메뉴 건너뛰기




Volumn 115, Issue , 2012, Pages 126-135

Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications

Author keywords

Biocatalysis; Enzymatic polymerization; Enzyme immobilization; Immobilization supports; Polymer synthesis

Indexed keywords

BIOCATALYSIS; ENVIRONMENTAL ISSUES; ENZYMATIC POLYMERIZATION; ENZYMATIC PROCESS; ENZYME PERFORMANCE; IMMOBILIZATION SUPPORT; INDUSTRIAL CATALYST; NATURAL ENZYME; ORGANIC SYNTHESIS; POLYMER SYNTHESIS; PRODUCT INHIBITION;

EID: 84861459402     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2011.11.054     Document Type: Article
Times cited : (183)

References (76)
  • 1
    • 3042854421 scopus 로고    scopus 로고
    • Effect of porosity on sulfonation of macroporous styrene-divinylbenzene beads
    • Ahmed M., Malik M.A., Pervez S., Raffiq M. Effect of porosity on sulfonation of macroporous styrene-divinylbenzene beads. Eur. Polym. J. 2004, 40:1609-1613.
    • (2004) Eur. Polym. J. , vol.40 , pp. 1609-1613
    • Ahmed, M.1    Malik, M.A.2    Pervez, S.3    Raffiq, M.4
  • 4
    • 0018416056 scopus 로고
    • Deacylation of benzylpenicillin by immobilized penicillin acylase in a continuous four-stage stirred-tank reactor
    • Carleysmith S.W., Lilly M.D. Deacylation of benzylpenicillin by immobilized penicillin acylase in a continuous four-stage stirred-tank reactor. Biotechnol. Bioeng. 1979, 21:1057-1073.
    • (1979) Biotechnol. Bioeng. , vol.21 , pp. 1057-1073
    • Carleysmith, S.W.1    Lilly, M.D.2
  • 5
    • 33847205076 scopus 로고    scopus 로고
    • Effects of macroporous resin size on Candida antarctica lipase B adsorption, fraction of active molecules, and catalytic activity for polyester synthesis
    • Chen B., Miller E.M., Miller L., Maikner J.J., Gross R.A. Effects of macroporous resin size on Candida antarctica lipase B adsorption, fraction of active molecules, and catalytic activity for polyester synthesis. Langmuir 2007, 23:1381-1387.
    • (2007) Langmuir , vol.23 , pp. 1381-1387
    • Chen, B.1    Miller, E.M.2    Miller, L.3    Maikner, J.J.4    Gross, R.A.5
  • 6
    • 34249884531 scopus 로고    scopus 로고
    • Effects of porous polystyrene resin parameters on Candida antarctica lipase B adsorption, distribution, and polyester synthesis activity
    • Chen B., Miller M.E., Gross R.A. Effects of porous polystyrene resin parameters on Candida antarctica lipase B adsorption, distribution, and polyester synthesis activity. Langmuir 2007, 23:6467-6474.
    • (2007) Langmuir , vol.23 , pp. 6467-6474
    • Chen, B.1    Miller, M.E.2    Gross, R.A.3
  • 7
    • 62649124791 scopus 로고    scopus 로고
    • Protein immobilization on epoxy-activated thin polymer films: effect of surface wettability and enzyme loading
    • Chen B., Pernodet N., Rafailovich M.H., Bakhtina A., Gross R.A. Protein immobilization on epoxy-activated thin polymer films: effect of surface wettability and enzyme loading. Langmuir 2008, 24:13457-13464.
    • (2008) Langmuir , vol.24 , pp. 13457-13464
    • Chen, B.1    Pernodet, N.2    Rafailovich, M.H.3    Bakhtina, A.4    Gross, R.A.5
  • 8
    • 84905500021 scopus 로고    scopus 로고
    • Green Polymer Chemistry: Biocatalysis and Biomaterials
    • (Eds.), ACS Symposium Series, American Chemical Society.
    • Cheng, H.N., Gross, R.A. (Eds.), 2010. Green Polymer Chemistry: Biocatalysis and Biomaterials. ACS Symposium Series. vol. 1043, American Chemical Society.
    • (2010) , pp. 1043
    • Cheng, H.N.1    Gross, R.A.2
  • 9
    • 84861461096 scopus 로고    scopus 로고
    • Enzyme-catalyzed synthesis of polyamides and polypeptides
    • Wiley-VCH, Weinheim, K. Loos (Ed.)
    • Cheng H.N. Enzyme-catalyzed synthesis of polyamides and polypeptides. Biocatalysis in Polymer Chemistry 2010, 131-141. Wiley-VCH, Weinheim. K. Loos (Ed.).
    • (2010) Biocatalysis in Polymer Chemistry , pp. 131-141
    • Cheng, H.N.1
  • 10
    • 79951791650 scopus 로고    scopus 로고
    • Electrospinning of poly[acrylonitrile-co-(glycidyl methacrylate)] nanofibrous mats for the immobilization of Candida antarctica lipase B
    • Dai T., Miletić N., Loos K., Elbahri M., Abetz V. Electrospinning of poly[acrylonitrile-co-(glycidyl methacrylate)] nanofibrous mats for the immobilization of Candida antarctica lipase B. Macromol. Chem. Phys. 2011, 212:319-327.
    • (2011) Macromol. Chem. Phys. , vol.212 , pp. 319-327
    • Dai, T.1    Miletić, N.2    Loos, K.3    Elbahri, M.4    Abetz, V.5
  • 11
    • 84886026997 scopus 로고    scopus 로고
    • Enzymatic synthesis of polyaniline and other electrically conductive polymers
    • Wiley-VCH, Weinheim, K. Loos (Ed.)
    • Cruz-Silva R., Roman P., Romera J. Enzymatic synthesis of polyaniline and other electrically conductive polymers. Biocatalysis in Polymer Chemistry 2010, 187-210. Wiley-VCH, Weinheim. K. Loos (Ed.).
    • (2010) Biocatalysis in Polymer Chemistry , pp. 187-210
    • Cruz-Silva, R.1    Roman, P.2    Romera, J.3
  • 13
    • 0035826279 scopus 로고    scopus 로고
    • Modulation of lipase properties in macro-aqueous systems by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase
    • Fernandez-Lorente G., Terreni M., Mateo C., Bastida A., Fernandez-Lafuente R., Dalmases P., Huguet J., Guisan J.M. Modulation of lipase properties in macro-aqueous systems by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase. Enzyme Microb. Technol. 2001, 28:389-396.
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 389-396
    • Fernandez-Lorente, G.1    Terreni, M.2    Mateo, C.3    Bastida, A.4    Fernandez-Lafuente, R.5    Dalmases, P.6    Huguet, J.7    Guisan, J.M.8
  • 14
    • 0141641134 scopus 로고    scopus 로고
    • Optimization of a polymeric HPLC phase: poly(glycidyl methacrylate-co-ethylene dimethacrylate): influence of the polymerization conditions on the pore structure of macroporous beads
    • Ferreira A., Bigan M., Blondeau D. Optimization of a polymeric HPLC phase: poly(glycidyl methacrylate-co-ethylene dimethacrylate): influence of the polymerization conditions on the pore structure of macroporous beads. React. Funct. Polym. 2003, 56:123-136.
    • (2003) React. Funct. Polym. , vol.56 , pp. 123-136
    • Ferreira, A.1    Bigan, M.2    Blondeau, D.3
  • 15
    • 53649085574 scopus 로고    scopus 로고
    • Immobilization of lipase on methyl-modified silica aerogels by physical adsorption
    • Gao S., Wang Y., Wang T., Luo G., Dai Y. Immobilization of lipase on methyl-modified silica aerogels by physical adsorption. Bioresour. Technol. 2009, 100:996-999.
    • (2009) Bioresour. Technol. , vol.100 , pp. 996-999
    • Gao, S.1    Wang, Y.2    Wang, T.3    Luo, G.4    Dai, Y.5
  • 16
    • 0035385138 scopus 로고    scopus 로고
    • Polymer synthesis by in vitro enzyme catalysis
    • Gross R.A., Kumar A., Kalra B. Polymer synthesis by in vitro enzyme catalysis. Chem. Rev. 2001, 101:2097-2124.
    • (2001) Chem. Rev. , vol.101 , pp. 2097-2124
    • Gross, R.A.1    Kumar, A.2    Kalra, B.3
  • 17
    • 84914017246 scopus 로고
    • Die Spaltung von Racemischer Mandelsäure mit einem optisch aktiven Anionenaustauscher
    • Grubhofer N., Schleith L. Die Spaltung von Racemischer Mandelsäure mit einem optisch aktiven Anionenaustauscher. Hoppe-Seyler's Z. Physiol. Chem. 1954, 296:262-266.
    • (1954) Hoppe-Seyler's Z. Physiol. Chem. , vol.296 , pp. 262-266
    • Grubhofer, N.1    Schleith, L.2
  • 18
    • 0000195821 scopus 로고
    • Enzymatic lactonisation of γ-hydroxyesters in organic solvents. Synthesis of optically pure γ-methylbutyrolactones and γ-phenylbutyrolactone
    • Gutman A.L., Zuobi K., Boltansky A. Enzymatic lactonisation of γ-hydroxyesters in organic solvents. Synthesis of optically pure γ-methylbutyrolactones and γ-phenylbutyrolactone. Tetrahedron Lett. 1987, 28(33):3861-3864.
    • (1987) Tetrahedron Lett. , vol.28 , Issue.33 , pp. 3861-3864
    • Gutman, A.L.1    Zuobi, K.2    Boltansky, A.3
  • 20
    • 84861458997 scopus 로고    scopus 로고
    • Enzymatic polymerization of vinyl polymers
    • Wiley-VCH, Weinheim, K. Loos (Ed.)
    • Hollmann F. Enzymatic polymerization of vinyl polymers. Biocatalysis in Polymer Chemistry 2010, 143-163. Wiley-VCH, Weinheim. K. Loos (Ed.).
    • (2010) Biocatalysis in Polymer Chemistry , pp. 143-163
    • Hollmann, F.1
  • 21
    • 84982462364 scopus 로고
    • Reactive polymers XXXV. The effect of polymerization conditions on the specific surface area of macroporous copolymers from glycidyl methacrylate-ethylene dimethacrylate
    • Horák D., Švec F., Bleha M., Kálal J. Reactive polymers XXXV. The effect of polymerization conditions on the specific surface area of macroporous copolymers from glycidyl methacrylate-ethylene dimethacrylate. Angew. Makromol. Chem. 1981, 95:109-111.
    • (1981) Angew. Makromol. Chem. , vol.95 , pp. 109-111
    • Horák, D.1    Švec, F.2    Bleha, M.3    Kálal, J.4
  • 22
    • 79955072084 scopus 로고    scopus 로고
    • Highly-stable magnetically-separable organic-inorganic hybrid microspheres for enzyme entrapment
    • Hwang E.T., Lee H., Kim J.H., Tatavarty R., Gu M.B. Highly-stable magnetically-separable organic-inorganic hybrid microspheres for enzyme entrapment. J. Mater. Chem. 2011, 21:6491-6493.
    • (2011) J. Mater. Chem. , vol.21 , pp. 6491-6493
    • Hwang, E.T.1    Lee, H.2    Kim, J.H.3    Tatavarty, R.4    Gu, M.B.5
  • 23
    • 0029745270 scopus 로고    scopus 로고
    • Targeted porous structure of macroporous copolymers based on glycidyl methacrylate
    • Jovanović S., Nastasović A., Jovanović N., Jeremić K. Targeted porous structure of macroporous copolymers based on glycidyl methacrylate. Mater. Sci. Forum 1996, 214:155-162.
    • (1996) Mater. Sci. Forum , vol.214 , pp. 155-162
    • Jovanović, S.1    Nastasović, A.2    Jovanović, N.3    Jeremić, K.4
  • 24
    • 0027575340 scopus 로고
    • Enzymatic polyesterification in organic media. Enzyme-catalyzed synthesis of linear polyesters. I. Condensation polymerization of linear hydroxyesters. II. Ring-opening polymerization of ε-caprolactone
    • Knani D., Gutman A.L., Kohn D.H. Enzymatic polyesterification in organic media. Enzyme-catalyzed synthesis of linear polyesters. I. Condensation polymerization of linear hydroxyesters. II. Ring-opening polymerization of ε-caprolactone. J. Polym. Sci. Pt A: Polym. Chem. 1993, 31:1221-1232.
    • (1993) J. Polym. Sci. Pt A: Polym. Chem. , vol.31 , pp. 1221-1232
    • Knani, D.1    Gutman, A.L.2    Kohn, D.H.3
  • 25
    • 3142763845 scopus 로고    scopus 로고
    • Application of chitin- and chitosan-based materials for enzyme immobilizations: a review
    • Krajewska B. Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. Enzyme Microb. Technol. 2004, 35:126-139.
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 126-139
    • Krajewska, B.1
  • 26
    • 10944250656 scopus 로고    scopus 로고
    • Immobilized microfluidic enzymatic reactors
    • Křenkova J., Foret F. Immobilized microfluidic enzymatic reactors. Electrophoresis 2004, 25:3550-3563.
    • (2004) Electrophoresis , vol.25 , pp. 3550-3563
    • Křenkova, J.1    Foret, F.2
  • 28
    • 73249125182 scopus 로고    scopus 로고
    • Enzymatic polymer synthesis: an opportunity for green polymer chemistry
    • Kobayashi S., Makino A. Enzymatic polymer synthesis: an opportunity for green polymer chemistry. Chem. Rev. 2009, 109:5288-5353.
    • (2009) Chem. Rev. , vol.109 , pp. 5288-5353
    • Kobayashi, S.1    Makino, A.2
  • 29
    • 57949102009 scopus 로고    scopus 로고
    • Adsorptive immobilization of enzymatic active substances on alumina-silica foam coated by carbon nanofibers
    • Kovalenko G.A., Perminova L.V., Chuenko T.V., Rudina N.A. Adsorptive immobilization of enzymatic active substances on alumina-silica foam coated by carbon nanofibers. Carbon 2009, 47:420-427.
    • (2009) Carbon , vol.47 , pp. 420-427
    • Kovalenko, G.A.1    Perminova, L.V.2    Chuenko, T.V.3    Rudina, N.A.4
  • 30
    • 78649906228 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis
    • Kumar S., Mohan U., Kamble A.L., Pawar S., Banerjee U.C. Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis. Bioresour. Technol. 2010, 101:6856-6858.
    • (2010) Bioresour. Technol. , vol.101 , pp. 6856-6858
    • Kumar, S.1    Mohan, U.2    Kamble, A.L.3    Pawar, S.4    Banerjee, U.C.5
  • 31
    • 0000735475 scopus 로고
    • Macroreticular resins. III. Formation of macroreticular styrene-divinylbenzene copolymers
    • Kun K.A., Kunin R. Macroreticular resins. III. Formation of macroreticular styrene-divinylbenzene copolymers. J. Polym. Sci. A-1 1968, 6:2689-2701.
    • (1968) J. Polym. Sci. A-1 , vol.6 , pp. 2689-2701
    • Kun, K.A.1    Kunin, R.2
  • 32
    • 84955330467 scopus 로고    scopus 로고
    • Immobilization of enzymes
    • Wiley-VCH, Weinheim, K. Drauz, H. Waldmann (Eds.)
    • Lalonde J., Margolin A. Immobilization of enzymes. Enzyme Catalysis in Organic Chemistry 2002, 163-184. Wiley-VCH, Weinheim. second ed. K. Drauz, H. Waldmann (Eds.).
    • (2002) Enzyme Catalysis in Organic Chemistry , pp. 163-184
    • Lalonde, J.1    Margolin, A.2
  • 33
    • 79955867174 scopus 로고    scopus 로고
    • Poly(2-hydroxyethyl methacrylate) for enzyme immobilization: impact on activity and stability of horseradish peroxidase
    • Lane S.M., Kuang Z., Yom J., Arifuzzaman S., Genzer J., Farmer B., Naik R., Vaia R.A. Poly(2-hydroxyethyl methacrylate) for enzyme immobilization: impact on activity and stability of horseradish peroxidase. Biomacromolecules 2011, 12:1822-1830.
    • (2011) Biomacromolecules , vol.12 , pp. 1822-1830
    • Lane, S.M.1    Kuang, Z.2    Yom, J.3    Arifuzzaman, S.4    Genzer, J.5    Farmer, B.6    Naik, R.7    Vaia, R.A.8
  • 37
    • 78650326349 scopus 로고    scopus 로고
    • Immobilization of penicillin G acylase in epoxy-activated magnetic cellulose microspheres for improvement of biocatalytic stability and activities
    • Luo X., Zhang L. Immobilization of penicillin G acylase in epoxy-activated magnetic cellulose microspheres for improvement of biocatalytic stability and activities. Biomacromolecules 2010, 11:2896-2903.
    • (2010) Biomacromolecules , vol.11 , pp. 2896-2903
    • Luo, X.1    Zhang, L.2
  • 38
    • 79953762889 scopus 로고
    • über einige chemische umsetzungen am polyaminostyrol
    • Manecke G., Singer S. über einige chemische umsetzungen am polyaminostyrol. Makromol. Chem. 1960, 37:119-142.
    • (1960) Makromol. Chem. , vol.37 , pp. 119-142
    • Manecke, G.1    Singer, S.2
  • 39
    • 0034575018 scopus 로고    scopus 로고
    • Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage
    • Mateo C., Fernandez-Lorente G., Abian O., Fernandez-Lafuente R., Guisan J.M. Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage. Biomacromolecules 2000, 1:739-745.
    • (2000) Biomacromolecules , vol.1 , pp. 739-745
    • Mateo, C.1    Fernandez-Lorente, G.2    Abian, O.3    Fernandez-Lafuente, R.4    Guisan, J.M.5
  • 43
    • 0040773468 scopus 로고
    • Synthese von verbindungen der cellulose mit eiweißstoffen
    • Micheel F., Ewers J. Synthese von verbindungen der cellulose mit eiweißstoffen. Makromol. Chem. 1949, 3:200-209.
    • (1949) Makromol. Chem. , vol.3 , pp. 200-209
    • Micheel, F.1    Ewers, J.2
  • 44
    • 80053574984 scopus 로고    scopus 로고
    • Immobilization - a route for improving enzyme performance
    • Research Signpost, Trivandrum, A. Nastasović, S.M. Jovanović (Eds.)
    • Miletić N., Bos C., Loos K. Immobilization - a route for improving enzyme performance. Polymeric Materials 2009, 131-153. Research Signpost, Trivandrum. A. Nastasović, S.M. Jovanović (Eds.).
    • (2009) Polymeric Materials , pp. 131-153
    • Miletić, N.1    Bos, C.2    Loos, K.3
  • 45
    • 58249131998 scopus 로고    scopus 로고
    • Macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) resins - versatile immobilization supports for biocatalysts
    • Miletić N., Vuković Z., Nastasović A., Loos K. Macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) resins - versatile immobilization supports for biocatalysts. J. Mol. Catal. B: Enzym. 2009, 56:196-201.
    • (2009) J. Mol. Catal. B: Enzym. , vol.56 , pp. 196-201
    • Miletić, N.1    Vuković, Z.2    Nastasović, A.3    Loos, K.4
  • 46
    • 73649083010 scopus 로고    scopus 로고
    • Immobilization of Candida antarctica lipase B on polystyrene nanoparticles
    • 71-71
    • Miletić N., Abetz V., Ebert K., Loos K. Immobilization of Candida antarctica lipase B on polystyrene nanoparticles. Macromol. Rapid Commun. 2010, 31. 71-71.
    • (2010) Macromol. Rapid Commun. , vol.31
    • Miletić, N.1    Abetz, V.2    Ebert, K.3    Loos, K.4
  • 47
    • 84861457889 scopus 로고    scopus 로고
    • Enzymatic polymerization of polyester
    • Wiley-VCH, Weinheim, K. Loos (Ed.)
    • Miletić N., Loos K., Gross R. Enzymatic polymerization of polyester. Biocatalysis in Polymer Chemistry 2010, 83-129. Wiley-VCH, Weinheim. K. Loos (Ed.).
    • (2010) Biocatalysis in Polymer Chemistry , pp. 83-129
    • Miletić, N.1    Loos, K.2    Gross, R.3
  • 48
    • 80355142669 scopus 로고    scopus 로고
    • Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier
    • Miletić N., Vuković Z., Nastasović A., Loos K. Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier. Macromol. Biosci. 2011, 11:1537-1543.
    • (2011) Macromol. Biosci. , vol.11 , pp. 1537-1543
    • Miletić, N.1    Vuković, Z.2    Nastasović, A.3    Loos, K.4
  • 49
    • 70349469826 scopus 로고    scopus 로고
    • Kinetics of hexavalent chromium sorption on amino-functionalized macroporous glycidyl methacrylate copolymer
    • Nastasović A., Sandić Z., Suručić Lj., Maksin D., Jakovljević D., Onjia A. Kinetics of hexavalent chromium sorption on amino-functionalized macroporous glycidyl methacrylate copolymer. J. Hazard. Mater. 2009, 171:153-159.
    • (2009) J. Hazard. Mater. , vol.171 , pp. 153-159
    • Nastasović, A.1    Sandić, Z.2    Suručić, L.3    Maksin, D.4    Jakovljević, D.5    Onjia, A.6
  • 50
    • 77951903786 scopus 로고    scopus 로고
    • Enzyme entrapment in reprecipitated polyaniline nano- and microparticles
    • Nemzer L.R., Schwartz A., Epstein A.J. Enzyme entrapment in reprecipitated polyaniline nano- and microparticles. Macromolecules 2010, 43:4324-4330.
    • (2010) Macromolecules , vol.43 , pp. 4324-4330
    • Nemzer, L.R.1    Schwartz, A.2    Epstein, A.J.3
  • 51
    • 0001534831 scopus 로고
    • Synthesis of ester oligomer by Aspergillus niger lipase
    • Okumara S., Iwai M., Tominaga Y. Synthesis of ester oligomer by Aspergillus niger lipase. Agric. Biol. Chem. 1984, 48:2805-2808.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 2805-2808
    • Okumara, S.1    Iwai, M.2    Tominaga, Y.3
  • 53
    • 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., Munoz G., Fernandez-Lorente G., Mateo C., Fernandez-Lafuente R., Guisan J.M. 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. 2002, 19-20:279-286.
    • (2002) J. Mol. Catal. B: Enzym. , pp. 279-286
    • Palomo, J.M.1    Munoz, G.2    Fernandez-Lorente, G.3    Mateo, C.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 55
    • 58249132554 scopus 로고    scopus 로고
    • Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase
    • Pchelintsev N.A., Youshko M.I., Švedas V.K. Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase. J. Mol. Catal. B: Enzym. 2009, 56:202-207.
    • (2009) J. Mol. Catal. B: Enzym. , vol.56 , pp. 202-207
    • Pchelintsev, N.A.1    Youshko, M.I.2    Švedas, V.K.3
  • 56
    • 78651149328 scopus 로고
    • Intermolecular cross linking of a protein in the crystalline state: carboxypeptidase-A
    • Quiocho F.A., Richards F.M. Intermolecular cross linking of a protein in the crystalline state: carboxypeptidase-A. Proc. Natl. Acad. Sci. 1964, 52:833-839.
    • (1964) Proc. Natl. Acad. Sci. , vol.52 , pp. 833-839
    • Quiocho, F.A.1    Richards, F.M.2
  • 57
    • 0000639866 scopus 로고
    • The enzymic behavior of carboxypeptidase-A in the solid state
    • Quiocho F.A., Richards F.M. The enzymic behavior of carboxypeptidase-A in the solid state. Biochemistry 1966, 5:4062-4076.
    • (1966) Biochemistry , vol.5 , pp. 4062-4076
    • Quiocho, F.A.1    Richards, F.M.2
  • 58
    • 0030569931 scopus 로고
    • Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials
    • Reetz M.T., Zonta A., Simpelkamp J. Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials. Biotechnol. Bioeng. 1995, 49:527-534.
    • (1995) Biotechnol. Bioeng. , vol.49 , pp. 527-534
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3
  • 59
    • 0041687879 scopus 로고    scopus 로고
    • Second generation sol-gel encapsulated lipases: robust heterogeneous biocatalysts
    • Reetz M.T., Tielmann P., Wiesenhofer W., Konen W., Zonta A. Second generation sol-gel encapsulated lipases: robust heterogeneous biocatalysts. Adv. Synth. Catal. 2003, 345:717-728.
    • (2003) Adv. Synth. Catal. , vol.345 , pp. 717-728
    • Reetz, M.T.1    Tielmann, P.2    Wiesenhofer, W.3    Konen, W.4    Zonta, A.5
  • 60
    • 4644259549 scopus 로고    scopus 로고
    • Strategies in making cross-linked enzyme crystals
    • Roy J.J., Abraham T.E. Strategies in making cross-linked enzyme crystals. Chem. Rev. 2004, 104:3705-3721.
    • (2004) Chem. Rev. , vol.104 , pp. 3705-3721
    • Roy, J.J.1    Abraham, T.E.2
  • 62
    • 34648813464 scopus 로고    scopus 로고
    • Characterization of Candida rugosa lipase immobilized on poly(N-methylolacrylamide) and its application in butyl butyrate synthesis
    • Santos J.C., Nunes G.F.M., Moreira A.B.R., Perez V.H., de Castro H.F. Characterization of Candida rugosa lipase immobilized on poly(N-methylolacrylamide) and its application in butyl butyrate synthesis. Chem. Eng. Technol. 2007, 30:1255-1261.
    • (2007) Chem. Eng. Technol. , vol.30 , pp. 1255-1261
    • Santos, J.C.1    Nunes, G.F.M.2    Moreira, A.B.R.3    Perez, V.H.4    de Castro, H.F.5
  • 63
    • 84861459352 scopus 로고    scopus 로고
    • Improved immobilization supports for Candida antarctica lipase B
    • Wiley-VCH, Weinheim, K. Loos (Ed.)
    • Saunders P., Brask J. Improved immobilization supports for Candida antarctica lipase B. Biocatalysis in Polymer Chemistry 2010, 65-82. Wiley-VCH, Weinheim. K. Loos (Ed.).
    • (2010) Biocatalysis in Polymer Chemistry , pp. 65-82
    • Saunders, P.1    Brask, J.2
  • 64
    • 0002924359 scopus 로고
    • Makroporöse Styrol-Divinylbenzol-Copolymere und ihre Verwendung in der Chromatographie und zur Darstellung von Ionenaustauschern
    • Seidl J., Malinsky J., DuŠek K., Heitz W. Makroporöse Styrol-Divinylbenzol-Copolymere und ihre Verwendung in der Chromatographie und zur Darstellung von Ionenaustauschern. Adv. Polym. Sci. 1967, 5:113-213.
    • (1967) Adv. Polym. Sci. , vol.5 , pp. 113-213
    • Seidl, J.1    Malinsky, J.2    Dušek, K.3    Heitz, W.4
  • 65
    • 0002156239 scopus 로고    scopus 로고
    • Immobilized enzymes: methods and applications
    • Springer-Verlag, Berlin, W.D. Fressner (Ed.)
    • Tischer W., Wedekind F. Immobilized enzymes: methods and applications. Biocatalysis-From Discovery to Application 1999, 95-126. Springer-Verlag, Berlin. W.D. Fressner (Ed.).
    • (1999) Biocatalysis-From Discovery to Application , pp. 95-126
    • Tischer, W.1    Wedekind, F.2
  • 66
    • 84948044359 scopus 로고
    • Studies on continuous enzyme reactions. Part V. Kinetics and industrial application of aminoacylase column for continuous optical resolution of acyl-dl-amino acids
    • Tosa T., Mori T., Fuse N., Chibata I. Studies on continuous enzyme reactions. Part V. Kinetics and industrial application of aminoacylase column for continuous optical resolution of acyl-dl-amino acids. Agric. Biol. Chem. 1969, 33:1047-1052.
    • (1969) Agric. Biol. Chem. , vol.33 , pp. 1047-1052
    • Tosa, T.1    Mori, T.2    Fuse, N.3    Chibata, I.4
  • 67
    • 0002977652 scopus 로고
    • Enzymatic ring-opening polymerization of lactones catalyzed by lipase
    • Uyama H., Kobayashi S. Enzymatic ring-opening polymerization of lactones catalyzed by lipase. Chem. Lett. 1993, 22:1149-1150.
    • (1993) Chem. Lett. , vol.22 , pp. 1149-1150
    • Uyama, H.1    Kobayashi, S.2
  • 68
    • 33746877356 scopus 로고    scopus 로고
    • Enzymatic synthesis of polyesters via polycondensation
    • Springer-Verlag, Berlin, S. Kobayashi, H. Ritter, D. Kaplan (Eds.)
    • Uyama H., Kobayashi S. Enzymatic synthesis of polyesters via polycondensation. Enzyme-Catalyzed Synthesis of Polymers 2006, 133-158. Springer-Verlag, Berlin. S. Kobayashi, H. Ritter, D. Kaplan (Eds.).
    • (2006) Enzyme-Catalyzed Synthesis of Polymers , pp. 133-158
    • Uyama, H.1    Kobayashi, S.2
  • 69
    • 84861457395 scopus 로고    scopus 로고
    • Enzymatic polymerization of phenolic monomers
    • Wiley-VCH, Weinheim, K. Loos (Ed.)
    • Uyama H. Enzymatic polymerization of phenolic monomers. Biocatalysis in Polymer Chemistry 2010, 165-185. Wiley-VCH, Weinheim. K. Loos (Ed.).
    • (2010) Biocatalysis in Polymer Chemistry , pp. 165-185
    • Uyama, H.1
  • 70
    • 84885976106 scopus 로고    scopus 로고
    • Enzymatic polymerizations of polysaccharides
    • Wiley-VCH, Weinheim, K. Loos (Ed.)
    • van der Vlist J., Loos K. Enzymatic polymerizations of polysaccharides. Biocatalysis in Polymer Chemistry 2010, 211-246. Wiley-VCH, Weinheim. K. Loos (Ed.).
    • (2010) Biocatalysis in Polymer Chemistry , pp. 211-246
    • van der Vlist, J.1    Loos, K.2
  • 71
    • 84875995175 scopus 로고    scopus 로고
    • Transferases in polymer chemistry
    • Springer-Verlag, Berlin, A.R.A. Palmans, A. Heise (Eds.)
    • van der Vlist J., Loos K. Transferases in polymer chemistry. Enzymatic Polymerization 2010, 21-54. Springer-Verlag, Berlin. A.R.A. Palmans, A. Heise (Eds.).
    • (2010) Enzymatic Polymerization , pp. 21-54
    • van der Vlist, J.1    Loos, K.2
  • 74
    • 33846850057 scopus 로고    scopus 로고
    • Synthesis of N-methylglucamine modified macroporous poly(GMA-co-TRIM) and its performance as a boron sorbent
    • Wang L., Qi T., Gao Z., Zhang Y., Chu J. Synthesis of N-methylglucamine modified macroporous poly(GMA-co-TRIM) and its performance as a boron sorbent. React. Funct. Polym. 2007, 67:202-209.
    • (2007) React. Funct. Polym. , vol.67 , pp. 202-209
    • Wang, L.1    Qi, T.2    Gao, Z.3    Zhang, Y.4    Chu, J.5
  • 75
    • 67651109235 scopus 로고    scopus 로고
    • Enzymatic conversion of Baicalin into Baicalein by β-glucuronidase encapsulated in biomimetic core-shell structured hybrid capsules
    • Zhang Y., Wu H., Li L., Li J., Jiang Z., Jiang Y., Chen Y. Enzymatic conversion of Baicalin into Baicalein by β-glucuronidase encapsulated in biomimetic core-shell structured hybrid capsules. J. Mol. Catal. B: Enzym. 2009, 57:130-135.
    • (2009) J. Mol. Catal. B: Enzym. , vol.57 , pp. 130-135
    • Zhang, Y.1    Wu, H.2    Li, L.3    Li, J.4    Jiang, Z.5    Jiang, Y.6    Chen, Y.7
  • 76
    • 74649083867 scopus 로고    scopus 로고
    • Artificial neural network-genetic algorithm based optimization for the immobilization of cellulase on the smart polymer Eudragit L-100
    • Zhang Y., Xu J., Yuan Z., Xu H., Yu Q. Artificial neural network-genetic algorithm based optimization for the immobilization of cellulase on the smart polymer Eudragit L-100. Bioresour. Technol. 2010, 101:3153-3158.
    • (2010) Bioresour. Technol. , vol.101 , pp. 3153-3158
    • Zhang, Y.1    Xu, J.2    Yuan, Z.3    Xu, H.4    Yu, Q.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.