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Volumn 85, Issue 12, 2003, Pages 1685-1693

Applications of microwaves in biological sciences

Author keywords

[No Author keywords available]

Indexed keywords


EID: 4544284955     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (62)

References (77)
  • 1
    • 0003638330 scopus 로고    scopus 로고
    • The US Chemical Industry. Copyright @ December 1996 by The American Chemical Society, American Institute of Chemical Engineering, The Chem. Manuf. Association, The Council of Chemical Resesearch, The Synthetic Org. Chem. Manuf. Association
    • Technology Vision 2020. The US Chemical Industry. Copyright @ December 1996 by The American Chemical Society, American Institute of Chemical Engineering, The Chem. Manuf. Association, The Council of Chemical Resesearch, The Synthetic Org. Chem. Manuf. Association.
    • Technology Vision 2020
  • 2
    • 0842320149 scopus 로고    scopus 로고
    • Enzymes in nonaqueous solvents: Applications in carbohydrate and peptide preparation
    • (eds Vulfson, E. N., Halling, P. J. and Holland, H. L.), Humana Press, New Jersey
    • Chen, S.-T., Sookkheo, B., Phutrahul, S. and Wang, K. T., Enzymes in nonaqueous solvents: Applications in carbohydrate and peptide preparation. In Enzymes in Nonaqueous Solvents: Methods and Protocols (eds Vulfson, E. N., Halling, P. J. and Holland, H. L.), Humana Press, New Jersey, 2001, pp. 373-400.
    • (2001) Enzymes in Nonaqueous Solvents: Methods and Protocols , pp. 373-400
    • Chen, S.-T.1    Sookkheo, B.2    Phutrahul, S.3    Wang, K.T.4
  • 3
    • 0029078472 scopus 로고
    • Microwave assisted organic reactions
    • Caddick, S., Microwave assisted organic reactions. Tetrahedron, 1995, 51, 10403-10432.
    • (1995) Tetrahedron , vol.51 , pp. 10403-10432
    • Caddick, S.1
  • 4
    • 0001024773 scopus 로고    scopus 로고
    • Microwave radiation as a catalyst for chemical reactions
    • Sridar, V., Microwave radiation as a catalyst for chemical reactions. Curr. Sci., 1998, 74, 446-450.
    • (1998) Curr. Sci. , vol.74 , pp. 446-450
    • Sridar, V.1
  • 6
    • 0037421895 scopus 로고    scopus 로고
    • Microwave chemistry: Out of the kitchen
    • Adam, D., Microwave chemistry: Out of the kitchen. Nature, 2003, 421, 571-572.
    • (2003) Nature , vol.421 , pp. 571-572
    • Adam, D.1
  • 7
    • 37049067241 scopus 로고
    • Microwave-assisted solid-state reactions involving metal powders
    • Whittaker, A. G. and Mingos, D. M. P., Microwave-assisted solid-state reactions involving metal powders. J. Chem. Soc., Dalton Trans., 1995, 2073-2079.
    • (1995) J. Chem. Soc., Dalton Trans. , pp. 2073-2079
    • Whittaker, A.G.1    Mingos, D.M.P.2
  • 8
    • 0036603599 scopus 로고    scopus 로고
    • High-speed combinatorial synthesis utilizing microwave irradiation
    • Kappe, C. O., High-speed combinatorial synthesis utilizing microwave irradiation. Curr. Opin. Chem. Biol., 2002, 6, 314-320.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 314-320
    • Kappe, C.O.1
  • 9
    • 0031047588 scopus 로고    scopus 로고
    • Non-thermal effects of microwaves on proteins: Thermophilic enzymes as model system
    • Porcelli, M. et al., Non-thermal effects of microwaves on proteins: thermophilic enzymes as model system. FEBS Lett., 1997, 402, 102-106.
    • (1997) FEBS Lett. , vol.402 , pp. 102-106
    • Porcelli, M.1
  • 13
    • 0347869990 scopus 로고    scopus 로고
    • Microwave exposure effect on a thermophilic alcohol dehydrogenase
    • Le Cara, F. et al., Microwave exposure effect on a thermophilic alcohol dehydrogenase. Protein Peptide Lett., 1999, 6, 155-162.
    • (1999) Protein Peptide Lett. , vol.6 , pp. 155-162
    • Le Cara, F.1
  • 14
    • 0013111767 scopus 로고    scopus 로고
    • Effect of microwave radiation on copper (II) 2,2′-bipyridyl- mediated hydrolysis of bis(p-nitrophenyl) phosphodiester and enzymatic hydrolysis of carbohydrates
    • Kabza, K. C., Gestwicki, J. E., McGrath, J. L. and Petrassi, H. M., Effect of microwave radiation on copper (II) 2,2′-bipyridyl-mediated hydrolysis of bis(p-nitrophenyl) phosphodiester and enzymatic hydrolysis of carbohydrates. J. Org. Chem., 1996, 61, 9599-9602.
    • (1996) J. Org. Chem. , vol.61 , pp. 9599-9602
    • Kabza, K.C.1    Gestwicki, J.E.2    McGrath, J.L.3    Petrassi, H.M.4
  • 15
    • 0026517617 scopus 로고    scopus 로고
    • Enzyme function in organic solvents
    • Gupta, M. N., Enzyme function in organic solvents. Eur. J. Biochem., 2002, 203, 25-32.
    • (2002) Eur. J. Biochem. , vol.203 , pp. 25-32
    • Gupta, M.N.1
  • 16
    • 0026892825 scopus 로고
    • Designing enzymes for use in organic solvents
    • Dordick, J. S., Designing enzymes for use in organic solvents. Biotechnol. Prog., 1992, 8, 259-267.
    • (1992) Biotechnol. Prog. , vol.8 , pp. 259-267
    • Dordick, J.S.1
  • 19
    • 0021763770 scopus 로고
    • Enzymatic catalysis in organic media at 100 degrees C
    • Zaks, A. and Klibanov, A. M., Enzymatic catalysis in organic media at 100 degrees C. Science, 1984, 224, 1249-1251.
    • (1984) Science , vol.224 , pp. 1249-1251
    • Zaks, A.1    Klibanov, A.M.2
  • 21
    • 0036669618 scopus 로고    scopus 로고
    • Enzyme activation for nonaqueous media
    • Lee, M.-Y. and Dordick, J. S., Enzyme activation for nonaqueous media. Curr. Opin. Biotechnol., 2002, 13, 376-384.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 376-384
    • Lee, M.-Y.1    Dordick, J.S.2
  • 22
    • 0024297108 scopus 로고
    • Inhibitor-induced enzyme activation in organic solvents
    • Russel, A. J. and Klibanov, A. M., Inhibitor-induced enzyme activation in organic solvents. J. Biol. Chem., 1988, 263, 11624-11626.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11624-11626
    • Russel, A.J.1    Klibanov, A.M.2
  • 23
    • 0034632430 scopus 로고    scopus 로고
    • Enhancing the enantioselectivity of lipase in transesterification by substrate matching: An enzyme memory based approach
    • Lee, D., Choi, Y. K. and Kim, M. J., Enhancing the enantioselectivity of lipase in transesterification by substrate matching: An enzyme memory based approach. Org. Lett., 2000, 2, 2553-2555.
    • (2000) Org. Lett. , vol.2 , pp. 2553-2555
    • Lee, D.1    Choi, Y.K.2    Kim, M.J.3
  • 25
    • 0035907697 scopus 로고    scopus 로고
    • Protein crystals as novel catalytic materials
    • Margolin, A. L. and Navia, M. A., Protein crystals as novel catalytic materials. Angew. Chem., Int. Ed. Engl., 2001, 40, 2204-2222.
    • (2001) Angew. Chem., Int. Ed. Engl. , vol.40 , pp. 2204-2222
    • Margolin, A.L.1    Navia, M.A.2
  • 27
    • 0000153467 scopus 로고    scopus 로고
    • Microwave-promoted lipase-catalysed reactions. Resolution of (±)-1-phenylethanol
    • Carrillo-Munoz, J.-R., Bouvet, D., Guibe-Jampel, E., Loupy, A. and Petit, A., Microwave-promoted lipase-catalysed reactions. Resolution of (±)-1-phenylethanol. J. Org. Chem., 1996, 61, 7746-7749.
    • (1996) J. Org. Chem. , vol.61 , pp. 7746-7749
    • Carrillo-Munoz, J.-R.1    Bouvet, D.2    Guibe-Jampel, E.3    Loupy, A.4    Petit, A.5
  • 28
    • 2142747977 scopus 로고
    • Introduction: The current status of immobilized protein technique
    • (ed. Taylor, R. F.), Marcel Dekker Inc, New York
    • Taylor, R. F., Introduction: The current status of immobilized protein technique. In Protein Immobilization: Fundamentals and Applications (ed. Taylor, R. F.), Marcel Dekker Inc, New York, 1991, pp. 1-10.
    • (1991) Protein Immobilization: Fundamentals and Applications , pp. 1-10
    • Taylor, R.F.1
  • 29
    • 0036905653 scopus 로고    scopus 로고
    • Factors governing the activity of lyophilised and immobilised lipase preparations in organic solvents
    • Persson, M., Wehtje, E. and Adlercreutz, P., Factors governing the activity of lyophilised and immobilised lipase preparations in organic solvents. ChemBiochem., 2002, 3, 566-571.
    • (2002) ChemBiochem. , vol.3 , pp. 566-571
    • Persson, M.1    Wehtje, E.2    Adlercreutz, P.3
  • 30
    • 0037330573 scopus 로고    scopus 로고
    • Synthesis of antioxidant propyl gallate using tannase from Aspergillus niger van Teighem in nonaqueous media
    • Sharma, S. and Gupta, M. N., Synthesis of antioxidant propyl gallate using tannase from Aspergillus niger van Teighem in nonaqueous media. Bioorg. Med. Chem. Lett., 2003, 13, 395-397.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 395-397
    • Sharma, S.1    Gupta, M.N.2
  • 31
    • 78049302791 scopus 로고    scopus 로고
    • Enzymatic conversions in organic and other low-water media
    • (eds Drauz, K. and Waldmann, H.), Wiley-VCH, Weinheim
    • Halling, P., Enzymatic conversions in organic and other low-water media. In Enzyme Catalysis in Organic Solvents (eds Drauz, K. and Waldmann, H.), Wiley-VCH, Weinheim, 2002, pp. 259-285.
    • (2002) Enzyme Catalysis in Organic Solvents , pp. 259-285
    • Halling, P.1
  • 32
    • 0030580312 scopus 로고    scopus 로고
    • Microwave radiation can increase the rate of enzyme-catalysed reactions in organic media
    • Parker, M.-C., Besson, T., Lamare, S. and Legoy, M.-D., Microwave radiation can increase the rate of enzyme-catalysed reactions in organic media. Tetrahedron Lett., 1996, 37, 8383-8386.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 8383-8386
    • Parker, M.-C.1    Besson, T.2    Lamare, S.3    Legoy, M.-D.4
  • 34
    • 0032507928 scopus 로고    scopus 로고
    • Microwave-promoted lipase-catalysed reactions
    • Lin, G. and Lin, W.-Y., Microwave-promoted lipase-catalysed reactions. Tetrahedron Lett., 1998, 39, 4333-4336.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 4333-4336
    • Lin, G.1    Lin, W.-Y.2
  • 35
    • 0037129173 scopus 로고    scopus 로고
    • Microwave-assisted rapid characterization of lipase selectivities
    • Bradoo, S., Rathi, P., Saxena, R. K. and Gupta, R., Microwave-assisted rapid characterization of lipase selectivities. J. Biochem. Biophys. Methods, 2002, 51, 115-120.
    • (2002) J. Biochem. Biophys. Methods , vol.51 , pp. 115-120
    • Bradoo, S.1    Rathi, P.2    Saxena, R.K.3    Gupta, R.4
  • 36
    • 0037707570 scopus 로고    scopus 로고
    • Non-thermal effects of microwaves on protease-catalysed esterification and transesterification
    • Roy, I. and Gupta, M. N., Non-thermal effects of microwaves on protease-catalysed esterification and transesterification. Tetrahedron, 2003, 59, 5431-5436.
    • (2003) Tetrahedron , vol.59 , pp. 5431-5436
    • Roy, I.1    Gupta, M.N.2
  • 37
    • 44949276637 scopus 로고
    • Tailoring the microenvironment of enzymes in water-poor systems
    • Mattiasson, B. and Adlercreutz, P., Tailoring the microenvironment of enzymes in water-poor systems. Trends Biotechnol., 1991, 9, 394-398.
    • (1991) Trends Biotechnol. , vol.9 , pp. 394-398
    • Mattiasson, B.1    Adlercreutz, P.2
  • 38
    • 0344240989 scopus 로고    scopus 로고
    • Enzyme inactivation analysis for industrial blanching applications: Comparison of microwave, conventional, and combination heat treatments on mushroom polyphenoloxidase activity
    • Devece, C., Rodriguez-Lopez, J. N., Fenoll, L. G., Tudela, J., Catala, J. M., de Los Reyes, E. and Garcia-Canovas, F., Enzyme inactivation analysis for industrial blanching applications: comparison of microwave, conventional, and combination heat treatments on mushroom polyphenoloxidase activity. J. Agric. Food Chem., 1999, 47, 4506-4511.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4506-4511
    • Devece, C.1    Rodriguez-Lopez, J.N.2    Fenoll, L.G.3    Tudela, J.4    Catala, J.M.5    De Los Reyes, E.6    Garcia-Canovas, F.7
  • 40
    • 0029348528 scopus 로고
    • Ultrafast protein determinations using microwave enhancement
    • Akins, R. E. and Tuan, R. S., Ultrafast protein determinations using microwave enhancement. Mol. Biotechnol., 1995, 4, 17-24.
    • (1995) Mol. Biotechnol. , vol.4 , pp. 17-24
    • Akins, R.E.1    Tuan, R.S.2
  • 41
    • 0036903608 scopus 로고    scopus 로고
    • A microassay for protein determination using microwaves
    • Jain, S., Sharma, S. and Gupta, M. N., A microassay for protein determination using microwaves. Anal. Biochem., 2002, 311, 84-86.
    • (2002) Anal. Biochem. , vol.311 , pp. 84-86
    • Jain, S.1    Sharma, S.2    Gupta, M.N.3
  • 43
    • 4544298965 scopus 로고    scopus 로고
    • www.chitosan.or.kr
  • 44
    • 0034666256 scopus 로고    scopus 로고
    • Combination therapy with transcatheter arterial chemoembolization and percutaneous microwave coagulation therapy for hepatocellular carcinoma
    • Seki, T. et al., Combination therapy with transcatheter arterial chemoembolization and percutaneous microwave coagulation therapy for hepatocellular carcinoma. Cancer, 2000, 89, 1245-1251.
    • (2000) Cancer , vol.89 , pp. 1245-1251
    • Seki, T.1
  • 45
    • 0030640879 scopus 로고    scopus 로고
    • Circulatory failure induced by 35 GHz microwave heating: Effects of chronic nitric oxide synthesis inhibition
    • Ryan, K. L., Frei, M. R. and Jauchem, J. R., Circulatory failure induced by 35 GHz microwave heating: effects of chronic nitric oxide synthesis inhibition. Shock, 1997, 7, 70-76.
    • (1997) Shock , vol.7 , pp. 70-76
    • Ryan, K.L.1    Frei, M.R.2    Jauchem, J.R.3
  • 46
    • 0035543353 scopus 로고    scopus 로고
    • Do enzymatic digestibility and Simons' stain reflect the differences in the available surface area of lignocellulosic substrates
    • Esteghlalian, A. R., Bilodeau, M., Mansfield, S. D. and Saddler, J. N., Do enzymatic digestibility and Simons' stain reflect the differences in the available surface area of lignocellulosic substrates. Biotechnol. Prog., 2001, 17, 1049-1054.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 1049-1054
    • Esteghlalian, A.R.1    Bilodeau, M.2    Mansfield, S.D.3    Saddler, J.N.4
  • 47
    • 0036237115 scopus 로고    scopus 로고
    • Enhancing the enzymatic hydrolysis of cellulosic materials using simultaneous ball milling
    • Mais, U., Esteghlalian, A. R., Saddler, J. N. and Mansfield, S. D., Enhancing the enzymatic hydrolysis of cellulosic materials using simultaneous ball milling. Appl. Biochem. Biotechnol., 2002, 98-100, 815-832.
    • (2002) Appl. Biochem. Biotechnol. , vol.98-100 , pp. 815-832
    • Mais, U.1    Esteghlalian, A.R.2    Saddler, J.N.3    Mansfield, S.D.4
  • 48
    • 0036510825 scopus 로고    scopus 로고
    • Hydrogenolysis of lignins: Influence of the pretreatment using microwave and ultrasound irradiations
    • Goncalves, A. R. and Schuchardt, U., Hydrogenolysis of lignins: influence of the pretreatment using microwave and ultrasound irradiations. Appl. Biochem. Biotechnol., 2002, 98-100, 1213-1219.
    • (2002) Appl. Biochem. Biotechnol. , vol.98-100 , pp. 1213-1219
    • Goncalves, A.R.1    Schuchardt, U.2
  • 49
    • 4544295885 scopus 로고    scopus 로고
    • patent 5196069
    • http://ettc.usc.edu/Jsc/cellulose; patent 5196069.
  • 50
    • 0028452866 scopus 로고
    • Immobilization of chitinase on a reversibly soluble-insoluble polymer for chitin hydrolysis
    • Chen, J. P. and Chang, K. C., Immobilization of chitinase on a reversibly soluble-insoluble polymer for chitin hydrolysis. J. Chem. Technol. Biotechnol., 1994, 60, 133-140.
    • (1994) J. Chem. Technol. Biotechnol. , vol.60 , pp. 133-140
    • Chen, J.P.1    Chang, K.C.2
  • 51
    • 0022729935 scopus 로고
    • Enzymatic degradation of chitin and its biological applications
    • Deshpande, M. V., Enzymatic degradation of chitin and its biological applications. J. Sci. Ind. Res., 1986, 45, 277-281.
    • (1986) J. Sci. Ind. Res. , vol.45 , pp. 277-281
    • Deshpande, M.V.1
  • 52
    • 0006564263 scopus 로고
    • Determining optimum conditions
    • (eds Khuri, A. I. and Cornell, J. A.), Marcel Dekker, New York
    • Khuri, A. I. and Cornell, J. A., Determining optimum conditions. In Response Surface Design and Analyses (eds Khuri, A. I. and Cornell, J. A.), Marcel Dekker, New York, 1987, pp. 149-205.
    • (1987) Response Surface Design and Analyses , pp. 149-205
    • Khuri, A.I.1    Cornell, J.A.2
  • 53
    • 0033972586 scopus 로고    scopus 로고
    • Statistical optimization of medium for the production of recombinant hirudin from Saccharomyces cerevisiae using response surface methodology
    • Rao, K. J., Kim, C.-H. and Rhee, S.-K., Statistical optimization of medium for the production of recombinant hirudin from Saccharomyces cerevisiae using response surface methodology. Process Biochem., 2000, 35, 639-647.
    • (2000) Process Biochem. , vol.35 , pp. 639-647
    • Rao, K.J.1    Kim, C.-H.2    Rhee, S.-K.3
  • 54
    • 0346661602 scopus 로고    scopus 로고
    • Accelerating enzymatic hydrolysis of chitin by microwave pre-treatment
    • Roy, I., Mondal, K. and Gupta, M. N., Accelerating enzymatic hydrolysis of chitin by microwave pre-treatment. Biotechnol. Prog., 2003, 19, 1648-1653.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1648-1653
    • Roy, I.1    Mondal, K.2    Gupta, M.N.3
  • 55
    • 0023996274 scopus 로고
    • Protein design for non-aqueous solvents
    • Arnold, F. H., Protein design for non-aqueous solvents. Protein Eng., 1988, 2, 21-25.
    • (1988) Protein Eng. , vol.2 , pp. 21-25
    • Arnold, F.H.1
  • 56
    • 0033693921 scopus 로고    scopus 로고
    • Cycloadditions under microwave irradiation conditions: Methods and applications
    • de la Hoz, A., Diaz-Ortis, A., Moreno, A. and Langa, F., Cycloadditions under microwave irradiation conditions: methods and applications. Eur. J. Org. Chem., 2000, 22, 3659-3673.
    • (2000) Eur. J. Org. Chem. , vol.22 , pp. 3659-3673
    • De La Hoz, A.1    Diaz-Ortis, A.2    Moreno, A.3    Langa, F.4
  • 59
    • 4544364747 scopus 로고    scopus 로고
    • Eur. Patent Appl. EP 905, 199 (1999)
    • Badejo, I. T., Eur. Patent Appl. EP 905, 199 (1999).
    • Badejo, I.T.1
  • 61
    • 77956909282 scopus 로고
    • Bovine pancreatic ribonuclease
    • (ed. Boyer, P.), Academic Press, New York, 3rd edn
    • Richards, F. M. and Wyckoff, H. W., Bovine pancreatic ribonuclease. In The Enzymes (ed. Boyer, P.), Academic Press, New York, 1971, vol. 4, 3rd edn, pp. 647-806.
    • (1971) The Enzymes , vol.4 , pp. 647-806
    • Richards, F.M.1    Wyckoff, H.W.2
  • 62
    • 52849120818 scopus 로고    scopus 로고
    • Use of the pH memory effect in lyophilized proteins to achieve preferential methylation of alpha-amino groups
    • Vakos, H. T., Kaplan, H., Black, B., Dawson, B. and Hefford, M. A., Use of the pH memory effect in lyophilized proteins to achieve preferential methylation of alpha-amino groups. J. Protein Chem., 2000, 19, 231-237.
    • (2000) J. Protein Chem. , vol.19 , pp. 231-237
    • Vakos, H.T.1    Kaplan, H.2    Black, B.3    Dawson, B.4    Hefford, M.A.5
  • 63
    • 0032530679 scopus 로고    scopus 로고
    • Candida rugosa lipases: Molecular biology and versatility in biotechnology
    • Benjamin, S. and Pandey, A., Candida rugosa lipases: molecular biology and versatility in biotechnology. Yeast, 1998, 14, 1069-1087.
    • (1998) Yeast , vol.14 , pp. 1069-1087
    • Benjamin, S.1    Pandey, A.2
  • 64
    • 0035923383 scopus 로고    scopus 로고
    • Production of biodiesel fuel from triglycerides and alcohol using immobilized lipase
    • Iso, M., Chen, B., Eguchi, M., Kudo, T. and Shreshtha, S., Production of biodiesel fuel from triglycerides and alcohol using immobilized lipase. J. Mol. Catal. B, Enzymes, 2001, 16, 53-58.
    • (2001) J. Mol. Catal. B, Enzymes , vol.16 , pp. 53-58
    • Iso, M.1    Chen, B.2    Eguchi, M.3    Kudo, T.4    Shreshtha, S.5
  • 65
    • 0025611814 scopus 로고
    • Continuous peptide synthesis in a water-immiscible organic solvent with an immobilized enzyme
    • Nakanishi, K. and Matsuno, R., Continuous peptide synthesis in a water-immiscible organic solvent with an immobilized enzyme. Ann. N. Y. Acad. Sci., 1990, 613, 652-655.
    • (1990) Ann. N. Y. Acad. Sci. , vol.613 , pp. 652-655
    • Nakanishi, K.1    Matsuno, R.2
  • 66
    • 0032888135 scopus 로고    scopus 로고
    • Lipase-catalysed synthesis of (S)-naproxen ester prodrug by transesterification in organic solvents
    • Tsai, S. W., Tsai, C. S. and Chang, C. S., Lipase-catalysed synthesis of (S)-naproxen ester prodrug by transesterification in organic solvents. Appl. Biochem. Biotechnol., 1999, 80, 205-219.
    • (1999) Appl. Biochem. Biotechnol. , vol.80 , pp. 205-219
    • Tsai, S.W.1    Tsai, C.S.2    Chang, C.S.3
  • 67
    • 0343453824 scopus 로고
    • New approaches to the enzymatic production of oligopeptides: Synthesis of the 'delicious peptide' and its fragments
    • (eds Galindo, E. and Ramirez, O. T.), Kluwer Academic Publishers, Amsterdam
    • Gill, I., Lopez-Fandino, R., Jorba, X. and Vulfson, E., New approaches to the enzymatic production of oligopeptides: Synthesis of the 'delicious peptide' and its fragments. In Advances in Bioprocess Engineering (eds Galindo, E. and Ramirez, O. T.), Kluwer Academic Publishers, Amsterdam, 1994, pp. 485-488.
    • (1994) Advances in Bioprocess Engineering , pp. 485-488
    • Gill, I.1    Lopez-Fandino, R.2    Jorba, X.3    Vulfson, E.4
  • 68
    • 0038355298 scopus 로고    scopus 로고
    • Studies on the optimized lipase-catalysed biosynthesis of cis-3-hexen-1-yl acetate in n-hexane
    • Chiang, W.-D., Chang, S.-W. and Shieh, C.-J., Studies on the optimized lipase-catalysed biosynthesis of cis-3-hexen-1-yl acetate in n-hexane. Process Biochem., 2003, 38, 1193-1199.
    • (2003) Process Biochem. , vol.38 , pp. 1193-1199
    • Chiang, W.-D.1    Chang, S.-W.2    Shieh, C.-J.3
  • 69
    • 0001384031 scopus 로고
    • High-oleic acid rapeseed oil as starting material for the production of confectionary fats via lipase-catalysed transesterification
    • Gitleson, T., Svensson, I., Adlercreutz, P., Mattiasson, B. and Nilsson, J., High-oleic acid rapeseed oil as starting material for the production of confectionary fats via lipase-catalysed transesterification. Indian Crops Prod., 1995, 4, 167-171.
    • (1995) Indian Crops Prod. , vol.4 , pp. 167-171
    • Gitleson, T.1    Svensson, I.2    Adlercreutz, P.3    Mattiasson, B.4    Nilsson, J.5
  • 70
    • 0032800489 scopus 로고    scopus 로고
    • Enzymatic synthesis and modification of polymers in nonaqueous solvents
    • Akkara, J. A., Ayyagari, M. S. R. and Bruno, F. F., Enzymatic synthesis and modification of polymers in nonaqueous solvents. Trends Biotechnol., 1999, 17, 67-73.
    • (1999) Trends Biotechnol. , vol.17 , pp. 67-73
    • Akkara, J.A.1    Ayyagari, M.S.R.2    Bruno, F.F.3
  • 72
    • 0035809096 scopus 로고    scopus 로고
    • Phospholipase D-catalysed transphosphatidylation in anhydrous organic solvents
    • Rich, J. O. and Khmelnitsky, Y. L., Phospholipase D-catalysed transphosphatidylation in anhydrous organic solvents. Biotechnol. Bioeng., 2001, 72, 374-377.
    • (2001) Biotechnol. Bioeng. , vol.72 , pp. 374-377
    • Rich, J.O.1    Khmelnitsky, Y.L.2
  • 73
    • 0037587485 scopus 로고    scopus 로고
    • Lipase-catalysed enantioselective ring opening of unactivated alicyclic-fused β-lactams in an organic solvent
    • Foro, E. and Fulop, F., Lipase-catalysed enantioselective ring opening of unactivated alicyclic-fused β-lactams in an organic solvent. Org. Lett., 2003, 5, 1209-1212.
    • (2003) Org. Lett. , vol.5 , pp. 1209-1212
    • Foro, E.1    Fulop, F.2
  • 75
    • 84988112821 scopus 로고
    • Enzymes in organic synthesis IX: Enzymatic acylation of the cyclic secondary amines
    • Djeghaba, Z. and De Jeso, B., Enzymes in organic synthesis IX: Enzymatic acylation of the cyclic secondary amines. Bull. Ploughshare. Chim. Belg., 1995, 104, 161-164.
    • (1995) Bull. Ploughshare. Chim. Belg. , vol.104 , pp. 161-164
    • Djeghaba, Z.1    De Jeso, B.2
  • 76
    • 0037468242 scopus 로고    scopus 로고
    • Modification of flavonoid using lipase in non-conventional media: Effect of the water content
    • Gayot, S., Santarelli, X. and Coulon, D., Modification of flavonoid using lipase in non-conventional media: effect of the water content. J. Biotechnol., 2003, 101, 29-36.
    • (2003) J. Biotechnol. , vol.101 , pp. 29-36
    • Gayot, S.1    Santarelli, X.2    Coulon, D.3
  • 77
    • 0003185575 scopus 로고
    • A simple procedure for the preparation of chiral amides
    • Gotor, V., Brieva, R. and Rebolledo, F., A simple procedure for the preparation of chiral amides. Tetrahedron Lett., 1988, 29, 6973-6974.
    • (1988) Tetrahedron Lett. , vol.29 , pp. 6973-6974
    • Gotor, V.1    Brieva, R.2    Rebolledo, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.