메뉴 건너뛰기




Volumn 54, Issue 33, 2015, Pages 8072-8079

Improving catalytic performance of Candida rugosa lipase by chemical modification with polyethylene glycol functional ionic liquids

Author keywords

[No Author keywords available]

Indexed keywords

CANDIDA; CATALYST ACTIVITY; CHEMICAL MODIFICATION; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; DIMETHYL SULFOXIDE; IONIC CONDUCTION; LIPASES; LIQUIDS; OLIVE OIL; ORGANIC SOLVENTS; POLYETHYLENE GLYCOLS; POLYETHYLENES; STABILITY; YEAST;

EID: 84940564493     PISSN: 08885885     EISSN: 15205045     Source Type: Journal    
DOI: 10.1021/acs.iecr.5b01881     Document Type: Article
Times cited : (51)

References (52)
  • 1
    • 84883272014 scopus 로고    scopus 로고
    • Biocatalysis in organic chemistry and biotechnology: Past, present, and future
    • Reetz, M. T. Biocatalysis in organic chemistry and biotechnology: past, present, and future. J. Am. Chem. Soc. 2013, 135, 12480.
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 12480
    • Reetz, M.T.1
  • 2
    • 77958046500 scopus 로고    scopus 로고
    • Hydrolases: Catalytically promiscuous enzymes for non-conventional reactions in organic synthesis
    • Busto, E.; Gotor-Fernandez, V.; Gotor, V. Hydrolases: catalytically promiscuous enzymes for non-conventional reactions in organic synthesis. Chem. Soc. Rev. 2010, 39, 4504.
    • (2010) Chem. Soc. Rev , vol.39 , pp. 4504
    • Busto, E.1    Gotor-Fernandez, V.2    Gotor, V.3
  • 4
    • 79953318981 scopus 로고    scopus 로고
    • Chemical modification in the creation of novel biocatalysts
    • Diaz-Rodriguez, A.; Davis, B. G. Chemical modification in the creation of novel biocatalysts. Curr. Opin. Chem. Biol. 2011, 15, 211.
    • (2011) Curr. Opin. Chem. Biol , vol.15 , pp. 211
    • Diaz-Rodriguez, A.1    Davis, B.G.2
  • 5
    • 84859424745 scopus 로고    scopus 로고
    • Modulation of the properties of immobilized CALB by chemical modification with 2, 3,4-trinitrobenzenesulfonate or ethylendiamine. Advantages of using adsorbed lipases on hydrophobic supports
    • Barbosa, O.; Ruiz, M.; Ortiz, C.; Fernandez, M. Modulation of the properties of immobilized CALB by chemical modification with 2,3,4-trinitrobenzenesulfonate or ethylendiamine. Advantages of using adsorbed lipases on hydrophobic supports. Process Biochem. 2012, 47, 867.
    • (2012) Process Biochem , vol.47 , pp. 867
    • Barbosa, O.1    Ruiz, M.2    Ortiz, C.3    Fernandez, M.4
  • 6
    • 77957825071 scopus 로고    scopus 로고
    • Chemical modification and immobilisation of lipase B from Candida antarctica onto mesoporous silicates
    • Forde, J.; Vakurov, A.; Gibson, T. D.; Millner, P. Chemical modification and immobilisation of lipase B from Candida antarctica onto mesoporous silicates. J. Mol. Catal. B: Enzym. 2010, 66, 203.
    • (2010) J. Mol. Catal. B: Enzym , vol.66 , pp. 203
    • Forde, J.1    Vakurov, A.2    Gibson, T.D.3    Millner, P.4
  • 7
    • 34447136294 scopus 로고    scopus 로고
    • Biocatalysis in ionic liquids
    • Van Rantwijk, F.; Sheldon, R. A. Biocatalysis in ionic liquids. Chem. Rev. 2007, 107, 2757.
    • (2007) Chem. Rev , vol.107 , pp. 2757
    • Van Rantwijk, F.1    Sheldon, R.A.2
  • 8
    • 84894488335 scopus 로고    scopus 로고
    • Modulating enzyme activity using ionic liquids or surfactants
    • Goldfeder, M.; Fishman, A. Modulating enzyme activity using ionic liquids or surfactants. Appl. Microbiol. Biotechnol. 2014, 98, 545.
    • (2014) Appl. Microbiol. Biotechnol , vol.98 , pp. 545
    • Goldfeder, M.1    Fishman, A.2
  • 9
    • 80051823718 scopus 로고    scopus 로고
    • Ionic liquid-inspired cations covalently bound to formate dehydrogenase improve its stability and activity in ionic liquids
    • Bekhouche, M.; Blum, L. J.; Doumeche, B. Ionic liquid-inspired cations covalently bound to formate dehydrogenase improve its stability and activity in ionic liquids. ChemCatChem 2011, 3, 875.
    • (2011) ChemCatChem , vol.3 , pp. 875
    • Bekhouche, M.1    Blum, L.J.2    Doumeche, B.3
  • 10
    • 84883884666 scopus 로고    scopus 로고
    • Enhancing catalytic performance of porcine pancreatic lipase by covalent modification using functional ionic liquids
    • Jia, R.; Hu, Y.; Liu, L.; Jiang, L.; Zou, B.; Huang, H. Enhancing catalytic performance of porcine pancreatic lipase by covalent modification using functional ionic liquids. ACS Catal. 2013, 3, 1976.
    • (2013) ACS Catal , vol.3 , pp. 1976
    • Jia, R.1    Hu, Y.2    Liu, L.3    Jiang, L.4    Zou, B.5    Huang, H.6
  • 11
    • 84925884138 scopus 로고    scopus 로고
    • Chemical modification with functionalized ionic liquids: A novel method to improve the enzymatic properties of Candida rugosa lipase
    • Hu, Y.; Yang, J.; Jia, R.; Ding, Y.; Li, S.; Huang, H. Chemical modification with functionalized ionic liquids: a novel method to improve the enzymatic properties of Candida rugosa lipase. Bioprocess Biosyst. Eng. 2014, 37, 1617.
    • (2014) Bioprocess Biosyst. Eng , vol.37 , pp. 1617
    • Hu, Y.1    Yang, J.2    Jia, R.3    Ding, Y.4    Li, S.5    Huang, H.6
  • 12
    • 84884174601 scopus 로고    scopus 로고
    • N-terminal PEGylated cellulase: A high stability enzyme in 1-butyl-3-methylimidazolium chloride
    • Li, L.; Xie, J.; Yu, S. T.; Su, Z. L. N-terminal PEGylated cellulase: a high stability enzyme in 1-butyl-3-methylimidazolium chloride. Green Chem. 2013, 15, 1624.
    • (2013) Green Chem , vol.15 , pp. 1624
    • Li, L.1    Xie, J.2    Yu, S.T.3    Su, Z.L.4
  • 13
    • 84884611957 scopus 로고    scopus 로고
    • Enhanced catalytic activity in organic solvents using molecularly dispersed haemoglobin-polymer surfactant constructs
    • Zhang, Y. X.; Patil, A. J.; Perriman, A. W.; Mann, S. Enhanced catalytic activity in organic solvents using molecularly dispersed haemoglobin-polymer surfactant constructs. Chem. Commun. 2013, 49, 9561.
    • (2013) Chem. Commun , vol.49 , pp. 9561
    • Zhang, Y.X.1    Patil, A.J.2    Perriman, A.W.3    Mann, S.4
  • 14
    • 10744228704 scopus 로고    scopus 로고
    • Stability of PEGylated salmon calcitonin in nasal mucosa
    • Na, D. H.; Youn, Y. S.; Park, E. J.; Lee, J. M. Stability of PEGylated salmon calcitonin in nasal mucosa. J. Pharm. Sci. 2004, 93, 256.
    • (2004) J. Pharm. Sci , vol.93 , pp. 256
    • Na, D.H.1    Youn, Y.S.2    Park, E.J.3    Lee, J.M.4
  • 15
    • 0036171890 scopus 로고    scopus 로고
    • Bioactivities of ricin retained and its immunoreactivity to anti-ricin polyclonal antibodies alleviated through pegylation
    • Hu, R. G.; Zhai, Q. W.; He, W.; Mei, L. Bioactivities of ricin retained and its immunoreactivity to anti-ricin polyclonal antibodies alleviated through pegylation. Int. J. Biochem. Cell Biol. 2002, 34, 396.
    • (2002) Int. J. Biochem. Cell Biol , vol.34 , pp. 396
    • Hu, R.G.1    Zhai, Q.W.2    He, W.3    Mei, L.4
  • 17
    • 77949496550 scopus 로고    scopus 로고
    • Chemical modification of stem bromelain with anhydride groups to enhance its stability and catalytic activity
    • Xue, Y.; Wu, C. Y.; Branford-White, C. J.; Ning, X. Chemical modification of stem bromelain with anhydride groups to enhance its stability and catalytic activity. J. Mol. Catal. B: Enzym. 2010, 63, 188.
    • (2010) J. Mol. Catal. B: Enzym , vol.63 , pp. 188
    • Xue, Y.1    Wu, C.Y.2    Branford-White, C.J.3    Ning, X.4
  • 18
    • 75149149796 scopus 로고    scopus 로고
    • Evaluation of the potential of polymeric carriers based on photo-crosslinkable chitosan in the formulation of lipase from Candida rugosa immobilization
    • Monier, M.; Wei, Y.; Sarhan, A. Evaluation of the potential of polymeric carriers based on photo-crosslinkable chitosan in the formulation of lipase from Candida rugosa immobilization. J. Mol. Catal. B: Enzym. 2010, 63, 93.
    • (2010) J. Mol. Catal. B: Enzym , vol.63 , pp. 93
    • Monier, M.1    Wei, Y.2    Sarhan, A.3
  • 19
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular-dichroism
    • Yang, J. T.; Wu, C. S. C.; Martinez, H. M. Calculation of protein conformation from circular-dichroism. Methods Enzymol. 1986, 130, 208.
    • (1986) Methods Enzymol , vol.130 , pp. 208
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3
  • 20
    • 33744799997 scopus 로고    scopus 로고
    • Are ionic liquids kosmotropic or chaotropic? An evaluation of available thermodynamic parameters for quantifying the ion kosmotropicity of ionic liquids
    • Zhao, H. Are ionic liquids kosmotropic or chaotropic? An evaluation of available thermodynamic parameters for quantifying the ion kosmotropicity of ionic liquids. J. Chem. Technol. Biotechnol. 2006, 81, 877.
    • (2006) J. Chem. Technol. Biotechnol , vol.81 , pp. 877
    • Zhao, H.1
  • 21
    • 31744432116 scopus 로고    scopus 로고
    • Effect of kosmotropicity of ionic liquids on the enzyme stability in aqueous solutions
    • Zhao, H.; Olubajo, O.; Song, Z.; Sims, A. L.; Person, T. E.; Lawal, R. A.; Holley, L. A. Effect of kosmotropicity of ionic liquids on the enzyme stability in aqueous solutions. Bioorg. Chem. 2006, 34, 15.
    • (2006) Bioorg. Chem , vol.34 , pp. 15
    • Zhao, H.1    Olubajo, O.2    Song, Z.3    Sims, A.L.4    Person, T.E.5    Lawal, R.A.6    Holley, L.A.7
  • 22
    • 70350225355 scopus 로고    scopus 로고
    • Hofmeister effects: An explanation for the impact of ionic liquids on biocatalysis
    • Yang, Z. Hofmeister effects: an explanation for the impact of ionic liquids on biocatalysis. J. Biotechnol. 2009, 144, 12.
    • (2009) J. Biotechnol , vol.144 , pp. 12
    • Yang, Z.1
  • 23
    • 77953522374 scopus 로고    scopus 로고
    • Methods for stabilizing and activating enzymes in ionic liquids - A review
    • Zhao, H. Methods for stabilizing and activating enzymes in ionic liquids-a review. J. Chem. Technol. Biotechnol. 2010, 85, 891.
    • (2010) J. Chem. Technol. Biotechnol , vol.85 , pp. 891
    • Zhao, H.1
  • 24
    • 77952584011 scopus 로고    scopus 로고
    • Chemical modifications by ionic liquid-inspired cations improve the activity and the stability of formate dehydrogenase in [MMIm][Me2PO4]
    • Bekhouche, M.; Doumeche, B.; Blum, L. J. Chemical modifications by ionic liquid-inspired cations improve the activity and the stability of formate dehydrogenase in [MMIm][Me2PO4]. J. Mol. Catal. B: Enzym. 2010, 65, 73.
    • (2010) J. Mol. Catal. B: Enzym , vol.65 , pp. 73
    • Bekhouche, M.1    Doumeche, B.2    Blum, L.J.3
  • 25
    • 0037452405 scopus 로고    scopus 로고
    • Stabilization of recombinant interferon-αby pegylation for encapsulation in PLGA microspheres
    • Diwan, M.; Park, T. G. Stabilization of recombinant interferon-αby pegylation for encapsulation in PLGA microspheres. Int. J. Pharm. 2003, 252, 111.
    • (2003) Int. J. Pharm , vol.252 , pp. 111
    • Diwan, M.1    Park, T.G.2
  • 26
    • 0344492722 scopus 로고    scopus 로고
    • Modification of purified lipases from Candida rugosa with polyethylene glycol: A systematic study
    • Hernaiz, M. J.; Sanchez-Montero, J. M.; Sinisterra, J. V. Modification of purified lipases from Candida rugosa with polyethylene glycol: a systematic study. Enzyme. Enzyme Microb. Technol. 1999, 24, 181.
    • (1999) Enzyme. Enzyme Microb. Technol , vol.24 , pp. 181
    • Hernaiz, M.J.1    Sanchez-Montero, J.M.2    Sinisterra, J.V.3
  • 27
    • 23844484942 scopus 로고    scopus 로고
    • Characteristics of the lipase from Candida rugosa modified with copolymers of polyoxyethylene derivative and maleic acid anhydride
    • Park, K.; Kim, H.; Maken, S.; Kim, Y.; Min, B.; Park, J. Characteristics of the lipase from Candida rugosa modified with copolymers of polyoxyethylene derivative and maleic acid anhydride. Korean J. Chem. Eng. 2005, 22, 412.
    • (2005) Korean J. Chem. Eng , vol.22 , pp. 412
    • Park, K.1    Kim, H.2    Maken, S.3    Kim, Y.4    Min, B.5    Park, J.6
  • 28
    • 79960272716 scopus 로고    scopus 로고
    • Specific ion effects of ionic liquids on enzyme activity and stability
    • Lai, J. Q.; Li, Z.; Lu, Y. H.; Yang, Z. Specific ion effects of ionic liquids on enzyme activity and stability. Green Chem. 2011, 13, 1860.
    • (2011) Green Chem , vol.13 , pp. 1860
    • Lai, J.Q.1    Li, Z.2    Lu, Y.H.3    Yang, Z.4
  • 29
    • 37849188833 scopus 로고    scopus 로고
    • Activation of lipase in ionic liquids by modification with comb-shaped poly(ethylene glycol)
    • Nakashima, K.; Okada, J.; Maruyama, T.; Kamiya, N.; Goto, M. Activation of lipase in ionic liquids by modification with comb-shaped poly(ethylene glycol). Sci. Technol. Adv. Mater. 2006, 7, 692.
    • (2006) Sci. Technol. Adv. Mater , vol.7 , pp. 692
    • Nakashima, K.1    Okada, J.2    Maruyama, T.3    Kamiya, N.4    Goto, M.5
  • 30
  • 31
    • 79957956788 scopus 로고    scopus 로고
    • Immobilization of papain by carboxyl-modified SBA-15: Rechecking the carboxyl after excluding the contribution of H2SO4 treatment
    • Bian, W.; Lou, L. L.; Yan, B.; Zhang, C.; Wu, S.; Liu, S. Immobilization of papain by carboxyl-modified SBA-15: rechecking the carboxyl after excluding the contribution of H2SO4 treatment. Microporous Mesoporous Mater. 2011, 143, 341.
    • (2011) Microporous Mesoporous Mater , vol.143 , pp. 341
    • Bian, W.1    Lou, L.L.2    Yan, B.3    Zhang, C.4    Wu, S.5    Liu, S.6
  • 32
    • 0343471966 scopus 로고    scopus 로고
    • Influence of the nature of modifier in the enzymatic activity of chemical modified semipurified lipase from Candida rugosa
    • Hernaiz, M. J.; Sanchez-Montero, J. M.; Sinisterra, J. V. Influence of the nature of modifier in the enzymatic activity of chemical modified semipurified lipase from Candida rugosa. Biotechnol. Bioeng. 1997, 55, 252.
    • (1997) Biotechnol. Bioeng , vol.55 , pp. 252
    • Hernaiz, M.J.1    Sanchez-Montero, J.M.2    Sinisterra, J.V.3
  • 33
    • 14344255109 scopus 로고    scopus 로고
    • Effect of the covalent modification with poly (ethylene glycol) on alphachymotrypsin stability upon encapsulation in poly (lactic-co-glycolic) microspheres
    • Castellanos, I. J.; Al-Azzam, W.; Griebenow, K. Effect of the covalent modification with poly (ethylene glycol) on alphachymotrypsin stability upon encapsulation in poly (lactic-co-glycolic) microspheres. J. Pharm. Sci. 2005, 94, 327.
    • (2005) J. Pharm. Sci , vol.94 , pp. 327
    • Castellanos, I.J.1    Al-Azzam, W.2    Griebenow, K.3
  • 34
    • 0033911947 scopus 로고    scopus 로고
    • Kinetic study of thermal inactivation for native and methoxypolyethylene glycol modified trypsin
    • He, Z. M.; Zhang, Z. D.; He, M. X. Kinetic study of thermal inactivation for native and methoxypolyethylene glycol modified trypsin. Process Biochem. 2000, 35, 1235.
    • (2000) Process Biochem , vol.35 , pp. 1235
    • He, Z.M.1    Zhang, Z.D.2    He, M.X.3
  • 35
    • 0031984007 scopus 로고    scopus 로고
    • Kinetics of thermal inactivation of horseradish peroxidase: Stabilizing effect of methoxypoly (ethylene glycol)
    • Garcia, D.; Ortega, F.; Marty, J. L. Kinetics of thermal inactivation of horseradish peroxidase: stabilizing effect of methoxypoly (ethylene glycol). Appl. Biochem. Biotechnol. 1998, 27, 49.
    • (1998) Appl. Biochem. Biotechnol , vol.27 , pp. 49
    • Garcia, D.1    Ortega, F.2    Marty, J.L.3
  • 36
    • 84880829379 scopus 로고    scopus 로고
    • Stabilization of enzymes in ionic liquids via modification of enzyme charge
    • Nordwald, E. M.; Kaar, J. L. Stabilization of enzymes in ionic liquids via modification of enzyme charge. Biotechnol. Bioeng. 2013, 110, 2352.
    • (2013) Biotechnol. Bioeng , vol.110 , pp. 2352
    • Nordwald, E.M.1    Kaar, J.L.2
  • 37
    • 0037375191 scopus 로고    scopus 로고
    • Increased stability of an esterase from Bacillus stearothermophilus in ionic liquids as compared to organic solvents
    • Persson, M.; Bornscheuer, U. T. Increased stability of an esterase from Bacillus stearothermophilus in ionic liquids as compared to organic solvents. J. Mol. Catal. B: Enzym. 2003, 22, 21.
    • (2003) J. Mol. Catal. B: Enzym , vol.22 , pp. 21
    • Persson, M.1    Bornscheuer, U.T.2
  • 38
    • 0036276725 scopus 로고    scopus 로고
    • A caveat for the use of log P values for the assessment of the biocompatibility of organic solvents
    • Pogorevc, M.; Stecher, H.; Faber, K. A caveat for the use of log P values for the assessment of the biocompatibility of organic solvents. Biotechnol. Lett. 2002, 24, 857.
    • (2002) Biotechnol. Lett , vol.24 , pp. 857
    • Pogorevc, M.1    Stecher, H.2    Faber, K.3
  • 39
    • 0035138047 scopus 로고    scopus 로고
    • Enhanced activity of Candida rugosa lipase modified by polyethylene glycol derivatives
    • Wu, J. C.; Zhang, G. F.; He, Z. M. Enhanced activity of Candida rugosa lipase modified by polyethylene glycol derivatives. Biotechnol. Lett. 2001, 23, 211.
    • (2001) Biotechnol. Lett , vol.23 , pp. 211
    • Wu, J.C.1    Zhang, G.F.2    He, Z.M.3
  • 40
    • 79957844706 scopus 로고    scopus 로고
    • Preparation and characterization of PEGyated Concanavalin A for affinity chromatography with improved stability
    • Wen, Z. Z.; Niemeyer, B. Preparation and characterization of PEGyated Concanavalin A for affinity chromatography with improved stability. J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 2011, 879, 1732.
    • (2011) J. Chromatogr. B: Anal. Technol. Biomed. Life Sci , vol.879 , pp. 1732
    • Wen, Z.Z.1    Niemeyer, B.2
  • 41
    • 80055006984 scopus 로고    scopus 로고
    • Effects of succinic anhydride modification on laccase stability and phenolics removal efficiency
    • Xiong, Y.; Gao, J.; Zheng, J.; Deng, N. Effects of succinic anhydride modification on laccase stability and phenolics removal efficiency. Chin. J. Catal. 2011, 32, 1584.
    • (2011) Chin. J. Catal , vol.32 , pp. 1584
    • Xiong, Y.1    Gao, J.2    Zheng, J.3    Deng, N.4
  • 42
    • 76349097336 scopus 로고    scopus 로고
    • Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods
    • Wang, Y. Q.; Chen, T. T.; Zhang, H. M. Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods. Spectrochim. Acta, Part A 2010, 75, 1130.
    • (2010) Spectrochim. Acta, Part A , vol.75 , pp. 1130
    • Wang, Y.Q.1    Chen, T.T.2    Zhang, H.M.3
  • 43
    • 79958834758 scopus 로고    scopus 로고
    • Imidazolium chloridebased ionic liquid-assisted improvement of lipase activity in organic solvents
    • Daneshjoo, S.; Akbari, N.; Sepahi, A. A. Imidazolium chloridebased ionic liquid-assisted improvement of lipase activity in organic solvents. Eng. Life. Sci. 2011, 11, 259.
    • (2011) Eng. Life. Sci , vol.11 , pp. 259
    • Daneshjoo, S.1    Akbari, N.2    Sepahi, A.A.3
  • 44
    • 34250343031 scopus 로고    scopus 로고
    • Improvement of activity and stability of chloroperoxidase by chemical modification
    • Liu, J. Z.; Wang, M. Improvement of activity and stability of chloroperoxidase by chemical modification. BMC Biotechnol. 2007, 7, 23.
    • (2007) BMC Biotechnol , vol.7 , pp. 23
    • Liu, J.Z.1    Wang, M.2
  • 45
    • 0037687640 scopus 로고    scopus 로고
    • Imaging the distribution and secondary structure of immobilized enzymes using infrared microspectroscopy
    • Mei, Y.; Miller, L.; Gao, W.; Gross, R. A. Imaging the distribution and secondary structure of immobilized enzymes using infrared microspectroscopy. Biomacromolecules 2003, 4, 70.
    • (2003) Biomacromolecules , vol.4 , pp. 70
    • Mei, Y.1    Miller, L.2    Gao, W.3    Gross, R.A.4
  • 46
    • 77952745485 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of lysozyme modified by PEGylation
    • Freitas, D. D.; Abrahao-Neto, J. Biochemical and biophysical characterization of lysozyme modified by PEGylation. Int. J. Pharm. 2010, 392, 111.
    • (2010) Int. J. Pharm , vol.392 , pp. 111
    • Freitas, D.D.1    Abrahao-Neto, J.2
  • 47
    • 4344684591 scopus 로고    scopus 로고
    • Reductive alkylation of lipase-experimental and molecular modeling approaches
    • Rahman, R. N. Z. A.; Tejo, B. A.; Basri, M. Reductive alkylation of lipase-experimental and molecular modeling approaches. Appl. Biochem. Biotechnol. 2004, 118, 11.
    • (2004) Appl. Biochem. Biotechnol , vol.118 , pp. 11
    • Rahman, R.N.Z.A.1    Tejo, B.A.2    Basri, M.3
  • 48
    • 67349101642 scopus 로고    scopus 로고
    • Lipases in water-in-ionic liquid microemulsions: Structural and activity studies
    • Pavlidis, I. V.; Gournis, D.; Papadopoulos, G. K. Lipases in water-in-ionic liquid microemulsions: Structural and activity studies. J. Mol. Catal. B: Enzym. 2009, 60, 50.
    • (2009) J. Mol. Catal. B: Enzym , vol.60 , pp. 50
    • Pavlidis, I.V.1    Gournis, D.2    Papadopoulos, G.K.3
  • 49
    • 80054840235 scopus 로고    scopus 로고
    • Biodiesel synthesis and conformation of lipase from Burkholderia cepacia in room temperature ionic liquids and organic solvents
    • Liu, Y.; Chen, D. W.; Yan, Y. J. Biodiesel synthesis and conformation of lipase from Burkholderia cepacia in room temperature ionic liquids and organic solvents. Bioresour. Technol. 2011, 102, 10414.
    • (2011) Bioresour. Technol , vol.102 , pp. 10414
    • Liu, Y.1    Chen, D.W.2    Yan, Y.J.3
  • 50
    • 84923248036 scopus 로고    scopus 로고
    • Comparison of three ionic liquid-tolerant cellulases by molecular dynamics
    • Jaeger, V.; Burney, P.; Pfaendtner, J. Comparison of three ionic liquid-tolerant cellulases by molecular dynamics. Biophys. J. 2015, 108, 880.
    • (2015) Biophys. J , vol.108 , pp. 880
    • Jaeger, V.1    Burney, P.2    Pfaendtner, J.3
  • 51
    • 77956171987 scopus 로고    scopus 로고
    • Esterification activity and conformation studies of Burkholderia cepacia lipase in conventional organic solvents, ionic liquids and their co-solvent mixture media
    • Pan, S. T.; Liu, X.; Xie, Y. D.; Yi, Y. Y. Esterification activity and conformation studies of Burkholderia cepacia lipase in conventional organic solvents, ionic liquids and their co-solvent mixture media. Bioresour. Technol. 2010, 101, 9822.
    • (2010) Bioresour. Technol , vol.101 , pp. 9822
    • Pan, S.T.1    Liu, X.2    Xie, Y.D.3    Yi, Y.Y.4
  • 52
    • 20144366621 scopus 로고    scopus 로고
    • Understanding structure-Stability relationships of Candida Antartica lipase B in ionic liquids
    • De Diego, T.; Lozano, P.; Gmouh, S.; Vaultier, M.; Iborra, J. L. Understanding structure-Stability relationships of Candida antartica lipase B in ionic liquids. Biomacromolecules 2005, 6, 1457.
    • (2005) Biomacromolecules , vol.6 , pp. 1457
    • De Diego, T.1    Lozano, P.2    Gmouh, S.3    Vaultier, M.4    Iborra, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.