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Volumn 54, Issue 38, 2015, Pages 5969-5979

Interfacial Activation of Candida antarctica Lipase B: Combined Evidence from Experiment and Simulation

Author keywords

[No Author keywords available]

Indexed keywords

BINS; CANDIDA; CHEMICAL ACTIVATION; ENZYME IMMOBILIZATION; ENZYMES; HYDROPHOBICITY; INTERFACES (MATERIALS); ISOMERS; MOLECULAR DYNAMICS; SUBSTRATES; SURFACE CHEMISTRY; YEAST;

EID: 84942684009     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00586     Document Type: Article
Times cited : (123)

References (55)
  • 1
    • 0031023666 scopus 로고    scopus 로고
    • 'Interfacial activation' of lipases: Facts and artifacts
    • Verger, R. (1997),Interfacial activation' of lipases: Facts and artifacts Trends Biotechnol. 15, 32-38 10.1016/S0167-7799(96)10064-0
    • (1997) Trends Biotechnol. , vol.15 , pp. 32-38
    • Verger, R.1
  • 2
    • 0033653715 scopus 로고    scopus 로고
    • What distinguishes an esterase from a lipase: A novel structural approach
    • Fojan, P., Jonson, P. H., Petersen, M. T. N., and Petersen, S. B. (2000) What distinguishes an esterase from a lipase: A novel structural approach Biochimie 82, 1033-1041 10.1016/S0300-9084(00)01188-3
    • (2000) Biochimie , vol.82 , pp. 1033-1041
    • Fojan, P.1    Jonson, P.H.2    Petersen, M.T.N.3    Petersen, S.B.4
  • 4
    • 33846209146 scopus 로고    scopus 로고
    • Trends in lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds
    • Ghanem, A. (2007) Trends in lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds Tetrahedron 63, 1721-1754 10.1016/j.tet.2006.09.110
    • (2007) Tetrahedron , vol.63 , pp. 1721-1754
    • Ghanem, A.1
  • 6
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • Derewenda, U., Brzozowski, A. M., Lawson, D. M., and Derewenda, Z. S. (1992) Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase Biochemistry 31, 1532-1541 10.1021/bi00120a034
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 7
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: Interfacial Enzymes with Attractive Applications
    • Schmid, R. D. and Verger, R. (1998) Lipases: Interfacial Enzymes with Attractive Applications Angew. Chem., Int. Ed. 37, 1608-1633 10.1002/(SICI)1521-3773(19980703)37:12<1608::AID-ANIE1608>3.3.CO;2-M
    • (1998) Angew. Chem., Int. Ed. , vol.37 , pp. 1608-1633
    • Schmid, R.D.1    Verger, R.2
  • 8
    • 84880105945 scopus 로고    scopus 로고
    • Immobilisation and application of lipases in organic media
    • Adlercreutz, P. (2013) Immobilisation and application of lipases in organic media Chem. Soc. Rev. 42, 6406-6436 10.1039/c3cs35446f
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 6406-6436
    • Adlercreutz, P.1
  • 9
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Uppenberg, J., Hansen, M. T., Patkar, S., and Jones, T. A. (1994) The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica Structure 2, 293-308 10.1016/S0969-2126(00)00031-9
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 10
    • 0029417196 scopus 로고
    • Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols
    • Uppenberg, J., Oehrner, N., Norin, M., Hult, K., Kleywegt, G. J., Patkar, S., Waagen, V., Anthonsen, T., and Jones, T. A. (1995) Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols Biochemistry 34, 16838-16851 10.1021/bi00051a035
    • (1995) Biochemistry , vol.34 , pp. 16838-16851
    • Uppenberg, J.1    Oehrner, N.2    Norin, M.3    Hult, K.4    Kleywegt, G.J.5    Patkar, S.6    Waagen, V.7    Anthonsen, T.8    Jones, T.A.9
  • 11
    • 84995904548 scopus 로고    scopus 로고
    • Genome Sequence of the Basidiomycetous Yeast Pseudozyma antarctica T-34, a Producer of the Glycolipid Biosurfactants Mannosylerythritol Lipids
    • Morita, T., Koike, H., Koyama, Y., Hagiwara, H., Ito, E., Fukuoka, T., Imura, T., Machida, M., and Kitamoto, D. (2013) Genome Sequence of the Basidiomycetous Yeast Pseudozyma antarctica T-34, a Producer of the Glycolipid Biosurfactants Mannosylerythritol Lipids Genome Announc. 1, e0006413 10.1128/genomeA.00064-13
    • (2013) Genome Announc. , vol.1 , pp. e0006413
    • Morita, T.1    Koike, H.2    Koyama, Y.3    Hagiwara, H.4    Ito, E.5    Fukuoka, T.6    Imura, T.7    Machida, M.8    Kitamoto, D.9
  • 12
    • 0031795317 scopus 로고    scopus 로고
    • One biocatalyst - Many applications: The use of Candida antarctica B-Lipase in organic synthesis
    • Anderson, E. M., Larsson, K. M., and Kirk, O. (1998) One biocatalyst-many applications: The use of Candida antarctica B-Lipase in organic synthesis Biocatal. Biotransform. 16, 181-204 10.3109/10242429809003198
    • (1998) Biocatal. Biotransform. , vol.16 , pp. 181-204
    • Anderson, E.M.1    Larsson, K.M.2    Kirk, O.3
  • 13
    • 60349109395 scopus 로고    scopus 로고
    • Understanding the Plasticity of the α/β Hydrolase Fold: Lid Swapping on the Candida antarctica Lipase B Results in Chimeras with Interesting Biocatalytic Properties
    • Skjøt, M., De Maria, L., Chatterjee, R., Svendsen, A., Patkar, S. A., Østergaard, P. R., and Brask, J. (2009) Understanding the Plasticity of the α/β Hydrolase Fold: Lid Swapping on the Candida antarctica Lipase B Results in Chimeras with Interesting Biocatalytic Properties ChemBioChem 10, 520-527 10.1002/cbic.200800668
    • (2009) ChemBioChem , vol.10 , pp. 520-527
    • Skjøt, M.1    De Maria, L.2    Chatterjee, R.3    Svendsen, A.4    Patkar, S.A.5    Østergaard, P.R.6    Brask, J.7
  • 14
    • 0037025268 scopus 로고    scopus 로고
    • Modulation of the enantioselectivity of Candida antarctica B lipase via conformational engineering. Kinetic resolution of (±)-α-hydroxy-phenylacetic acid derivatives
    • Palomo, J. M., Fernández-Lorente, G., Mateo, C., Fuentes, M., Fernández-Lafuente, R., and Guisan, J. M. (2002) Modulation of the enantioselectivity of Candida antarctica B lipase via conformational engineering. Kinetic resolution of (±)-α-hydroxy-phenylacetic acid derivatives Tetrahedron: Asymmetry 13, 1337-1345 10.1016/S0957-4166(02)00325-7
    • (2002) Tetrahedron: Asymmetry , vol.13 , pp. 1337-1345
    • Palomo, J.M.1    Fernández-Lorente, G.2    Mateo, C.3    Fuentes, M.4    Fernández-Lafuente, R.5    Guisan, J.M.6
  • 15
    • 50449108577 scopus 로고    scopus 로고
    • Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties
    • Fernandez-Lorente, G., Cabrera, Z., Godoy, C., Fernandez-Lafuente, R., Palomo, J. M., and Guisan, J. M. (2008) Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties Process Biochem. 43, 1061-1067 10.1016/j.procbio.2008.05.009
    • (2008) Process Biochem. , vol.43 , pp. 1061-1067
    • Fernandez-Lorente, G.1    Cabrera, Z.2    Godoy, C.3    Fernandez-Lafuente, R.4    Palomo, J.M.5    Guisan, J.M.6
  • 16
    • 68649084001 scopus 로고    scopus 로고
    • Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports
    • Cabrera, Z., Fernandez-Lorente, G., Fernandez-Lafuente, R., Palomo, J. M., and Guisan, J. M. (2009) Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports J. Mol. Catal. B: Enzym. 57, 171-176 10.1016/j.molcatb.2008.08.012
    • (2009) J. Mol. Catal. B: Enzym. , vol.57 , pp. 171-176
    • Cabrera, Z.1    Fernandez-Lorente, G.2    Fernandez-Lafuente, R.3    Palomo, J.M.4    Guisan, J.M.5
  • 17
    • 0031965757 scopus 로고    scopus 로고
    • Chiral Recognition of Alcohol Enantiomers in Acyl Transfer Reactions Catalysed by Candida antarctica Lipase B
    • Orrenius, C., Hæffner, F., Rotticci, D., Öhrner, N., Norin, T., and Hult, K. (1998) Chiral Recognition Of Alcohol Enantiomers In Acyl Transfer Reactions Catalysed By Candida antarctica Lipase B Biocatal. Biotransform. 16, 1-15 10.3109/10242429809040107
    • (1998) Biocatal. Biotransform. , vol.16 , pp. 1-15
    • Orrenius, C.1    Hæffner, F.2    Rotticci, D.3    Öhrner, N.4    Norin, T.5    Hult, K.6
  • 18
    • 0034848412 scopus 로고    scopus 로고
    • Rational design of enantioselective enzymes requires considerations of entropy
    • Ottosson, J., Rotticci-Mulder, J. C., Rotticci, D., and Hult, K. (2001) Rational design of enantioselective enzymes requires considerations of entropy Protein Sci. 10, 1769-1774 10.1110/ps.13501
    • (2001) Protein Sci. , vol.10 , pp. 1769-1774
    • Ottosson, J.1    Rotticci-Mulder, J.C.2    Rotticci, D.3    Hult, K.4
  • 19
    • 20444448921 scopus 로고    scopus 로고
    • Creating Space for Large Secondary Alcohols by Rational Redesign of Candida antarctica Lipase B
    • Magnusson, A. O., Rotticci-Mulder, J. C., Santagostino, A., and Hult, K. (2005) Creating Space for Large Secondary Alcohols by Rational Redesign of Candida antarctica Lipase B ChemBioChem 6, 1051-1056 10.1002/cbic.200400410
    • (2005) ChemBioChem , vol.6 , pp. 1051-1056
    • Magnusson, A.O.1    Rotticci-Mulder, J.C.2    Santagostino, A.3    Hult, K.4
  • 20
    • 22744445622 scopus 로고    scopus 로고
    • An S-Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature
    • Magnusson, A. O., Takwa, M., Hamberg, A., and Hult, K. (2005) An S-Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature Angew. Chem., Int. Ed. 44, 4582-4585 10.1002/anie.200500971
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 4582-4585
    • Magnusson, A.O.1    Takwa, M.2    Hamberg, A.3    Hult, K.4
  • 22
    • 78649448002 scopus 로고    scopus 로고
    • Engineering of Candida antarctica lipase B for hydrolysis of bulky carboxylic acid esters
    • Juhl, P. B., Doderer, K., Hollmann, F., Thum, O., and Pleiss, J. (2010) Engineering of Candida antarctica lipase B for hydrolysis of bulky carboxylic acid esters J. Biotechnol. 150, 474-480 10.1016/j.jbiotec.2010.09.951
    • (2010) J. Biotechnol. , vol.150 , pp. 474-480
    • Juhl, P.B.1    Doderer, K.2    Hollmann, F.3    Thum, O.4    Pleiss, J.5
  • 23
    • 25844525807 scopus 로고    scopus 로고
    • Improving the catalytic activity of Candida antarctica lipase B by circular permutation
    • Qian, Z. and Lutz, S. (2005) Improving the catalytic activity of Candida antarctica lipase B by circular permutation J. Am. Chem. Soc. 127, 13466-13467 10.1021/ja053932h
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13466-13467
    • Qian, Z.1    Lutz, S.2
  • 24
    • 37549058473 scopus 로고    scopus 로고
    • Investigating the Structural and Functional Consequences of Circular Permutation on Lipase B from Candida antarctica
    • Qian, Z., Fields, C. J., and Lutz, S. (2007) Investigating the Structural and Functional Consequences of Circular Permutation on Lipase B from Candida antarctica ChemBioChem 8, 1989-1996 10.1002/cbic.200700373
    • (2007) ChemBioChem , vol.8 , pp. 1989-1996
    • Qian, Z.1    Fields, C.J.2    Lutz, S.3
  • 26
    • 81255186021 scopus 로고    scopus 로고
    • In silico approaches towards understanding CALB using molecular dynamics simulation and docking
    • Kumaresan, J., Kothai, T., and Lakshmi, B. S. (2011) In silico approaches towards understanding CALB using molecular dynamics simulation and docking Mol. Simul. 37, 1053-1061 10.1080/08927022.2011.589050
    • (2011) Mol. Simul. , vol.37 , pp. 1053-1061
    • Kumaresan, J.1    Kothai, T.2    Lakshmi, B.S.3
  • 27
    • 84866423968 scopus 로고    scopus 로고
    • Lipase B from Candida antarctica binds to hydrophobic substrate-water interfaces via hydrophobic anchors surrounding the active site entrance
    • Gruber, C. C. and Pleiss, J. (2012) Lipase B from Candida antarctica binds to hydrophobic substrate-water interfaces via hydrophobic anchors surrounding the active site entrance J. Mol. Catal. B: Enzym. 84, 48-54 10.1016/j.molcatb.2012.05.012
    • (2012) J. Mol. Catal. B: Enzym. , vol.84 , pp. 48-54
    • Gruber, C.C.1    Pleiss, J.2
  • 28
    • 84874104322 scopus 로고    scopus 로고
    • Amino acid oxidation of Candida antarctica lipase B studied by molecular dynamics simulations and site-directed mutagenesis
    • Irani, M., Törnvall, U., Genheden, S., Larsen, M. W., Hatti-Kaul, R., and Ryde, U. (2013) Amino acid oxidation of Candida antarctica lipase B studied by molecular dynamics simulations and site-directed mutagenesis Biochemistry 52, 1280-1289 10.1021/bi301298m
    • (2013) Biochemistry , vol.52 , pp. 1280-1289
    • Irani, M.1    Törnvall, U.2    Genheden, S.3    Larsen, M.W.4    Hatti-Kaul, R.5    Ryde, U.6
  • 29
    • 0029148636 scopus 로고
    • On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase
    • Martinelle, M., Holmquist, M., and Hult, K. (1995) On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase Biochim. Biophys. Acta, Lipids Lipid Metab. 1258, 272-276 10.1016/0005-2760(95)00131-U
    • (1995) Biochim. Biophys. Acta, Lipids Lipid Metab. , vol.1258 , pp. 272-276
    • Martinelle, M.1    Holmquist, M.2    Hult, K.3
  • 31
    • 34547804902 scopus 로고    scopus 로고
    • Influence of self-assembled monolayer surface chemistry on Candida antarctica lipase B adsorption and specific activity
    • Laszlo, J. A. and Evans, K. O. (2007) Influence of self-assembled monolayer surface chemistry on Candida antarctica lipase B adsorption and specific activity J. Mol. Catal. B: Enzym. 48, 84-89 10.1016/j.molcatb.2007.06.010
    • (2007) J. Mol. Catal. B: Enzym. , vol.48 , pp. 84-89
    • Laszlo, J.A.1    Evans, K.O.2
  • 34
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell, A. D., Feig, M., and Brooks, C. L. (2004) Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations J. Comput. Chem. 25, 1400-1415 10.1002/jcc.20065
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • MacKerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 36
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual Molecular Dynamics
    • Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD: Visual Molecular Dynamics J. Mol. Graphics 14, 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 37
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Sugita, Y. and Okamoto, Y. (1999) Replica-exchange molecular dynamics method for protein folding Chem. Phys. Lett. 314, 141-151 10.1016/S0009-2614(99)01123-9
    • (1999) Chem. Phys. Lett. , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 42
    • 52949088587 scopus 로고    scopus 로고
    • Statistically optimal analysis of samples from multiple equilibrium states
    • Shirts, M. R. and Chodera, J. D. (2008) Statistically optimal analysis of samples from multiple equilibrium states J. Chem. Phys. 129, 124105 10.1063/1.2978177
    • (2008) J. Chem. Phys. , vol.129 , pp. 124105
    • Shirts, M.R.1    Chodera, J.D.2
  • 43
    • 33845280446 scopus 로고
    • Comparing the Polarities of the Amino Acids: Side Chain Distribution Coefficients between the Vapor Phase, Cyclohexane, 1-Octanol, and Neutral Aqueous Solution
    • Radzicka, A. and Wolfenden, R. (1988) Comparing the Polarities of the Amino Acids: Side Chain Distribution Coefficients between the Vapor Phase, Cyclohexane, 1-Octanol, and Neutral Aqueous Solution Biochemistry 27, 1664-1670 10.1021/bi00405a042
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 44
    • 33748578351 scopus 로고    scopus 로고
    • Site-specific immobilization of genetically engineered variants of Candida antarctica lipase B
    • Blank, K., Morfill, J., and Gaub, H. E. (2006) Site-specific immobilization of genetically engineered variants of Candida antarctica lipase B ChemBioChem 7, 1349-1351 10.1002/cbic.200600198
    • (2006) ChemBioChem , vol.7 , pp. 1349-1351
    • Blank, K.1    Morfill, J.2    Gaub, H.E.3
  • 45
    • 33748296438 scopus 로고    scopus 로고
    • Functional expression of Candida antarctica lipase B in Eschericha coli
    • Blank, K., Morfill, J., Gumpp, H., and Gaub, H. E. (2006) Functional expression of Candida antarctica lipase B in Eschericha coli J. Biotechnol. 125, 474-483 10.1016/j.jbiotec.2006.04.004
    • (2006) J. Biotechnol. , vol.125 , pp. 474-483
    • Blank, K.1    Morfill, J.2    Gumpp, H.3    Gaub, H.E.4
  • 47
    • 0037450983 scopus 로고    scopus 로고
    • Highly sensitive active-site titration of lipase in microscale culture media using fluorescent organophosphorus ester
    • Fujii, R., Utsunomiya, Y., Hiratake, J., Sogabe, A., and Sakata, K. (2003) Highly sensitive active-site titration of lipase in microscale culture media using fluorescent organophosphorus ester Biochim. Biophys. Acta, Mol. Cell Biol. Lipids 1631, 197-205 10.1016/S1388-1981(03)00006-4
    • (2003) Biochim. Biophys. Acta, Mol. Cell Biol. Lipids , vol.1631 , pp. 197-205
    • Fujii, R.1    Utsunomiya, Y.2    Hiratake, J.3    Sogabe, A.4    Sakata, K.5
  • 48
    • 0020564420 scopus 로고
    • A kinetic study on the enzymatic hydrolysis of fluorescein diacetate and fluorescein-di-beta-D-galactopyranoside
    • Hofmann, J. and Sernetz, M. (1983) A kinetic study on the enzymatic hydrolysis of fluorescein diacetate and fluorescein-di-beta-D-galactopyranoside Anal. Biochem. 131, 180-186 10.1016/0003-2697(83)90151-3
    • (1983) Anal. Biochem. , vol.131 , pp. 180-186
    • Hofmann, J.1    Sernetz, M.2
  • 49
    • 0026044752 scopus 로고
    • Kinetic fluorescence measurement of fluorescein di-beta-D-galactoside hydrolysis by beta-galactosidase: Intermediate channeling in stepwise catalysis by a free single enzyme
    • Huang, Z. J. (1991) Kinetic fluorescence measurement of fluorescein di-beta-D-galactoside hydrolysis by beta-galactosidase: intermediate channeling in stepwise catalysis by a free single enzyme Biochemistry 30, 8535-8540 10.1021/bi00099a006
    • (1991) Biochemistry , vol.30 , pp. 8535-8540
    • Huang, Z.J.1
  • 50
    • 0028285357 scopus 로고
    • No intermediate channelling in stepwise hydrolysis of fluorescein di-β-D-galactoside by β-galactosidase
    • Fiedler, F. and Hinz, H. (1994) No intermediate channelling in stepwise hydrolysis of fluorescein di-β-D-galactoside by β-galactosidase Eur. J. Biochem. 222, 75-81 10.1111/j.1432-1033.1994.tb18843.x
    • (1994) Eur. J. Biochem. , vol.222 , pp. 75-81
    • Fiedler, F.1    Hinz, H.2
  • 51
    • 80054794059 scopus 로고    scopus 로고
    • Morpholinecarbonyl-Rhodamine 110 based substrates for the determination of protease activity with accurate kinetic parameters
    • Terentyeva, T. G., Van Rossom, W., Van der Auweraer, M., Blank, K., and Hofkens, J. (2011) Morpholinecarbonyl-Rhodamine 110 based substrates for the determination of protease activity with accurate kinetic parameters Bioconjugate Chem. 22, 1932-1938 10.1021/bc2001038
    • (2011) Bioconjugate Chem. , vol.22 , pp. 1932-1938
    • Terentyeva, T.G.1    Van Rossom, W.2    Van Der Auweraer, M.3    Blank, K.4    Hofkens, J.5
  • 53
    • 0034682172 scopus 로고    scopus 로고
    • Mass Transport Limitations Reduce the Effective Stereospecificity in Enzyme-Catalyzed Kinetic Resolution
    • Rotticci, D., Norin, T., and Hult, K. (2000) Mass Transport Limitations Reduce the Effective Stereospecificity in Enzyme-Catalyzed Kinetic Resolution Org. Lett. 2, 1373-1376 10.1021/ol005639m
    • (2000) Org. Lett. , vol.2 , pp. 1373-1376
    • Rotticci, D.1    Norin, T.2    Hult, K.3
  • 54
    • 34547537549 scopus 로고    scopus 로고
    • Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports
    • Fernández-Lorente, G., Palomo, J. M., Cabrera, Z., Guisán, J. M., and Fernández-Lafuente, R. (2007) Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports Enzyme Microb. Technol. 41, 565-569 10.1016/j.enzmictec.2007.05.004
    • (2007) Enzyme Microb. Technol. , vol.41 , pp. 565-569
    • Fernández-Lorente, G.1    Palomo, J.M.2    Cabrera, Z.3    Guisán, J.M.4    Fernández-Lafuente, R.5
  • 55
    • 0037010728 scopus 로고    scopus 로고
    • Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
    • Palomo, J. M., Muñoz, G., Fernández-Lorente, G., Mateo, C., Fernández-Lafuente, R., and Guisán, J. M. (2002) Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases J. Mol. Catal. B: Enzym. 19-20, 279-286 10.1016/S1381-1177(02)00178-9
    • (2002) J. Mol. Catal. B: Enzym. , vol.19-20 , pp. 279-286
    • Palomo, J.M.1    Muñoz, G.2    Fernández-Lorente, G.3    Mateo, C.4    Fernández-Lafuente, R.5    Guisán, J.M.6


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