메뉴 건너뛰기




Volumn 10, Issue 9, 1999, Pages 297-302

New frontiers in food enzymology: Recombinant lipoxygenases

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMOLOGY; FOOD; FOOD ENZYMOLOGY; LIPOXYGENASE; RECOMBINANT GENE;

EID: 0033507314     PISSN: 09242244     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0924-2244(00)00010-8     Document Type: Article
Times cited : (43)

References (62)
  • 1
    • 85120129123 scopus 로고    scopus 로고
    • Ueda, N., Susuki, H. and Yamamoto, S. (1998) ‘Mammalian Lipoxygenases: Structure, Function and Evolutionary Aspects' in Eicosanoids and Related Compounds in Plants and Animals , (Rowley, A.F., Kühn, K. and Schewe, T. eds), pp. 47–67, Portland Press
  • 2
    • 85120116230 scopus 로고    scopus 로고
    • Veldink, G.A., Hilbers, M.P., Nieuwenhuizen, W.F. and Vliegenthart, J.F.G. (1998) ‘Plant Lipoxygenase: Structure and Mechanism' in Eicosanoids and Related Compounds in Plants and Animals , (Rowley, A.F., Kühn, K. and Schewe, T. eds), pp. 69–95, Portland Press
  • 3
    • 85120103248 scopus 로고    scopus 로고
    • Casey, R. (1999) ‘Genetic Manipulation of Lipoxygenases for the Agrifood Industry' in Genetics and Breeding for Crop Quality and Resistance , (Scarascia Mugnozza, G.T., Porceddu, E. and Pagnotta, M.A. eds), pp. 259–269, Kluwer Academic Publishers
  • 4
    • 85120120211 scopus 로고    scopus 로고
    • Casey, R. (1997) ‘Lipoxygenases and Breadmaking' in Proceedings of the First European Symposium on Enzymes and Grain Processing , (Angelino, S.A.G.F., Hamer, R.J., van Hartingsfeld, W., Heidekamp, F. and van der Lugt, J.P. eds), pp. 188–194, TNO, Zeist, The Netherlands
  • 5
    • 85120109247 scopus 로고    scopus 로고
    • Whitehead, I.M., Muller, B.L. and Dean, C. (1995) ‘Industrial Use of Soybean Lipoxygenase for the Production of Natural Green Note Flavor Compounds' in Cereal Foods World 40, 193–197
  • 6
    • 85120098943 scopus 로고    scopus 로고
    • Casey, R., Domoney, C., Forster, C., Robinson, D. and Wu, Z. (1996) ‘The Significance of Plant Lipoxygenases to the Agrifood Industry' in Agrifood Quality: An Interdisciplinary Approach , (Fenwick, G.R., Hedley, C., Richards, R.L. and Khokhar, S. eds), pp. 127–130, The Royal Society of Chemistry
  • 7
    • 85120136121 scopus 로고    scopus 로고
    • Hughes, R.K., West, S.I. and Casey, R. (1999) ‘Recombinant Plant Lipoxygenases' in AgBiotechNet 1, October, pp. 1–4, CAB International
  • 10
    • 0000750182 scopus 로고
    • Isolation and Characterization of a Soybean (Glycine max) Lipoxygenase-3 Gene
    • R.L. Yenofsky M. Fine C. Liu Isolation and Characterization of a Soybean (Glycine max) Lipoxygenase-3 Gene Mol. Gen. Genet. 211 1988 215 222
    • (1988) Mol. Gen. Genet. , vol.211 , pp. 215-222
    • Yenofsky, R.L.1    Fine, M.2    Liu, C.3
  • 11
    • 0029346885 scopus 로고
    • Sink Limitation Induces the Expression of Multiple Soybean Vegetative Lipoxygenase mRNAs While the Endogenous Jasmonic Acid Level Remains Low
    • T.W. Bunker D.S. Koetje L.C. Stephenson R.A. Creelman J.E. Mullet H.D. Grimes Sink Limitation Induces the Expression of Multiple Soybean Vegetative Lipoxygenase mRNAs While the Endogenous Jasmonic Acid Level Remains Low Plant Cell 7 1995 1319 1331
    • (1995) Plant Cell , vol.7 , pp. 1319-1331
    • Bunker, T.W.1    Koetje, D.S.2    Stephenson, L.C.3    Creelman, R.A.4    Mullet, J.E.5    Grimes, H.D.6
  • 12
    • 0033198536 scopus 로고    scopus 로고
    • Protein Dynamics, Activity and Cellular Localization of Soybean Lipoxygenases Indicate Distinct Functional Roles for Individual Isoforms
    • A.M. Fischer W.E. Dubbs R.A. Baker M.A. Fuller L.C. Stephenson H.D. Grimes Protein Dynamics, Activity and Cellular Localization of Soybean Lipoxygenases Indicate Distinct Functional Roles for Individual Isoforms Plant Journal 19 1999 543 554
    • (1999) Plant Journal , vol.19 , pp. 543-554
    • Fischer, A.M.1    Dubbs, W.E.2    Baker, R.A.3    Fuller, M.A.4    Stephenson, L.C.5    Grimes, H.D.6
  • 13
    • 0029809331 scopus 로고    scopus 로고
    • Characterization of Three Potato Lipoxygenases with Distinct Enzymatic Activities and Different Organ-specific and Wound-regulated Expression Patterns
    • J. Royo G. Vancanneyt A.G. Pérez C. Sanz K. Stõrmann S. Rosahl J.J. Sánchez-Serrano Characterization of Three Potato Lipoxygenases with Distinct Enzymatic Activities and Different Organ-specific and Wound-regulated Expression Patterns J. Biol. Chem. 271 1996 21012 21019
    • (1996) J. Biol. Chem. , vol.271 , pp. 21012-21019
    • Royo, J.1    Vancanneyt, G.2    Pérez, A.G.3    Sanz, C.4    Stõrmann, K.5    Rosahl, S.6    Sánchez-Serrano, J.J.7
  • 14
    • 0029047317 scopus 로고
    • A Chloroplast Lipoxygenase is Required for Wound-induced Jasmonic Acid Accumulation in Arabidopsis
    • E. Bell R.A. Creelman J.E. Mullet A Chloroplast Lipoxygenase is Required for Wound-induced Jasmonic Acid Accumulation in Arabidopsis Proc. Natl. Acad. Sci. USA 92 1995 8675 8679
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8675-8679
    • Bell, E.1    Creelman, R.A.2    Mullet, J.E.3
  • 15
    • 11944260974 scopus 로고
    • Octadecanoid Precursors of Jasmonic Acid Activate the Synthesis of Wound-inducible Proteinase Inhibitors
    • E.E. Farmer C.A. Ryan Octadecanoid Precursors of Jasmonic Acid Activate the Synthesis of Wound-inducible Proteinase Inhibitors Plant Cell 4 1992 129 134
    • (1992) Plant Cell , vol.4 , pp. 129-134
    • Farmer, E.E.1    Ryan, C.A.2
  • 16
    • 0017596280 scopus 로고
    • A Simple Method for the Preparation of Pure 9-D-hydroperoxides of Linoleic Acid and Methyl Linoleate Based on the Positional Specificity of Lipoxygenase in Tomato Fruit
    • J.A. Matthew H.W.-S. Chan T. Galliard A Simple Method for the Preparation of Pure 9-D-hydroperoxides of Linoleic Acid and Methyl Linoleate Based on the Positional Specificity of Lipoxygenase in Tomato Fruit Lipids 12 1977 324 326
    • (1977) Lipids , vol.12 , pp. 324-326
    • Matthew, J.A.1    Chan, H.W.-S.2    Galliard, T.3
  • 17
    • 0031177739 scopus 로고    scopus 로고
    • A Gene Encoding a Chloroplast-targeted Lipoxygenase in Tomato Leaves is Transiently Induced by Wounding, Systemin and Methyl Jasmonate
    • T. Heitz D.R. Bergey C.A. Ryan A Gene Encoding a Chloroplast-targeted Lipoxygenase in Tomato Leaves is Transiently Induced by Wounding, Systemin and Methyl Jasmonate Plant Physiol. 114 1997 1085 1093
    • (1997) Plant Physiol. , vol.114 , pp. 1085-1093
    • Heitz, T.1    Bergey, D.R.2    Ryan, C.A.3
  • 19
    • 0033103289 scopus 로고    scopus 로고
    • Isolation of Lipoxygenase cDNA Clones From Pea Nodule mRNA
    • J.-P. Wisniewski C.D. Gardner N.J. Brewin Isolation of Lipoxygenase cDNA Clones From Pea Nodule mRNA Plant Mol. Biol. 39 1999 775 783
    • (1999) Plant Mol. Biol. , vol.39 , pp. 775-783
    • Wisniewski, J.-P.1    Gardner, C.D.2    Brewin, N.J.3
  • 20
    • 85120112961 scopus 로고    scopus 로고
    • Forster, C. Unpublished (See EMBL database accessions Y15410 and Y15423)
  • 21
    • 85120138707 scopus 로고    scopus 로고
    • Shibata, D., Slusarenko, A., Casey, R., Hildebrand, D. and Bell, E. (1994) ‘Lipoxygenases' in Plant Mol. Biol. Rep. 12 (CPGN Supplement) S41–42
  • 22
    • 0032568536 scopus 로고    scopus 로고
    • The Incompatible Reaction Between Phytophthora parasitica var. nicotianae race D and Tobacco is Suppressed in Transgenic Plants Expressing Antisense Lipoxygenase Sequences
    • I. Rancé J. Fournier M.T. Esquerré-Tugayé The Incompatible Reaction Between Phytophthora parasitica var. nicotianae race D and Tobacco is Suppressed in Transgenic Plants Expressing Antisense Lipoxygenase Sequences Proc. Natl. Acad. Sci. USA 95 1998 6554 6559
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6554-6559
    • Rancé, I.1    Fournier, J.2    Esquerré-Tugayé, M.T.3
  • 24
    • 0002262342 scopus 로고
    • Volatile Products of the Lipoxygenase Pathway Evolved from Phaseolus vulgaris (L.) Leaves Inoculated with Pseudomonas syringae pv Phaseolicola
    • K.P.C. Croft F. Jüttner A.J. Slusarenko Volatile Products of the Lipoxygenase Pathway Evolved from Phaseolus vulgaris (L.) Leaves Inoculated with Pseudomonas syringae pv Phaseolicola Plant Physiology 101 1993 13 24
    • (1993) Plant Physiology , vol.101 , pp. 13-24
    • Croft, K.P.C.1    Jüttner, F.2    Slusarenko, A.J.3
  • 25
    • 0002928236 scopus 로고
    • Agronomic Performance of Soybean Lipoxygenase Isolines
    • T.W. Pfeiffer D.F. Hildebrand D.M. TeKrony Agronomic Performance of Soybean Lipoxygenase Isolines Crop Science 32 1992 362 387
    • (1992) Crop Science , vol.32 , pp. 362-387
    • Pfeiffer, T.W.1    Hildebrand, D.F.2    TeKrony, D.M.3
  • 27
    • 0024059642 scopus 로고
    • The Complete Amino Acid Sequence of a Pea (Pisum sativum) Seed Lipoxygenase Predicted From a Near Full-length cDNA
    • P.M. Ealing R. Casey The Complete Amino Acid Sequence of a Pea ( Pisum sativum ) Seed Lipoxygenase Predicted From a Near Full-length cDNA Biochem. J. 253 1988 915 918
    • (1988) Biochem. J. , vol.253 , pp. 915-918
    • Ealing, P.M.1    Casey, R.2
  • 28
    • 0024842181 scopus 로고
    • The cDNA Cloning of a Pea (Pisum sativum) Seed Lipoxygenase. Sequence Comparisons of the Two Major Pea Seed Lipoxygenase Isoforms
    • P.M. Ealing R. Casey The cDNA Cloning of a Pea ( Pisum sativum ) Seed Lipoxygenase. Sequence Comparisons of the Two Major Pea Seed Lipoxygenase Isoforms Biochem. J. 264 1989 929 932
    • (1989) Biochem. J. , vol.264 , pp. 929-932
    • Ealing, P.M.1    Casey, R.2
  • 29
    • 0032126176 scopus 로고    scopus 로고
    • Characterization of Authentic Recombinant Pea Seed Lipoxygenases with Distinct Properties and Reaction Mechanisms
    • R.K. Hughes Z. Wu D.S. Robinson D. Hardy S.I. West S.A. Fairhurst R. Casey Characterization of Authentic Recombinant Pea Seed Lipoxygenases with Distinct Properties and Reaction Mechanisms Biochem. J. 333 1998 33 43
    • (1998) Biochem. J. , vol.333 , pp. 33-43
    • Hughes, R.K.1    Wu, Z.2    Robinson, D.S.3    Hardy, D.4    West, S.I.5    Fairhurst, S.A.6    Casey, R.7
  • 30
    • 0026134778 scopus 로고
    • Effect of Ethanol and Low Temperature Culture on Expression of Soybean Lipoxygenase L-1 in Escherichia coli
    • J. Steczko G.A. Donoho J.E. Dixon T. Sugimoto B. Axelrod Effect of Ethanol and Low Temperature Culture on Expression of Soybean Lipoxygenase L-1 in Escherichia coli Prot. Express. Purif. 2 1991 221 227
    • (1991) Prot. Express. Purif. , vol.2 , pp. 221-227
    • Steczko, J.1    Donoho, G.A.2    Dixon, J.E.3    Sugimoto, T.4    Axelrod, B.5
  • 31
    • 0028641345 scopus 로고
    • Position 713 is Critical for Catalysis but not Iron Binding in Soybean Lipoxygenase 3
    • J.A. Kramer K.R. Johnson W.R. Dunham R.H. Sands M.O. Funk Position 713 is Critical for Catalysis but not Iron Binding in Soybean Lipoxygenase 3 Biochemistry 33 1994 15017 15022
    • (1994) Biochemistry , vol.33 , pp. 15017-15022
    • Kramer, J.A.1    Johnson, K.R.2    Dunham, W.R.3    Sands, R.H.4    Funk, M.O.5
  • 35
    • 85120111245 scopus 로고    scopus 로고
    • Casey, R. Unpublished (See EMBL database accession Y18548)
  • 36
    • 0028296131 scopus 로고
    • The Primary Structure of a Lipoxygenase from the Shoots of Etiolated Lentil Seedlings Derived From its cDNA
    • M.P. Hilbers A. Rossi A. Finazzi-Agro G.A. Veldink J.F.G. Vliegenthart The Primary Structure of a Lipoxygenase from the Shoots of Etiolated Lentil Seedlings Derived From its cDNA Biochim. Biophys. Acta 1211 1994 239 242
    • (1994) Biochim. Biophys. Acta , vol.1211 , pp. 239-242
    • Hilbers, M.P.1    Rossi, A.2    Finazzi-Agro, A.3    Veldink, G.A.4    Vliegenthart, J.F.G.5
  • 37
    • 0029952657 scopus 로고    scopus 로고
    • Purification and Characterization of a Lentil Seedling Lipoxygenase Expressed in E. coli: Implications for the Mechanism of Oxodiene Formation by Lipoxygenases
    • M.P. Hilbers A. Finazzi-Agro G.A. Veldink J.F.G. Vliegenthart Purification and Characterization of a Lentil Seedling Lipoxygenase Expressed in E. coli : Implications for the Mechanism of Oxodiene Formation by Lipoxygenases Int. J. Biochem. Cell Biol. 28 1996 751 760
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 751-760
    • Hilbers, M.P.1    Finazzi-Agro, A.2    Veldink, G.A.3    Vliegenthart, J.F.G.4
  • 38
    • 0028049915 scopus 로고
    • A Novel Lipoxygenase from Rice. Primary Structure and Specific Expression Upon Incompatible Infection with Rice Blast Fungus
    • Y.-L. Peng Y. Shirano H. Ohta T. Hibino K. Tanaka D. Shibata A Novel Lipoxygenase from Rice. Primary Structure and Specific Expression Upon Incompatible Infection with Rice Blast Fungus J. Biol. Chem. 269 1994 3755 3761
    • (1994) J. Biol. Chem. , vol.269 , pp. 3755-3761
    • Peng, Y.-L.1    Shirano, Y.2    Ohta, H.3    Hibino, T.4    Tanaka, K.5    Shibata, D.6
  • 39
    • 0026578448 scopus 로고
    • cDNA Cloning of Rice Lipoxygenase L-2 and Characterization Using an Active Enzyme Expressed from the cDNA in Escherichia coli
    • H. Ohta Y. Shirano K. Tanaka Y. Morita D. Shibata cDNA Cloning of Rice Lipoxygenase L-2 and Characterization Using an Active Enzyme Expressed from the cDNA in Escherichia coli Eur. J. Biochem. 206 1992 331 336
    • (1992) Eur. J. Biochem. , vol.206 , pp. 331-336
    • Ohta, H.1    Shirano, Y.2    Tanaka, K.3    Morita, Y.4    Shibata, D.5
  • 40
    • 0029838864 scopus 로고    scopus 로고
    • Specificity of Two Lipoxygenases From Rice: Unusual Regiospecificity of a Lipoxygenase Isoenzyme
    • L.-Y. Zhang M. Hamberg Specificity of Two Lipoxygenases From Rice Unusual Regiospecificity of a Lipoxygenase Isoenzyme Lipids 31 1996 803 809
    • (1996) Lipids , vol.31 , pp. 803-809
    • Zhang, L.-Y.1    Hamberg, M.2
  • 41
    • 0029807113 scopus 로고    scopus 로고
    • Lipid Body Lipoxygenase Characterized by Protein Fragmentation, cDNA Sequence and a Very Early Expression of the Enzyme During Germination of Cucumber Seeds
    • M. Hohne A. Nellen K. Schwennesen H. Kindl Lipid Body Lipoxygenase Characterized by Protein Fragmentation, cDNA Sequence and a Very Early Expression of the Enzyme During Germination of Cucumber Seeds Eur. J. Biochem. 241 1996 6 11
    • (1996) Eur. J. Biochem. , vol.241 , pp. 6-11
    • Hohne, M.1    Nellen, A.2    Schwennesen, K.3    Kindl, H.4
  • 42
    • 0032563269 scopus 로고    scopus 로고
    • All Three Acyl Moieties of Trilinolein are Efficiently Oxygenated by Recombinant His-tagged Lipid Body Lipoxygenase in vitro
    • I. Feussner A. Bachmann M. Hohne H. Kindl All Three Acyl Moieties of Trilinolein are Efficiently Oxygenated by Recombinant His-tagged Lipid Body Lipoxygenase in vitro FEBS Lett. 431 1998 433 436
    • (1998) FEBS Lett. , vol.431 , pp. 433-436
    • Feussner, I.1    Bachmann, A.2    Hohne, M.3    Kindl, H.4
  • 44
    • 0026776366 scopus 로고
    • Expression and Secretion of Pea-seed Lipoxygenase Isoenzymes in Saccharomyces cerevisiae
    • K. Knust D. von Wettstein Expression and Secretion of Pea-seed Lipoxygenase Isoenzymes in Saccharomyces cerevisiae Appl. Microbiol. Biotech. 37 1992 342 351
    • (1992) Appl. Microbiol. Biotech. , vol.37 , pp. 342-351
    • Knust, K.1    von Wettstein, D.2
  • 45
    • 0032011685 scopus 로고    scopus 로고
    • Relation Between Positional Specificity and Chirality in Mammalian Lipoxygenases
    • S.T. Prigge J. Gaffney L.M. Amzel Relation Between Positional Specificity and Chirality in Mammalian Lipoxygenases Nature Structural Biology 5 1998 178 179
    • (1998) Nature Structural Biology , vol.5 , pp. 178-179
    • Prigge, S.T.1    Gaffney, J.2    Amzel, L.M.3
  • 46
    • 0033616797 scopus 로고    scopus 로고
    • Conversion of Cucumber Linoleate 13-lipoxygenase to a 9-lipoxygenating Species by Site-directed Mutagenesis
    • E. Hornung M. Walther H. Kühn I. Feussner Conversion of Cucumber Linoleate 13-lipoxygenase to a 9-lipoxygenating Species by Site-directed Mutagenesis Proc. Natl. Acad. Sci. USA 96 1999 4192 4197
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4192-4197
    • Hornung, E.1    Walther, M.2    Kühn, H.3    Feussner, I.4
  • 47
    • 0029864977 scopus 로고    scopus 로고
    • Structure Conservation in Lipoxygenases: Structural Analysis of Soybean Lipoxygenase-1 and Modelling of Human Lipoxygenases
    • S.T. Prigge J.C. Boyington B.J. Gaffney L.M. Amzel Structure Conservation in Lipoxygenases Structural Analysis of Soybean Lipoxygenase-1 and Modelling of Human Lipoxygenases Proteins: Structure, Function and Genetics 24 1996 275 291
    • (1996) Proteins: Structure, Function and Genetics , vol.24 , pp. 275-291
    • Prigge, S.T.1    Boyington, J.C.2    Gaffney, B.J.3    Amzel, L.M.4
  • 48
    • 0033588022 scopus 로고    scopus 로고
    • Lipoxygenases: Occurrence, Functions, Catalysis and Acquisition of Substrate
    • A.R. Brash Lipoxygenases Occurrence, Functions, Catalysis and Acquisition of Substrate J. Biol. Chem. 274 1999 23679 23682
    • (1999) J. Biol. Chem. , vol.274 , pp. 23679-23682
    • Brash, A.R.1
  • 49
    • 0027246677 scopus 로고
    • The Three-dimensional Structure of an Arachidonic Acid 15-lipoxygenase
    • J.C. Boyington B.J. Gaffney L.M. Amzel The Three-dimensional Structure of an Arachidonic Acid 15-lipoxygenase Science 260 1993 1482 1486
    • (1993) Science , vol.260 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 51
    • 0033592315 scopus 로고    scopus 로고
    • Nature of Hydrogen Transfer in Soybean Lipoxygenase 1; Separation of Primary and Secondary Isotope Effects
    • K.W. Rickert J.P. Klinman Nature of Hydrogen Transfer in Soybean Lipoxygenase 1; Separation of Primary and Secondary Isotope Effects Biochemistry 38 1999 12218 12228
    • (1999) Biochemistry , vol.38 , pp. 12218-12228
    • Rickert, K.W.1    Klinman, J.P.2
  • 52
    • 85120143200 scopus 로고
    • High Performance Liquid Chromatographic Analysis of the Products of Linoleic Acid Oxidation Catalyzed by Pea (Pisum sativum) Seed Lipoxygenases
    • Z. Wu D.S. Robinson C. Domoney R. Casey High Performance Liquid Chromatographic Analysis of the Products of Linoleic Acid Oxidation Catalyzed by Pea ( Pisum sativum ) Seed Lipoxygenases J. Agric. Food Chem. 27 1995 858 962
    • (1995) J. Agric. Food Chem. , vol.27 , pp. 858-962
    • Wu, Z.1    Robinson, D.S.2    Domoney, C.3    Casey, R.4
  • 55
    • 85120133496 scopus 로고    scopus 로고
    • Dörnenburg, H., Hunter, K.J. and Davies, C. (1999) ‘Pea Lipoxygenase-2 (LOX-2) is a Stress Related Enzyme and Appears to be Responsible for Co-oxidation of Ascorbate’. Abs. Plant Protein Club Annual Symposium “ Pathway Engineering in Plants ”, York, p.15
  • 57
    • 1842267468 scopus 로고
    • Lipoxygenase Action and Lipid Binding in Breadmaking
    • P.J. Frasier Lipoxygenase Action and Lipid Binding in Breadmaking Bakers' Digest 53 1979 8 29
    • (1979) Bakers' Digest , vol.53 , pp. 8-29
    • Frasier, P.J.1
  • 58
    • 0033028681 scopus 로고    scopus 로고
    • Kinetics of Thermal Inactivation of Pea Seed Lipoxygenases and the Effects of Additives on Their Thermostability
    • M.D. Busto R.K. Owusu-Apenten D.S. Robinson Z. Wu R. Casey R.K. Hughes Kinetics of Thermal Inactivation of Pea Seed Lipoxygenases and the Effects of Additives on Their Thermostability Food Chem. 65 1999 323 329
    • (1999) Food Chem. , vol.65 , pp. 323-329
    • Busto, M.D.1    Owusu-Apenten, R.K.2    Robinson, D.S.3    Wu, Z.4    Casey, R.5    Hughes, R.K.6
  • 59
    • 0032518266 scopus 로고    scopus 로고
    • DNA Shuffling of a Family of Genes From Diverse Species Accelerates Directed Evolution
    • A. Crameri S.-A. Raillard E. Bermudez W.P.C. Stemmer DNA Shuffling of a Family of Genes From Diverse Species Accelerates Directed Evolution Nature 391 1998 288 291
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.-A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 60
    • 0029670577 scopus 로고    scopus 로고
    • Directed Evolution of a Para-nitrobenzyl Esterase for Aqueous–Organic Solvents
    • J.C. Moore F.H. Arnold Directed Evolution of a Para-nitrobenzyl Esterase for Aqueous–Organic Solvents Nature Biotech. 14 1996 458 467
    • (1996) Nature Biotech. , vol.14 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 61
    • 0028431011 scopus 로고
    • Expression of Lipoxygenase in Wounded Tubers of Solanum tuberosum
    • A. Geerts D. Feltkamp S. Rosahl Expression of Lipoxygenase in Wounded Tubers of Solanum tuberosum Plant Physiol. 105 1994 269 277
    • (1994) Plant Physiol. , vol.105 , pp. 269-277
    • Geerts, A.1    Feltkamp, D.2    Rosahl, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.