistry. Adv. Mater. (Weinheim, Ger.). 9:1997;943-954.
    • (1997) Adv. Mater. (Weinheim, Ger.) , vol.9 , pp. 943-954
    • Reetz, M.T.1
  • 51
    • 0001050722 scopus 로고    scopus 로고
    • Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution
    • Reetz, M.T., Zonta, A., Schimossek, K., Liebeton, K., Jaeger, K.-E., 1997. Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution. Angew. Chem. 109, 2961-2963; Angew. Chem., Int. Ed. Engl. 36, 2830-2832.
    • (1997) Angew. Chem. , vol.109 , pp. 2961-2963
    • Reetz, M.T.1    Zonta, A.2    Schimossek, K.3    Liebeton, K.4    Jaeger, K.-E.5
  • 52
    • 0001050721 scopus 로고    scopus 로고
    • Reetz, M.T., Zonta, A., Schimossek, K., Liebeton, K., Jaeger, K.-E., 1997. Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution. Angew. Chem. 109, 2961-2963; Angew. Chem., Int. Ed. Engl. 36, 2830-2832.
    • Angew. Chem., Int. Ed. Engl. , vol.36 , pp. 2830-2832
  • 53
    • 0030569931 scopus 로고    scopus 로고
    • Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials
    • Reetz M.T., Zonta A., Simpelkamp J. Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials. Biotechnol. Bioeng. 49:1996;527-534.
    • (1996) Biotechnol. Bioeng. , vol.49 , pp. 527-534
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3
  • 54
    • 0002089444 scopus 로고
    • Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic sol-gel materials
    • Reetz, M.T., Zonta, A. and Simpelkamp, J., 1995. Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic sol-gel materials. Angew. Chem. 107, 373-376; Angew. Chem., Int. Ed. Engl. 34, 301-303.
    • (1995) Angew. Chem. , vol.107 , pp. 373-376
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3
  • 55
    • 0010457806 scopus 로고    scopus 로고
    • Reetz, M.T., Zonta, A. and Simpelkamp, J., 1995. Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic sol-gel materials. Angew. Chem. 107, 373-376; Angew. Chem., Int. Ed. Engl. 34, 301-303.
    • , vol.34 , pp. 301-303
  • 56
    • 1542495409 scopus 로고    scopus 로고
    • In situ fixation of lipase-containing hydrophobic sol-gel materials on sintered glass-highly efficient heterogeneous biocatalysts
    • (Cambridge)
    • Reetz, M.T., Zonta, A., Simpelkamp, J. and Könen, W., 1996b. In situ fixation of lipase-containing hydrophobic sol-gel materials on sintered glass-highly efficient heterogeneous biocatalysts. Chem. Commun. (Cambridge) 1397-1398.
    • (1996) Chem. Commun. , pp. 1397-1398
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3    Könen, W.4
  • 58
    • 0027506517 scopus 로고
    • Stereoselective hydrolysis of triglycerides by animal and microbial lipases
    • Rogalska E., Cudrey C., Ferrato F., Verger R. Stereoselective hydrolysis of triglycerides by animal and microbial lipases. Chirality. 5:1993;24-30.
    • (1993) Chirality , vol.5 , pp. 24-30
    • Rogalska, E.1    Cudrey, C.2    Ferrato, F.3    Verger, R.4
  • 62
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: Interfacial enzymes with attractive applications
    • (in press).
    • Schmid, R.D. and Verger, R., 1998. Lipases: Interfacial enzymes with attractive applications. Angew. Chem. (in press).
    • (1998) Angew. Chem.
    • Schmid, R.D.1    Verger, R.2
  • 66
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature (London). 370:1994;389-391.
    • (1994) Nature (London) , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 67
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer W.P.C. DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA. 91:1994;10747-10751.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 68
    • 0029032855 scopus 로고
    • Lipase from Chromobacterium viscosum: Biochemical characterization indicating homology to the lipase from Pseudomonas glumae
    • Taipa M.A., Liebeton K., Costa J.V., Cabral J.M.S., Jaeger K.-E. Lipase from Chromobacterium viscosum: Biochemical characterization indicating homology to the lipase from Pseudomonas glumae. Biochim. Biophys. Acta. 1256:1995;396-402.
    • (1995) Biochim. Biophys. Acta , vol.1256 , pp. 396-402
    • Taipa, M.A.1    Liebeton, K.2    Costa, J.V.3    Cabral, J.M.S.4    Jaeger, K.-E.5
  • 70
    • 0000760617 scopus 로고
    • Lipase-supported synthesis of biologically active compounds
    • Theil F. Lipase-supported synthesis of biologically active compounds. Chem. Rev. 95:1995;2203-2227.
    • (1995) Chem. Rev. , vol.95 , pp. 2203-2227
    • Theil, F.1
  • 71
    • 0028559002 scopus 로고
    • Enantioselective esterification of 2-methylbutyric acid catalyzed via lipase immobilized in microemulsion-based organogels
    • Uemasu I., Hinze W.L. Enantioselective esterification of 2-methylbutyric acid catalyzed via lipase immobilized in microemulsion-based organogels. Chirality. 6:1994;649-653.
    • (1994) Chirality , vol.6 , pp. 649-653
    • Uemasu, I.1    Hinze, W.L.2
  • 73
    • 0029028451 scopus 로고
    • Determination of lipase specificities through the use of chiral triglycerides and their racemics
    • Villeneuve P., Pina M., Montet D., Graille J. Determination of lipase specificities through the use of chiral triglycerides and their racemics. Chem. Phys. Lipids. 76:1995;109-113.
    • (1995) Chem. Phys. Lipids , vol.76 , pp. 109-113
    • Villeneuve, P.1    Pina, M.2    Montet, D.3    Graille, J.4
  • 74
    • 0000663924 scopus 로고    scopus 로고
    • Activity and adsorption of lipase from Humicola lanuginosa on surfaces with different wettabilities
    • Wannerberger K., Welin-Klintström S., Arnebrant T. Activity and adsorption of lipase from Humicola lanuginosa on surfaces with different wettabilities. Langmuir. 13:1997;784-790.
    • (1997) Langmuir , vol.13 , pp. 784-790
    • Wannerberger, K.1    Welin-Klintström, S.2    Arnebrant, T.3
  • 76
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang J.-H., Dawes G., Stemmer W.P.C. Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA. 94:1997;4504-4509.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.-H.1    Dawes, G.2    Stemmer, W.P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.