메뉴 건너뛰기




Volumn 251, Issue , 2014, Pages 392-403

Immobilization of Thermomyces lanuginosus lipase on mesoporous poly-hydroxybutyrate particles and application in alkyl esters synthesis: Isotherm, thermodynamic and mass transfer studies

Author keywords

Alkyl esters synthesis; Immobilization; Physical adsorption; Poly hydroxybutyrate particles; Thermomyces lanuginosus lipase

Indexed keywords

ADSORPTION; BIOCATALYSTS; EMULSIONS; ENZYMES; ESTERIFICATION; ISOTHERMS; MASS TRANSFER; OLEIC ACID; RADIOACTIVE WASTE VITRIFICATION; REACTION KINETICS; SYNTHESIS (CHEMICAL);

EID: 84900810403     PISSN: 13858947     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cej.2014.04.087     Document Type: Article
Times cited : (75)

References (58)
  • 1
    • 0001406913 scopus 로고
    • Action de la lipase pancreatique sur lês esteres en emulsion
    • Sarda L., Desnuelle P. Action de la lipase pancreatique sur lês esteres en emulsion. Biochim. Biophys. Acta 1958, 30:513-521.
    • (1958) Biochim. Biophys. Acta , vol.30 , pp. 513-521
    • Sarda, L.1    Desnuelle, P.2
  • 3
    • 0000321692 scopus 로고
    • Enzyme-catalyzed processes in organic solvents
    • Zaks A., Klibanov A.M. Enzyme-catalyzed processes in organic solvents. Proc. Natl. Acad. Sci. USA 1985, 82:3192-3196.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3192-3196
    • Zaks, A.1    Klibanov, A.M.2
  • 4
    • 84880105945 scopus 로고    scopus 로고
    • Immobilisation and application of lipases in organic media
    • Adlercreutz P. Immobilisation and application of lipases in organic media. Chem. Soc. Rev. 2013, 42:6406-6436.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 6406-6436
    • Adlercreutz, P.1
  • 5
    • 84858071530 scopus 로고    scopus 로고
    • Lipase promiscuity and its biochemical applications
    • Kapoor M., Gupta M.N. Lipase promiscuity and its biochemical applications. Process Biochem. 2012, 47:555-569.
    • (2012) Process Biochem. , vol.47 , pp. 555-569
    • Kapoor, M.1    Gupta, M.N.2
  • 6
    • 84860450495 scopus 로고    scopus 로고
    • Properties and biotechnological applications of porcine pancreatic lipase
    • Mendes A.A., Oliveira P.C., Castro H.F. Properties and biotechnological applications of porcine pancreatic lipase. J. Mol. Catal. B: Enzym. 2012, 78:119-134.
    • (2012) J. Mol. Catal. B: Enzym. , vol.78 , pp. 119-134
    • Mendes, A.A.1    Oliveira, P.C.2    Castro, H.F.3
  • 7
    • 77949541519 scopus 로고    scopus 로고
    • Lipase from Thermomyces lanuginosus: uses and prospects as an industrial biocatalyst
    • Fernandez-Lafuente R. Lipase from Thermomyces lanuginosus: uses and prospects as an industrial biocatalyst. J. Mol. Catal. B: Enzym. 2010, 62:197-212.
    • (2010) J. Mol. Catal. B: Enzym. , vol.62 , pp. 197-212
    • Fernandez-Lafuente, R.1
  • 8
    • 79952225241 scopus 로고    scopus 로고
    • Biotechnological approach of microbial lipase: a review
    • Sharma D., Sharma B., Shukla A.K. Biotechnological approach of microbial lipase: a review. Biotechnology 2011, 10:23-40.
    • (2011) Biotechnology , vol.10 , pp. 23-40
    • Sharma, D.1    Sharma, B.2    Shukla, A.K.3
  • 10
    • 84866850412 scopus 로고    scopus 로고
    • Production of biodiesel via ethanolysis of waste cooking oil using immobilised lipase
    • Chesterfield D.M., Rogers P.L., Al-Zaini E.O., Adesina A.A. Production of biodiesel via ethanolysis of waste cooking oil using immobilised lipase. Chem. Eng. J. 2012, 207-208:701-710.
    • (2012) Chem. Eng. J. , pp. 701-710
    • Chesterfield, D.M.1    Rogers, P.L.2    Al-Zaini, E.O.3    Adesina, A.A.4
  • 11
    • 84894283493 scopus 로고    scopus 로고
    • Estimation of critical properties of reaction mixtures obtained in different reaction conditions during the synthesis of biodiesel with supercritical methanol from soybean oil
    • Olivares-Carrillo P., Quesada-Medina J., de los Ríos A.P., Hernández-Fernández F.J. Estimation of critical properties of reaction mixtures obtained in different reaction conditions during the synthesis of biodiesel with supercritical methanol from soybean oil. Chem. Eng. J. 2014, 241:418-432.
    • (2014) Chem. Eng. J. , vol.241 , pp. 418-432
    • Olivares-Carrillo, P.1    Quesada-Medina, J.2    de los Ríos, A.P.3    Hernández-Fernández, F.J.4
  • 12
    • 47649126380 scopus 로고    scopus 로고
    • Synthesis, characterization and biodegradation studies of poly(ester urethane)s
    • Umare S.S., Chandure A.S. Synthesis, characterization and biodegradation studies of poly(ester urethane)s. Chem. Eng. J. 2008, 142:65-77.
    • (2008) Chem. Eng. J. , vol.142 , pp. 65-77
    • Umare, S.S.1    Chandure, A.S.2
  • 13
    • 64649087148 scopus 로고    scopus 로고
    • A simple procedure for the synthesis of potential 6-azauridine prodrugs by Thermomyces lanuginosus lipase
    • Wang Z.Y., Li N., Zong M.H. A simple procedure for the synthesis of potential 6-azauridine prodrugs by Thermomyces lanuginosus lipase. J. Mol. Catal. B: Enzym. 2009, 59:212-219.
    • (2009) J. Mol. Catal. B: Enzym. , vol.59 , pp. 212-219
    • Wang, Z.Y.1    Li, N.2    Zong, M.H.3
  • 14
    • 84874118049 scopus 로고    scopus 로고
    • Geranyl acetate synthesis catalyzed by Thermomyces lanuginosus lipase immobilized on electrospun polyacrylonitrile nanofiber membrane
    • Gupta A., Dhakate S.R., Pahwa M., Sinha S., Chand S., Mathur R.B. Geranyl acetate synthesis catalyzed by Thermomyces lanuginosus lipase immobilized on electrospun polyacrylonitrile nanofiber membrane. Process Biochem. 2013, 48:124-132.
    • (2013) Process Biochem. , vol.48 , pp. 124-132
    • Gupta, A.1    Dhakate, S.R.2    Pahwa, M.3    Sinha, S.4    Chand, S.5    Mathur, R.B.6
  • 15
    • 80051704822 scopus 로고    scopus 로고
    • Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts
    • Mendes A.A., Castro H.F., Rodrigues D.S., Adriano W.S., Tardioli P.W., Mammarella E.J., Giordano R.C., Giordano R.L.C. Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts. J. Ind. Microbiol. Biotechnol. 2011, 38:1055-1066.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 1055-1066
    • Mendes, A.A.1    Castro, H.F.2    Rodrigues, D.S.3    Adriano, W.S.4    Tardioli, P.W.5    Mammarella, E.J.6    Giordano, R.C.7    Giordano, R.L.C.8
  • 16
    • 78649321427 scopus 로고    scopus 로고
    • Immobilization and stabilization of microbial lipases by multipoint covalent attachment on aldehyde-resin affinity: application of the biocatalysts in biodiesel synthesis
    • Mendes A.A., Giordano R.C., Giordano R.L.C., Castro H.F. Immobilization and stabilization of microbial lipases by multipoint covalent attachment on aldehyde-resin affinity: application of the biocatalysts in biodiesel synthesis. J. Mol. Catal. B: Enzym. 2011, 68:109-115.
    • (2011) J. Mol. Catal. B: Enzym. , vol.68 , pp. 109-115
    • Mendes, A.A.1    Giordano, R.C.2    Giordano, R.L.C.3    Castro, H.F.4
  • 18
    • 80052961596 scopus 로고    scopus 로고
    • Biocatalytic esterification of palm oil fatty acids for biodiesel production using glycine-based cross-linked protein coated microcrystalline lipase
    • Raita M., Laothanachareon T., Champreda V., Laosiripojana N. Biocatalytic esterification of palm oil fatty acids for biodiesel production using glycine-based cross-linked protein coated microcrystalline lipase. J. Mol. Catal. B: Enzym. 2011, 73:74-79.
    • (2011) J. Mol. Catal. B: Enzym. , vol.73 , pp. 74-79
    • Raita, M.1    Laothanachareon, T.2    Champreda, V.3    Laosiripojana, N.4
  • 19
    • 77957856686 scopus 로고    scopus 로고
    • Pore size of macroporous polystyrene microspheres affects lipase immobilization
    • Li Y., Gao F., Wei W., Qu J.B., Ma G.H., Zhou W.Q. Pore size of macroporous polystyrene microspheres affects lipase immobilization. J. Mol. Catal. B: Enzym. 2010, 66:182-189.
    • (2010) J. Mol. Catal. B: Enzym. , vol.66 , pp. 182-189
    • Li, Y.1    Gao, F.2    Wei, W.3    Qu, J.B.4    Ma, G.H.5    Zhou, W.Q.6
  • 20
    • 84856327687 scopus 로고    scopus 로고
    • Improvement of catalytic activity and stability of lipase by immobilization on organobentonite
    • Dong H., Li J., Li Y., Hu L., Luo D. Improvement of catalytic activity and stability of lipase by immobilization on organobentonite. Chem. Eng. J. 2012, 181-182:590-596.
    • (2012) Chem. Eng. J. , pp. 590-596
    • Dong, H.1    Li, J.2    Li, Y.3    Hu, L.4    Luo, D.5
  • 21
    • 79957560384 scopus 로고    scopus 로고
    • Simple and efficient immobilization of lipase B from Candida antarctica on porous styrene-divinylbenzene beads
    • Hernandez K., Garcia-Galan C., Fernández-Lafuente R. Simple and efficient immobilization of lipase B from Candida antarctica on porous styrene-divinylbenzene beads. Enzyme Microb. Technol. 2011, 49:72-78.
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 72-78
    • Hernandez, K.1    Garcia-Galan, C.2    Fernández-Lafuente, R.3
  • 22
    • 0032486523 scopus 로고    scopus 로고
    • A single step purification, immobilization and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
    • Bastida A., Sabuquillo P., Armisén P., Fernández-Lafuente R., Huguet J., Guisán J.M. A single step purification, immobilization and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol. Bioeng. 1998, 58:486-493.
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 486-493
    • Bastida, A.1    Sabuquillo, P.2    Armisén, P.3    Fernández-Lafuente, R.4    Huguet, J.5    Guisán, J.M.6
  • 23
    • 0034697072 scopus 로고    scopus 로고
    • Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches
    • Villeneuve P., Muderhwa J.M., Graille J., Haas M.J. Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J. Mol. Catal. B: Enzym. 2000, 9:113-148.
    • (2000) J. Mol. Catal. B: Enzym. , vol.9 , pp. 113-148
    • Villeneuve, P.1    Muderhwa, J.M.2    Graille, J.3    Haas, M.J.4
  • 27
    • 84874691680 scopus 로고    scopus 로고
    • The spinning cloth disc reactor for immobilized enzymes: a new process intensification technology for enzymatic reactions
    • Feng X., Patterson D.A., Balaban M., Fauconnier G., Emanuelsson E.A.C. The spinning cloth disc reactor for immobilized enzymes: a new process intensification technology for enzymatic reactions. Chem. Eng. J. 2013, 221:407-417.
    • (2013) Chem. Eng. J. , vol.221 , pp. 407-417
    • Feng, X.1    Patterson, D.A.2    Balaban, M.3    Fauconnier, G.4    Emanuelsson, E.A.C.5
  • 28
    • 84889652117 scopus 로고    scopus 로고
    • Immobilization of porcine pancreatic lipase on poly-hydroxybutyrate particles for the production of ethyl esters from macaw palm oils and pineapple flavor
    • Silva N.C.A., Miranda J.S., Bolina I.C.A., Silva W.C., Hirata D.B., Castro H.F., Mendes A.A. Immobilization of porcine pancreatic lipase on poly-hydroxybutyrate particles for the production of ethyl esters from macaw palm oils and pineapple flavor. Biochem. Eng. J. 2014, 82:139-149.
    • (2014) Biochem. Eng. J. , vol.82 , pp. 139-149
    • Silva, N.C.A.1    Miranda, J.S.2    Bolina, I.C.A.3    Silva, W.C.4    Hirata, D.B.5    Castro, H.F.6    Mendes, A.A.7
  • 29
    • 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., Fernández-Lorente G., Fernández-Lafuente R., Palomo J.M., Guisán J.M. Novozym 435 displays very different selectivity compared to lipase from Candida antarctica B adsorbed on other hydrophobic supports. J. Mol. Catal. B: Enzym. 2009, 57:171-176.
    • (2009) J. Mol. Catal. B: Enzym. , vol.57 , pp. 171-176
    • Cabrera, Z.1    Fernández-Lorente, G.2    Fernández-Lafuente, R.3    Palomo, J.M.4    Guisán, J.M.5
  • 30
    • 84871774120 scopus 로고    scopus 로고
    • Covalent immobilization of organic solvent tolerant lipase on aluminum oxide pellets and its potential application in esterification reaction
    • Kumar D., Nagar S., Bhushan I., Kumar L., Parshad R., Gupta V.K. Covalent immobilization of organic solvent tolerant lipase on aluminum oxide pellets and its potential application in esterification reaction. J. Mol. Catal. B: Enzym. 2013, 87:51-61.
    • (2013) J. Mol. Catal. B: Enzym. , vol.87 , pp. 51-61
    • Kumar, D.1    Nagar, S.2    Bhushan, I.3    Kumar, L.4    Parshad, R.5    Gupta, V.K.6
  • 31
    • 0037079654 scopus 로고    scopus 로고
    • Ethyl oleate synthesis by porcine pancreatic lipase in organic solvents
    • Hazarika S., Goswami P., Dutta N.N., Hazarika A.K. Ethyl oleate synthesis by porcine pancreatic lipase in organic solvents. Chem. Eng. J. 2002, 85:61-68.
    • (2002) Chem. Eng. J. , vol.85 , pp. 61-68
    • Hazarika, S.1    Goswami, P.2    Dutta, N.N.3    Hazarika, A.K.4
  • 32
    • 0033038670 scopus 로고    scopus 로고
    • Characterization and uti-lization of Candida rugosa lipase immobilized on controlled pore silica
    • Soares C.M.F., de Castro H.F., Zanin G.M., Moraes F.F. Characterization and uti-lization of Candida rugosa lipase immobilized on controlled pore silica. Appl. Biochem. Biotechnol. 1999, 77(79):745-757.
    • (1999) Appl. Biochem. Biotechnol. , vol.77 , Issue.79 , pp. 745-757
    • Soares, C.M.F.1    de Castro, H.F.2    Zanin, G.M.3    Moraes, F.F.4
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 84859754353 scopus 로고    scopus 로고
    • Immobilization of enzymes for use in organic media
    • Humana Press, Totowa, NJ, J.M. Guisan (Ed.)
    • Adlercreutz P. Immobilization of enzymes for use in organic media. Immobilization of Enzymes and Cells 2006, 251-256. Humana Press, Totowa, NJ. J.M. Guisan (Ed.).
    • (2006) Immobilization of Enzymes and Cells , pp. 251-256
    • Adlercreutz, P.1
  • 35
    • 72049131056 scopus 로고    scopus 로고
    • Insights into the modeling of adsorption isotherm systems
    • Foo K.Y., Hameed B.H. Insights into the modeling of adsorption isotherm systems. Chem. Eng. J. 2010, 156:2-10.
    • (2010) Chem. Eng. J. , vol.156 , pp. 2-10
    • Foo, K.Y.1    Hameed, B.H.2
  • 36
    • 0016037387 scopus 로고
    • Pore and solid diffusion models for fixed-bed adsorbers
    • Webber T.W., Chakkravorti R.K. Pore and solid diffusion models for fixed-bed adsorbers. AIChE J. 1974, 20:228-238.
    • (1974) AIChE J. , vol.20 , pp. 228-238
    • Webber, T.W.1    Chakkravorti, R.K.2
  • 37
    • 0023435073 scopus 로고
    • Single-step unimolecular non-first-order enzyme deactivation kinetics
    • Sadana A., Henley J.P. Single-step unimolecular non-first-order enzyme deactivation kinetics. Biotechnol. Bioeng. 1987, 30:717-723.
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 717-723
    • Sadana, A.1    Henley, J.P.2
  • 39
    • 84862817808 scopus 로고    scopus 로고
    • Immobilization of Burkholderia sp. lipase on a ferric silica nanocomposite for biodiesel production
    • Tran D.T., Chen C.L., Chang J.S. Immobilization of Burkholderia sp. lipase on a ferric silica nanocomposite for biodiesel production. J. Biotechnol. 2012, 158:112-119.
    • (2012) J. Biotechnol. , vol.158 , pp. 112-119
    • Tran, D.T.1    Chen, C.L.2    Chang, J.S.3
  • 40
    • 84856216198 scopus 로고    scopus 로고
    • Surface functionalized mesoporous activated carbon for the immobilization of acidic lipase and their application to hydrolysis of waste cooked oil: isotherm and kinetic studies
    • Ramani K., Karthikeyan S., Boopathy R., Kennedy L.J., Mandal A.B., Sekaran G. Surface functionalized mesoporous activated carbon for the immobilization of acidic lipase and their application to hydrolysis of waste cooked oil: isotherm and kinetic studies. Process Biochem. 2012, 47:435-445.
    • (2012) Process Biochem. , vol.47 , pp. 435-445
    • Ramani, K.1    Karthikeyan, S.2    Boopathy, R.3    Kennedy, L.J.4    Mandal, A.B.5    Sekaran, G.6
  • 41
    • 34548837202 scopus 로고    scopus 로고
    • Immobilization of mushroom polyphenol oxidase on poly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) macroporous beaded copolymers
    • Vaidya B.K., Karale A.J., Suthar H.K., Ingavle G., Pathak T.S., Ponrathnam S., Nene S. Immobilization of mushroom polyphenol oxidase on poly(allyl glycidyl ether-co-ethylene glycol dimethacrylate) macroporous beaded copolymers. React. Funct. Polym. 2007, 67:905-915.
    • (2007) React. Funct. Polym. , vol.67 , pp. 905-915
    • Vaidya, B.K.1    Karale, A.J.2    Suthar, H.K.3    Ingavle, G.4    Pathak, T.S.5    Ponrathnam, S.6    Nene, S.7
  • 43
    • 84898538492 scopus 로고    scopus 로고
    • Kinetics of enzymatic transesterification and thermal deactivation using immobilized Burkholderia lipase as catalyst
    • Tran D.T., Chang J.S. Kinetics of enzymatic transesterification and thermal deactivation using immobilized Burkholderia lipase as catalyst. Bioprocess. Biosyst. Eng. 2014, 37:481-491.
    • (2014) Bioprocess. Biosyst. Eng. , vol.37 , pp. 481-491
    • Tran, D.T.1    Chang, J.S.2
  • 44
    • 7444222410 scopus 로고    scopus 로고
    • Kinetic and thermodynamic properties of an immobilized endoglucanase from Arachniotus citrinus
    • Saleem M., Rashid M.H., Jabbar A., Perveen R., Khalid A.M., Rajoka M.I. Kinetic and thermodynamic properties of an immobilized endoglucanase from Arachniotus citrinus. Process Biochem. 2005, 40:849-855.
    • (2005) Process Biochem. , vol.40 , pp. 849-855
    • Saleem, M.1    Rashid, M.H.2    Jabbar, A.3    Perveen, R.4    Khalid, A.M.5    Rajoka, M.I.6
  • 45
    • 80052964449 scopus 로고    scopus 로고
    • Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8
    • Olesesan A.T., Azura L.K., Forghani B., Bakar F.A., Mohamed A.K.S., Radu S., Manap M.Y.A., Saari N. Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8. New Biotechnol. 2011, 28:738-745.
    • (2011) New Biotechnol. , vol.28 , pp. 738-745
    • Olesesan, A.T.1    Azura, L.K.2    Forghani, B.3    Bakar, F.A.4    Mohamed, A.K.S.5    Radu, S.6    Manap, M.Y.A.7    Saari, N.8
  • 46
    • 0038735357 scopus 로고    scopus 로고
    • Kinetic modeling of immobilized-lipase catalyzed transesterification of n-octanol with vinyl acetate in non-aqueous media
    • Yadav G.D., Trivedi A.H. Kinetic modeling of immobilized-lipase catalyzed transesterification of n-octanol with vinyl acetate in non-aqueous media. Enzyme Microb. Technol. 2003, 32:783-789.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 783-789
    • Yadav, G.D.1    Trivedi, A.H.2
  • 47
    • 78649330812 scopus 로고    scopus 로고
    • Optimized synthesis of (Z)-3-hexen-1-yl caproate using germinated rapeseed lipase in organic solvent
    • Liaquat M. Optimized synthesis of (Z)-3-hexen-1-yl caproate using germinated rapeseed lipase in organic solvent. J. Mol. Catal. B: Enzym. 2011, 68:59-65.
    • (2011) J. Mol. Catal. B: Enzym. , vol.68 , pp. 59-65
    • Liaquat, M.1
  • 48
    • 84856318182 scopus 로고    scopus 로고
    • Synthesis of n-amyl isobutyrate catalyzed by Candida rugosa lipase immobilized into poly(N-isopropylacrylamide-co-itaconic acid) hydrogels
    • Milasinovic N., Knezevic-Jugovic Z., Jakovljevic Z., Filipovic J., Krusic M.K. Synthesis of n-amyl isobutyrate catalyzed by Candida rugosa lipase immobilized into poly(N-isopropylacrylamide-co-itaconic acid) hydrogels. Chem. Eng. J. 2012, 181-182:614-623.
    • (2012) Chem. Eng. J. , pp. 614-623
    • Milasinovic, N.1    Knezevic-Jugovic, Z.2    Jakovljevic, Z.3    Filipovic, J.4    Krusic, M.K.5
  • 49
    • 0035931397 scopus 로고    scopus 로고
    • Kinetic characterization of enzymatic esterification in a solvent system: adsorptive control of water with molecular sieves
    • Giacometti J., Giacometti F., Milin C., Vasic-Racki D. Kinetic characterization of enzymatic esterification in a solvent system: adsorptive control of water with molecular sieves. J. Mol. Catal. B: Enzym. 2001, 11:921-928.
    • (2001) J. Mol. Catal. B: Enzym. , vol.11 , pp. 921-928
    • Giacometti, J.1    Giacometti, F.2    Milin, C.3    Vasic-Racki, D.4
  • 52
    • 67649405319 scopus 로고    scopus 로고
    • Immobilized lipase-catalysed synthesis of cinnamyl laurate in non-aqueous media
    • Yadav G.D., Dhoot S.B. Immobilized lipase-catalysed synthesis of cinnamyl laurate in non-aqueous media. J. Mol. Catal. B: Enzyme 2009, 57:34-39.
    • (2009) J. Mol. Catal. B: Enzyme , vol.57 , pp. 34-39
    • Yadav, G.D.1    Dhoot, S.B.2
  • 53
    • 77649340406 scopus 로고    scopus 로고
    • Lipase-catalyzed hydrazinolysis of phenyl benzoate: kinetic modeling approach
    • Yadav G.D., Borkar I.V. Lipase-catalyzed hydrazinolysis of phenyl benzoate: kinetic modeling approach. Process Biochem. 2010, 45:586-592.
    • (2010) Process Biochem. , vol.45 , pp. 586-592
    • Yadav, G.D.1    Borkar, I.V.2
  • 54
    • 84886843763 scopus 로고    scopus 로고
    • Kinetic study of lipase catalyzed transesterification of jatropha oil in circulated batch packed bed reactor
    • Veny H., Aroua M.K., Sulaiman N.M.N. Kinetic study of lipase catalyzed transesterification of jatropha oil in circulated batch packed bed reactor. Chem. Eng. J. 2014, 237:123-130.
    • (2014) Chem. Eng. J. , vol.237 , pp. 123-130
    • Veny, H.1    Aroua, M.K.2    Sulaiman, N.M.N.3
  • 55
    • 33645421765 scopus 로고    scopus 로고
    • Lipase-catalyzed glycerolysis of fats and oils in ionic liquids: a further study on the reaction system
    • Guo Z., Xu X. Lipase-catalyzed glycerolysis of fats and oils in ionic liquids: a further study on the reaction system. Green Chem. 2006, 8:54-62.
    • (2006) Green Chem. , vol.8 , pp. 54-62
    • Guo, Z.1    Xu, X.2
  • 57
    • 79960447435 scopus 로고    scopus 로고
    • Poly(styrene-divinylbenzene) beads surface functionalized with di-block polymer grafting and multi-modal ligand attachment: performance of reversibly immobilized lipase in ester synthesis
    • Bayramoglu G., Karagoz B., Altintas B., Arica M.Y., Bicak N. Poly(styrene-divinylbenzene) beads surface functionalized with di-block polymer grafting and multi-modal ligand attachment: performance of reversibly immobilized lipase in ester synthesis. Bioprocess Biosyst. Eng. 2011, 34:735-746.
    • (2011) Bioprocess Biosyst. Eng. , vol.34 , pp. 735-746
    • Bayramoglu, G.1    Karagoz, B.2    Altintas, B.3    Arica, M.Y.4    Bicak, N.5
  • 58
    • 78049244834 scopus 로고    scopus 로고
    • Immobilization of lipase in organic solvent in the presence of fatty acid additives
    • Ozturk T.K., Kilinc A. Immobilization of lipase in organic solvent in the presence of fatty acid additives. J. Mol. Catal. B: Enzym. 2010, 67:214-218.
    • (2010) J. Mol. Catal. B: Enzym. , vol.67 , pp. 214-218
    • Ozturk, T.K.1    Kilinc, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.