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Volumn 35, Issue 1, 2015, Pages 15-28

Optimization protocols and improved strategies of cross-linked enzyme aggregates technology: Current development and future challenges

Author keywords

Biocatalysis; Cross linked enzyme aggregates; Enzyme immobilization; Improved strategies; Process optimization

Indexed keywords

AGGREGATES; OPTIMIZATION; PROCESS CONTROL;

EID: 84923375346     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.3109/07388551.2013.795516     Document Type: Review
Times cited : (232)

References (138)
  • 1
    • 2942756031 scopus 로고    scopus 로고
    • Enantioselective synthesis of phenylacetamides in the presence of high organic cosolvent concentrations catalyzed by stabilized penicillin G acylase. Effect of the acyl donor
    • Abian O, Mateo C, Palomo JM, et al. (2004). Enantioselective synthesis of phenylacetamides in the presence of high organic cosolvent concentrations catalyzed by stabilized penicillin G acylase. Effect of the acyl donor. Biotechnol Prog, 20, 984-8.
    • (2004) Biotechnol Prog , vol.20 , pp. 984-988
    • Abian, O.1    Mateo, C.2    Palomo, J.M.3
  • 3
    • 69749104380 scopus 로고    scopus 로고
    • How to overcome limitations in biotechnological processes-examples from hydroxynitrile lyase applications
    • Andexer JN, Langermann JV, Kragl U, Pohl M. (2009). How to overcome limitations in biotechnological processes-examples from hydroxynitrile lyase applications. Trends Biotechnol, 27, 599-608.
    • (2009) Trends Biotechnol , vol.27 , pp. 599-608
    • Andexer, J.N.1    Langermann, J.V.2    Kragl, U.3    Pohl, M.4
  • 4
    • 84869067264 scopus 로고    scopus 로고
    • Laccase-based CLEAs: Chitosan as a novel cross-linking agent
    • [Epub ahead of print]
    • Arsenault A, Cabana H, Peter Jones J. (2011). Laccase-based CLEAs: chitosan as a novel cross-linking agent. Enzyme Res [Epub ahead of print], doi:10.4061/2011/376015.
    • (2011) Enzyme Res
    • Arsenault, A.1    Cabana, H.2    Peter Jones, J.3
  • 5
    • 84859448274 scopus 로고    scopus 로고
    • Highly biocompatible enzyme aggregates crosslinked by L-lysine
    • Ayhan H, Ayhan F, Gülsu A. (2012). Highly biocompatible enzyme aggregates crosslinked by L-lysine. Turk J Biochem, 37, 14-20.
    • (2012) Turk J Biochem , vol.37 , pp. 14-20
    • Ayhan, H.1    Ayhan, F.2    Gülsu, A.3
  • 6
    • 38049085641 scopus 로고    scopus 로고
    • Preparation of cross-linked tyrosinase aggregates
    • Aytar BS, Bakir U. (2008). Preparation of cross-linked tyrosinase aggregates. Process Biochem, 43, 125-31.
    • (2008) Process Biochem , vol.43 , pp. 125-131
    • Aytar, B.S.1    Bakir, U.2
  • 7
    • 72049108887 scopus 로고    scopus 로고
    • Influence of alcohols and osmolytes on thermal stability and catalytic activity of myoglobin: Co-solvent clustering effects
    • Bellezza F, Cipiciani A, Cinell, S, Onori G. (2009). Influence of alcohols and osmolytes on thermal stability and catalytic activity of myoglobin: co-solvent clustering effects. Chem Phys Lett, 482, 139-42.
    • (2009) Chem Phys Lett , vol.482 , pp. 139-142
    • Bellezza, F.1    Cipiciani, A.2    Cinell, S.3    Onori, G.4
  • 8
    • 51249110348 scopus 로고    scopus 로고
    • Bioinspired enzyme encapsulation for biocatalysis
    • Betancor L, Luckarift HR. (2008). Bioinspired enzyme encapsulation for biocatalysis. Trends Biotechnol, 26, 566-72.
    • (2008) Trends Biotechnol , vol.26 , pp. 566-572
    • Betancor, L.1    Luckarift, H.R.2
  • 9
    • 0037171640 scopus 로고    scopus 로고
    • Enzymes immobilized on magnetic carriers: Efficient and selective system for protein modification
    • BÍlková Z, Slováková M, Horák D, et al. (2002). Enzymes immobilized on magnetic carriers: efficient and selective system for protein modification. J Chromatogr B Anal Technol Biomed Life Sci, 770, 177-81.
    • (2002) J Chromatogr B Anal Technol Biomed Life Sci , vol.770 , pp. 177-181
    • Bílková, Z.1    Slováková, M.2    Horák, D.3
  • 10
    • 0036323592 scopus 로고    scopus 로고
    • Eupergit oxirane acrylic beads: How to make the enzyme fit for biocatalysts
    • Boller T, Meier C, Menzler S. (2002). Eupergit oxirane acrylic beads: how to make the enzyme fit for biocatalysts. Org Process Res Dev, 6, 509-19.
    • (2002) Org Process Res Dev , vol.6 , pp. 509-519
    • Boller, T.1    Meier, C.2    Menzler, S.3
  • 11
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilization
    • Brady D, Jordaan J. (2009). Advances in enzyme immobilization. Biotechnol Lett, 31, 1639-50.
    • (2009) Biotechnol Lett , vol.31 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 12
    • 34848883383 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals
    • Cabana H, Jones JP, Agathos SN. (2007). Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. J Biotechnol, 132, 23-31.
    • (2007) J Biotechnol , vol.132 , pp. 23-31
    • Cabana, H.1    Jones, J.P.2    Agathos, S.N.3
  • 13
    • 64949125943 scopus 로고    scopus 로고
    • Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine-disrupting chemicals
    • Cabana H, Jones JP, Agathos SN. (2009). Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine-disrupting chemicals. Biotechnol Bioeng, 102, 1582-92.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1582-1592
    • Cabana, H.1    Jones, J.P.2    Agathos, S.N.3
  • 14
    • 55049131930 scopus 로고    scopus 로고
    • Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: A recyclable enantioselective catalyst
    • Cabirol FL, Tan PL, Tay B, et al. (2008). Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: a recyclable enantioselective catalyst. Adv Synth Catal, 350, 2329-38.
    • (2008) Adv Synth Catal , vol.350 , pp. 2329-2338
    • Cabirol, F.L.1    Tan, P.L.2    Tay, B.3
  • 15
    • 0034682159 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates: A simple and effective method for the immobilization of penicillin acylase
    • Cao L, van Rantwijk F, Sheldon RA. (2000). Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase. Org Lett, 2, 1361-4.
    • (2000) Org Lett , vol.2 , pp. 1361-1364
    • Cao, L.1    Van Rantwijk, F.2    Sheldon, R.A.3
  • 17
    • 67651036201 scopus 로고    scopus 로고
    • Acetonitrile-induced unfolding of porcine pepsin A: A proposal for a critical role of hydration structures in conformational stability
    • Cardoso T, Oliveira C, Sarmento AC, et al. (2009). Acetonitrile-induced unfolding of porcine pepsin A: a proposal for a critical role of hydration structures in conformational stability. Int J Biol Macromol, 45, 213-20.
    • (2009) Int J Biol Macromol , vol.45 , pp. 213-220
    • Cardoso, T.1    Oliveira, C.2    Sarmento, A.C.3
  • 18
    • 78349258236 scopus 로고    scopus 로고
    • Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial applications
    • Cerdobbel A, Winter KD, Desmet T, Soetaert W. (2010). Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications. Biotechnol J, 5, 1192-7.
    • (2010) Biotechnol J , vol.5 , pp. 1192-1197
    • Cerdobbel, A.1    Winter, K.D.2    Desmet, T.3    Soetaert, W.4
  • 19
    • 84872977574 scopus 로고    scopus 로고
    • Baeyer-Villiger oxidation with peracid generated in situ by CaLB-CLEA catalyzed perhydrolysis
    • Chávez G, Kaul RH, Sheldon RA, Mamo G. (2013). Baeyer-Villiger oxidation with peracid generated in situ by CaLB-CLEA catalyzed perhydrolysis. J Mol Catal B Enzym, 89, 67-72.
    • (2013) J Mol Catal B Enzym , vol.89 , pp. 67-72
    • Chávez, G.1    Kaul, R.H.2    Sheldon, R.A.3    Mamo, G.4
  • 20
    • 33644635865 scopus 로고    scopus 로고
    • Synthesis of cross-linked enzyme aggregates (CLEAs) in CO2-expanded micellar solutions
    • Chen J, Zhang JL, Han BX, et al. (2006). Synthesis of cross-linked enzyme aggregates (CLEAs) in CO2-expanded micellar solutions. Colloid Surf B, 48, 72-6.
    • (2006) Colloid Surf B , vol.48 , pp. 72-76
    • Chen, J.1    Zhang, J.L.2    Han, B.X.3
  • 21
    • 84865732724 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of b-glucosidase from Prunus domestica seeds
    • Chen L, Hu YD, Li N, Zong MH. (2012). Cross-linked enzyme aggregates of b-glucosidase from Prunus domestica seeds. Biotechnol Lett, 34, 1673-8.
    • (2012) Biotechnol Lett , vol.34 , pp. 1673-1678
    • Chen, L.1    Hu, Y.D.2    Li, N.3    Zong, M.H.4
  • 22
    • 0042432086 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes: An update
    • Cherry JR, Fidantsef AL. (2003). Directed evolution of industrial enzymes: an update. Curr Opin Biotechnol, 14, 438-43.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 438-443
    • Cherry, J.R.1    Fidantsef, A.L.2
  • 23
    • 80051793850 scopus 로고    scopus 로고
    • Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
    • Cowan DA, Fernandez-Lafuente R. (2011). Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzyme Microb Tech, 49, 326-46.
    • (2011) Enzyme Microb Tech , vol.49 , pp. 326-346
    • Cowan, D.A.1    Fernandez-Lafuente, R.2
  • 24
    • 85027941304 scopus 로고    scopus 로고
    • Optimization of medium for phenylalanine ammonia lyase production in E. Coli using response surface methodology
    • Cui JD. (2010). Optimization of medium for phenylalanine ammonia lyase production in E. coli using response surface methodology. Korean J Chem Eng, 27, 174-8.
    • (2010) Korean J Chem Eng , vol.27 , pp. 174-178
    • Cui, J.D.1
  • 25
    • 43949141783 scopus 로고    scopus 로고
    • Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia. Coli
    • Cui JD, Jia SR, Sun AY. (2008). Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia. coli. Lett Appl Microbiol, 46, 631-5.
    • (2008) Lett Appl Microbiol , vol.46 , pp. 631-635
    • Cui, J.D.1    Jia, S.R.2    Sun, A.Y.3
  • 26
    • 84863720938 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of phenylalanine ammonia lyase: Novel biocatalysts for synthesis of L-phenylalanine
    • Cui JD, Zhang S, Sun LM. (2012). Cross-linked enzyme aggregates of phenylalanine ammonia lyase: novel biocatalysts for synthesis of L-phenylalanine. Appl Biochem Biotechol, 167, 835-44.
    • (2012) Appl Biochem Biotechol , vol.167 , pp. 835-844
    • Cui, J.D.1    Zhang, S.2    Sun, L.M.3
  • 27
    • 33846489558 scopus 로고    scopus 로고
    • Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions
    • Dalal S, Kapoor M, Gupta MN. (2007a). Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions. J Mol Catal B Enzym, 44, 128-32.
    • (2007) J Mol Catal B Enzym , vol.44 , pp. 128-132
    • Dalal, S.1    Kapoor, M.2    Gupta, M.N.3
  • 28
    • 34547350610 scopus 로고    scopus 로고
    • A multipurpose immobilized biocatalyst with pectinase, xylanase and cellulase activities
    • Dalal S, Shaema A, Gupta MN. (2007b). A multipurpose immobilized biocatalyst with pectinase, xylanase and cellulase activities. Chem Cent J, 1, 16-21.
    • (2007) Chem Cent J , vol.1 , pp. 16-21
    • Dalal, S.1    Shaema, A.2    Gupta, M.N.3
  • 30
    • 33947315288 scopus 로고    scopus 로고
    • Stability and activity of enzyme aggregates of Calb in supercritical CO2
    • Dijkstra ZJ, Merchant RZ, Keurentjes JTF. (2007). Stability and activity of enzyme aggregates of Calb in supercritical CO2. J Supercrit Fluids, 41, 102-8.
    • (2007) J Supercrit Fluids , vol.41 , pp. 102-108
    • Dijkstra, Z.J.1    Merchant, R.Z.2    Keurentjes, J.T.F.3
  • 31
    • 84923378085 scopus 로고    scopus 로고
    • A new application of supercritical CO2 technology for cross linked enzyme aggregates
    • Dinçyüerk D, Aptis H, Salfin S, Salgin U. (2012). A new application of supercritical CO2 technology for cross linked enzyme aggregates. New Biotechnol, 29, S84.
    • (2012) New Biotechnol , vol.29 , pp. S84
    • Dinçyüerk, D.1    Aptis, H.2    Salfin, S.3    Salgin, U.4
  • 32
    • 77955496659 scopus 로고    scopus 로고
    • Preparation of crosslinked aggregates of aminoacylase from Aspergillus melleus by using bovine serum albumin as an inert additive
    • Dong T, Zhao L, Huang Y, Tan X. (2010). Preparation of crosslinked aggregates of aminoacylase from Aspergillus melleus by using bovine serum albumin as an inert additive. Bioresour Technol, 101, 6569-71.
    • (2010) Bioresour Technol , vol.101 , pp. 6569-6571
    • Dong, T.1    Zhao, L.2    Huang, Y.3    Tan, X.4
  • 33
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation
    • Fernandez-Lafuente R. (2009). Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb Tech, 45, 405-418.
    • (2009) Enzyme Microb Tech , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 34
    • 0038583463 scopus 로고    scopus 로고
    • Bio-imprinting of lipases with fatty acids
    • Fishman A, Cogan U. (2003). Bio-imprinting of lipases with fatty acids. J Mol Catal B Enzym, 22, 193-202.
    • (2003) J Mol Catal B Enzym , vol.22 , pp. 193-202
    • Fishman, A.1    Cogan, U.2
  • 35
    • 78049316762 scopus 로고    scopus 로고
    • Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase
    • Frushicheva MP, Cao J, Chu ZT, Warshe A. (2010). Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase. PNAS, 107, 16869-74.
    • (2010) PNAS , vol.107 , pp. 16869-16874
    • Frushicheva, M.P.1    Cao, J.2    Chu, Z.T.3    Warshe, A.4
  • 36
    • 84870783601 scopus 로고    scopus 로고
    • Chemical amination of lipase B from Candida antarctica is an efficient solution for the preparation of crosslinked enzyme aggregates
    • Galvis M, Barbosa O, Cruz J, et al. (2012). Chemical amination of lipase B from Candida antarctica is an efficient solution for the preparation of crosslinked enzyme aggregates. Process Biochem, 47, 2373-8.
    • (2012) Process Biochem , vol.47 , pp. 2373-2378
    • Galvis, M.1    Barbosa, O.2    Cruz, J.3
  • 40
    • 84870482214 scopus 로고    scopus 로고
    • Formation of enzyme polymer engineered structure for laccase and cross-linked laccase aggregates stabilization
    • Hassani T, Ba S, Cabana H. (2013). Formation of enzyme polymer engineered structure for laccase and cross-linked laccase aggregates stabilization. Bioresour Technol, 128, 640-5.
    • (2013) Bioresour Technol , vol.128 , pp. 640-645
    • Hassani, T.1    Ba, S.2    Cabana, H.3
  • 41
    • 36849048228 scopus 로고    scopus 로고
    • Intrinsic motions along an enzymatic reaction trajectory
    • Henzler-Wildman KA, Thai V, Lei M, et al. (2007). Intrinsic motions along an enzymatic reaction trajectory. Nature, 450, 838-44.
    • (2007) Nature , vol.450 , pp. 838-844
    • Henzler-Wildman, K.A.1    Thai, V.2    Lei, M.3
  • 42
    • 78650818528 scopus 로고    scopus 로고
    • Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
    • Hernandez K, Fernandez-Lafuente R. (2011). Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance. Enzyme Microb Tech, 48, 107-22.
    • (2011) Enzyme Microb Tech , vol.48 , pp. 107-122
    • Hernandez, K.1    Fernandez-Lafuente, R.2
  • 43
    • 37749006460 scopus 로고    scopus 로고
    • Immobilization of thermophilic enzymes in miniaturized flow reactors
    • Hickey AM, Marle L, McCreedy T, et al. (2007). Immobilization of thermophilic enzymes in miniaturized flow reactors. Biochem Soc Tran, 35, 1621-3.
    • (2007) Biochem Soc Tran , vol.35 , pp. 1621-1623
    • Hickey, A.M.1    Marle, L.2    McCreedy, T.3
  • 44
    • 2942517661 scopus 로고    scopus 로고
    • Immobilization of crosslinked lipase aggregates within microporous polymeric membranes
    • Hilal N, Nigmatullin R, Patova RA. (2004). Immobilization of crosslinked lipase aggregates within microporous polymeric membranes. J Memb Sci, 238, 131-41.
    • (2004) J Memb Sci , vol.238 , pp. 131-141
    • Hilal, N.1    Nigmatullin, R.2    Patova, R.A.3
  • 45
    • 33847415135 scopus 로고    scopus 로고
    • Integrated microreaction system for optical resolution of racemic amino acids
    • Honda T, Miyazaki M, Yamaguchi Y, et al. (2007). Integrated microreaction system for optical resolution of racemic amino acids. Lab Chip, 7, 366-72.
    • (2007) Lab Chip , vol.7 , pp. 366-372
    • Honda, T.1    Miyazaki, M.2    Yamaguchi, Y.3
  • 46
    • 84861456071 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates (CLEAs) of recombinant poly-3-hydroxybutyrate depolymerase from Streptomyces exfoliatus
    • Hormigo D, GarcIá-Hidalgo J, Acebal C, et al. (2012). Preparation and characterization of cross-linked enzyme aggregates (CLEAs) of recombinant poly-3-hydroxybutyrate depolymerase from Streptomyces exfoliatus. Bioresour Technol, 115, 177-82.
    • (2012) Bioresour Technol , vol.115 , pp. 177-182
    • Hormigo, D.1    Garciá-Hidalgo, J.2    Acebal, C.3
  • 47
    • 84872415717 scopus 로고    scopus 로고
    • Enzyme stabilization by nano/microsized hybrid materials
    • Hwang ET, Gu MB. (2013). Enzyme stabilization by nano/microsized hybrid materials. Eng Life Sci, 13, 49-61.
    • (2013) Eng Life Sci , vol.13 , pp. 49-61
    • Hwang, E.T.1    Gu, M.B.2
  • 48
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilizationaqueous and non-aqueous environment
    • Iyer PV, Ananthanarayan L. (2008). Enzyme stability and stabilizationaqueous and non-aqueous environment. Process Biochem, 43, 1019-32.
    • (2008) Process Biochem , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 49
    • 0037141606 scopus 로고    scopus 로고
    • Evaluation of the performance of immobilized penicillin G acylase using activesite titration
    • Janssen MHA, van Langen LM, Pereira SRM, et al. (2002). Evaluation of the performance of immobilized penicillin G acylase using activesite titration. Biotechnol Bioeng, 78, 425-32.
    • (2002) Biotechnol Bioeng , vol.78 , pp. 425-432
    • Janssen, M.H.A.1    Van Langen, L.M.2    Pereira, S.R.M.3
  • 50
    • 84862610938 scopus 로고    scopus 로고
    • Preparation of immobilized lipase through combination of cross-linked enzyme aggregates and biomimetic silicification
    • Jiang YJ, Wang Q, Wang WQ, et al. (2012). Preparation of immobilized lipase through combination of cross-linked enzyme aggregates and biomimetic silicification. Chin J Catal, 33, 857-62.
    • (2012) Chin J Catal , vol.33 , pp. 857-862
    • Jiang, Y.J.1    Wang, Q.2    Wang, W.Q.3
  • 51
    • 0028816956 scopus 로고
    • Horse liver alcohol dehydrogenase can accept NADP as coenzyme in high concentrations of acetonitrile
    • Johansson A, Mosbach K, Mansson MO. (1995). Horse liver alcohol dehydrogenase can accept NADP as coenzyme in high concentrations of acetonitrile. Eur J Biochem, 227, 551-5.
    • (1995) Eur J Biochem , vol.227 , pp. 551-555
    • Johansson, A.1    Mosbach, K.2    Mansson, M.O.3
  • 52
    • 77649220084 scopus 로고    scopus 로고
    • Biotransformation of amides to acids using a co-cross-linked enzyme aggregate of Rhodococcus erythropolis amidase
    • Joo PH, Uhm KN, Kim HK. (2010). Biotransformation of amides to acids using a co-cross-linked enzyme aggregate of Rhodococcus erythropolis amidase. J Microbiol Biotechnol, 20, 325-31.
    • (2010) J Microbiol Biotechnol , vol.20 , pp. 325-331
    • Joo, P.H.1    Uhm, K.N.2    Kim, H.K.3
  • 53
    • 84869882126 scopus 로고    scopus 로고
    • Characterization and preparation of highly stable aggregates of a novel type of hydrolase (BL28) from Bacillus licheniformis
    • Ju H, Jang E, Ryu BH, Kim TD. (2013). Characterization and preparation of highly stable aggregates of a novel type of hydrolase (BL28) from Bacillus licheniformis. Bioresour Technol, 128, 81-6.
    • (2013) Bioresour Technol , vol.128 , pp. 81-86
    • Ju, H.1    Jang, E.2    Ryu, B.H.3    Kim, T.D.4
  • 54
    • 84873999847 scopus 로고    scopus 로고
    • One-pot bioconversion of sucrose to trehalose using enzymatic sequential reactions in combined cross-linked enzyme aggregates
    • 2013
    • Jung DH, Jung JH, Seo DH, et al. (2013). One-pot bioconversion of sucrose to trehalose using enzymatic sequential reactions in combined cross-linked enzyme aggregates. Bioresour Technol, 2013, 130, 801-4.
    • (2013) Bioresour Technol , vol.130 , pp. 801-804
    • Jung, D.H.1    Jung, J.H.2    Seo, D.H.3
  • 55
    • 72049093472 scopus 로고    scopus 로고
    • Formation of cross-linked glucose oxidase aggregates in mesocellular foams
    • Jung D, Paradiso M, Hartmann M. (2009). Formation of cross-linked glucose oxidase aggregates in mesocellular foams. J Mater Sci, 44, 6747-53.
    • (2009) J Mater Sci , vol.44 , pp. 6747-6753
    • Jung, D.1    Paradiso, M.2    Hartmann, M.3
  • 56
    • 84870052901 scopus 로고    scopus 로고
    • Bioimprinted immobilization of Candida antarctica lipase A for concentration of omega-3 polyunsaturated fatty acids
    • Kahveci D, Xu XB. (2012). Bioimprinted immobilization of Candida antarctica lipase A for concentration of omega-3 polyunsaturated fatty acids. J Am Oil Chem Soc, 89, 1839-45.
    • (2012) J Am Oil Chem Soc , vol.89 , pp. 1839-1845
    • Kahveci, D.1    Xu, X.B.2
  • 57
    • 33846842389 scopus 로고    scopus 로고
    • Molecular imprinting of cyclodextrin glycosyltransferases from Paenibacillus sp. A11 and Bacillus macerans with g-cyclodextrin
    • Kaulpiboon J, Pongsawasdi P, Zimmermann W. (2007). Molecular imprinting of cyclodextrin glycosyltransferases from Paenibacillus sp. A11 and Bacillus macerans with g-cyclodextrin. FEBS J, 274, 1001-10.
    • (2007) FEBS J , vol.274 , pp. 1001-1010
    • Kaulpiboon, J.1    Pongsawasdi, P.2    Zimmermann, W.3
  • 58
    • 82355169618 scopus 로고    scopus 로고
    • Recent advances and applications of immobilized enzyme technologies: A review
    • Khan AA, Alzohairy MA. (2010). Recent advances and applications of immobilized enzyme technologies: a review. Res J Biol Sci, 5, 565-75.
    • (2010) Res J Biol Sci , vol.5 , pp. 565-575
    • Khan, A.A.1    Alzohairy, M.A.2
  • 59
    • 77954262707 scopus 로고    scopus 로고
    • Immobilization of cross-linked lipase aggregates onto magnetic beads for enzymatic degradation of polycaprolactone
    • Kim M, Park JM, Um HJ, et al. (2010). Immobilization of cross-linked lipase aggregates onto magnetic beads for enzymatic degradation of polycaprolactone. J Basic Microbiol, 50, 218-26.
    • (2010) J Basic Microbiol , vol.50 , pp. 218-226
    • Kim, M.1    Park, J.M.2    Um, H.J.3
  • 60
    • 84863025476 scopus 로고    scopus 로고
    • Synthesis and characterization of CLEA-lysozyme immobilized PS/PSMA nanofiber
    • Kim M, Park JM, Yoon J, Kim YH. (2011). Synthesis and characterization of CLEA-lysozyme immobilized PS/PSMA nanofiber. J Nanosci Nanotechnol, 11, 7894-900.
    • (2011) J Nanosci Nanotechnol , vol.11 , pp. 7894-7900
    • Kim, M.1    Park, J.M.2    Yoon, J.3    Kim, Y.H.4
  • 61
    • 33846932034 scopus 로고    scopus 로고
    • Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization
    • Kim MIL, Kim JB, Jia HF, et al. (2007). Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: a simple and effective method for enzyme stabilization. Biotechnol Bioeng, 96, 210-8.
    • (2007) Biotechnol Bioeng , vol.96 , pp. 210-218
    • Kim, M.I.L.1    Kim, J.B.2    Jia, H.F.3
  • 62
    • 41649097552 scopus 로고    scopus 로고
    • One-dimensional crosslinked enzyme aggregates in SBA-15: Superior catalytic behavior to conventional enzyme immobilization
    • Kim MIL, Kim JB, Lee JW, et al. (2008). One-dimensional crosslinked enzyme aggregates in SBA-15: superior catalytic behavior to conventional enzyme immobilization. Micropor Micropor Mater, 111, 18-23.
    • (2008) Micropor Micropor Mater , vol.111 , pp. 18-23
    • Kim, M.I.L.1    Kim, J.B.2    Lee, J.W.3
  • 63
    • 78649906228 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis
    • Kumar S, Mohan U, Kamble AL, et al. (2010). Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis. Bioresour Technol, 101, 6856-8.
    • (2010) Bioresour Technol , vol.101 , pp. 6856-6858
    • Kumar, S.1    Mohan, U.2    Kamble, A.L.3
  • 64
    • 27844571788 scopus 로고    scopus 로고
    • Simple synthesis of hierarchically ordered mesocellular mesoporous silica materials hosting crosslinked enzyme aggregates
    • Lee JW, Kim JB, Kim JY, et al. (2005a). Simple synthesis of hierarchically ordered mesocellular mesoporous silica materials hosting crosslinked enzyme aggregates. Small, 7, 744-53.
    • (2005) Small , vol.7 , pp. 744-753
    • Lee, J.W.1    Kim, J.B.2    Kim, J.Y.3
  • 65
    • 28044449397 scopus 로고    scopus 로고
    • Preparation of a magnetically switchable bio-electrocatalytic system employing cross-linked enzyme aggregates in magnetic mesocellular carbon foam
    • Lee JW, Lee DH, Oh E, et al. (2005b). Preparation of a magnetically switchable bio-electrocatalytic system employing cross-linked enzyme aggregates in magnetic mesocellular carbon foam. Angew Chem Int Ed, 44, 7427-32.
    • (2005) Angew Chem Int Ed , vol.44 , pp. 7427-7432
    • Lee, J.W.1    Lee, D.H.2    Oh, E.3
  • 66
    • 84880105717 scopus 로고    scopus 로고
    • Evaluation of immobilized enzymes for industrial applications
    • Liese A, Hilterhaus L. (2013). Evaluation of immobilized enzymes for industrial applications. Chem Soc Rev [Epub ahead of print], doi:10.1039/C3CS35511J.
    • (2013) Chem Soc Rev [Epub Ahead of Print]
    • Liese, A.1    Hilterhaus, L.2
  • 67
    • 79961191747 scopus 로고    scopus 로고
    • Conformation and activity of sol-gels encapsulated cross-linked enzyme aggregates of lipase from Burkholderia cepacia
    • Liu Y, Guo YL, Chen DW, et al. (2011). Conformation and activity of sol-gels encapsulated cross-linked enzyme aggregates of lipase from Burkholderia cepacia. Adv Mater Res, 291-294, 614-20.
    • (2011) Adv Mater Res , vol.291-294 , pp. 614-620
    • Liu, Y.1    Guo, Y.L.2    Chen, D.W.3
  • 68
    • 0036671720 scopus 로고    scopus 로고
    • Crosslinked enzyme aggregates with enhanced activity: Application to lipases
    • López-Serrano P, Cao L, Van Ranteijk, Sheldon RA. (2002). Crosslinked enzyme aggregates with enhanced activity: application to lipases. Biotechnol Lett, 24, 1379-83.
    • (2002) Biotechnol Lett , vol.24 , pp. 1379-1383
    • López-Serrano, P.1    Cao, L.2    Van Ranteijk3    Sheldon, R.A.4
  • 69
    • 33947602594 scopus 로고    scopus 로고
    • Improvement of enzyme activity, stability and selectivity via immobilization techniques
    • Mateo C, Palomo JM, Fernandez-Lorente G, et al. (2007). Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Tech, 40, 1451-63.
    • (2007) Enzyme Microb Tech , vol.40 , pp. 1451-1463
    • Mateo, C.1    Palomo, J.M.2    Fernandez-Lorente, G.3
  • 70
    • 2342420355 scopus 로고    scopus 로고
    • A new, mild crosslinking methodology to prepare cross-linked enzyme aggregates
    • Mateo C, Palomo JM, van Langen LM, et al. (2004). A new, mild crosslinking methodology to prepare cross-linked enzyme aggregates. Biotechnol Bioeng, 86, 273-6.
    • (2004) Biotechnol Bioeng , vol.86 , pp. 273-276
    • Mateo, C.1    Palomo, J.M.2    Van Langen, L.M.3
  • 71
    • 71249115113 scopus 로고    scopus 로고
    • Preparation and use of cross-linked enzyme aggregates (CLEAs) of laccases
    • Matijosyte I, Arends IWCE, de Vries S, Sheldon RA. (2010). Preparation and use of cross-linked enzyme aggregates (CLEAs) of laccases. J Mol Catal B Enzym, 62, 142-8.
    • (2010) J Mol Catal B Enzym , vol.62 , pp. 142-148
    • Matijosyte, I.1    Iwce, A.2    De Vries, S.3    Sheldon, R.A.4
  • 72
    • 49649123905 scopus 로고    scopus 로고
    • Co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase on to aryamine glass beads affixed on plastic strip for determination of triglycerides in serum
    • Minakshi, Pundir CS. (2008). Co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase on to aryamine glass beads affixed on plastic strip for determination of triglycerides in serum. Indian J Biochem Biophys, 45, 111-5.
    • (2008) Indian J Biochem Biophys , vol.45 , pp. 111-115
    • Minakshi1    Pundir, C.S.2
  • 73
    • 70249089069 scopus 로고    scopus 로고
    • Improved cross-linked enzyme aggregates for the production of desacetyl b-lactam antibiotics intermediates
    • Montoro-Garcá S, Gil-Ortiz F, Navarro-Fernández J, et al. (2010). Improved cross-linked enzyme aggregates for the production of desacetyl b-lactam antibiotics intermediates. Bioresour Technol, 101, 331-6.
    • (2010) Bioresour Technol , vol.101 , pp. 331-336
    • Montoro-Garcá, S.1    Gil-Ortiz, F.2    Navarro-Fernández, J.3
  • 74
    • 84873496493 scopus 로고    scopus 로고
    • Directed evolution of a model primordial enzyme provides insights into the development of the genetic code
    • Müller MM, Allison JR, Hongdilokkul N, et al. (2013). Directed evolution of a model primordial enzyme provides insights into the development of the genetic code. PLOS Genet, 9, 1-9 e1003187.
    • (2013) PLOS Genet , vol.9 , Issue.1-9 , pp. e1003187
    • Müller, M.M.1    Allison, J.R.2    Hongdilokkul, N.3
  • 75
    • 1842609060 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of cotton fibers in supercritical CO2
    • Muratov G, Kim C. (2002). Enzymatic hydrolysis of cotton fibers in supercritical CO2. Biotechnol Bioproc E, 7, 85-8.
    • (2002) Biotechnol Bioproc e , vol.7 , pp. 85-88
    • Muratov, G.1    Kim, C.2
  • 76
    • 84866363855 scopus 로고    scopus 로고
    • Characterization of bioimprinted tannase and its kinetic and thermodynamics properties in synthesis of propyl gallate by transesterification in anhydrous medium
    • Nie GJ, Zheng ZM, Gong GH, et al. (2012). Characterization of bioimprinted tannase and its kinetic and thermodynamics properties in synthesis of propyl gallate by transesterification in anhydrous medium. Appl Biochem Biotechnol, 167, 2305-17.
    • (2012) Appl Biochem Biotechnol , vol.167 , pp. 2305-2317
    • Nie, G.J.1    Zheng, Z.M.2    Gong, G.H.3
  • 77
    • 77951975638 scopus 로고    scopus 로고
    • Water miscible mono alcohols effect on the structural conformation of Bacillus clausii GMBAE 42 serine alkaline protease
    • Ö ztürk DC, Kazan D, Denizci AA, et al. (2010). Water miscible mono alcohols effect on the structural conformation of Bacillus clausii GMBAE 42 serine alkaline protease. J Mol Catal B Enzym, 64, 184-8.
    • (2010) J Mol Catal B Enzym , vol.64 , pp. 184-188
    • Ztürk, D.C.O.1    Kazan, D.2    Denizci, A.A.3
  • 78
    • 78651379960 scopus 로고    scopus 로고
    • Cross-linking of enzyme coaggregate with polyethyleneimine: A simple and promising method for preparing stable biocatalyst of Serratia marcescens lipase
    • Pan J, Kong XD, Li CX, et al. (2011). Cross-linking of enzyme coaggregate with polyethyleneimine: a simple and promising method for preparing stable biocatalyst of Serratia marcescens lipase. J Mol Catal B Enzym, 68, 256-61.
    • (2011) J Mol Catal B Enzym , vol.68 , pp. 256-261
    • Pan, J.1    Kong, X.D.2    Li, C.X.3
  • 79
    • 84871414583 scopus 로고    scopus 로고
    • Immobilization of lysozyme-CLEA onto electrospun chitosan nanofiber for effective antibacterial applications
    • Park JM, Kim M, Park HS, et al. (2013). Immobilization of lysozyme-CLEA onto electrospun chitosan nanofiber for effective antibacterial applications. Int J Bio Macromol, 54, 37-43.
    • (2013) Int J Bio Macromol , vol.54 , pp. 37-43
    • Park, J.M.1    Kim, M.2    Park, H.S.3
  • 80
    • 71249098174 scopus 로고    scopus 로고
    • Immobilization of the crosslinked para-nitrobenzyl esterase of Bacillus subtilis aggregates onto magnetic beads
    • Park JM, Kim M, Park JY, et al. (2010). Immobilization of the crosslinked para-nitrobenzyl esterase of Bacillus subtilis aggregates onto magnetic beads. Process Biochem, 45, 259-63.
    • (2010) Process Biochem , vol.45 , pp. 259-263
    • Park, J.M.1    Kim, M.2    Park, J.Y.3
  • 81
    • 84869016992 scopus 로고    scopus 로고
    • Enhancing the production of Rhodobacter sphaeroides-derived physiologically active substances using carbonic anhydrase-immobilized electrospun nanofibers
    • Park JM, Kim MN, Lee HJ, et al. (2012). Enhancing the production of Rhodobacter sphaeroides-derived physiologically active substances using carbonic anhydrase-immobilized electrospun nanofibers. Macromolecules, 13, 3780-6.
    • (2012) Macromolecules , vol.13 , pp. 3780-3786
    • Park, J.M.1    Kim, M.N.2    Lee, H.J.3
  • 82
    • 3543087310 scopus 로고    scopus 로고
    • Trends and innovations in industrial biocatalysis for the production of fine chemicals
    • Panke S, Held M, Wubbolts M. (2004). Trends and innovations in industrial biocatalysis for the production of fine chemicals. Curr Opin Biotechnol, 15, 272-9.
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 272-279
    • Panke, S.1    Held, M.2    Wubbolts, M.3
  • 83
    • 33745762337 scopus 로고    scopus 로고
    • Biocatalysis: Synthesis of chiral intermediates for pharmaceuticals
    • Patel RN. (2006). Biocatalysis: synthesis of chiral intermediates for pharmaceuticals. Curr Org Chem, 10, 1289-321.
    • (2006) Curr Org Chem , vol.10 , pp. 1289-1321
    • Patel, R.N.1
  • 84
    • 58249132554 scopus 로고    scopus 로고
    • Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase
    • Pchelintsev NA, Youshko MI, S vedas VK. (2009). Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase. J Mol Catal B Enzym, 256, 202-7.
    • (2009) J Mol Catal B Enzym , vol.256 , pp. 202-207
    • Pchelintsev, N.A.1    Youshko, M.I.2    Vedas, V.K.S.3
  • 85
    • 33846197938 scopus 로고    scopus 로고
    • Biocatalysis for pharmaceutical intermediates: The future is now
    • Pollard DJ, Woodley JM. (2007). Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol, 25, 66-73.
    • (2007) Trends Biotechnol , vol.25 , pp. 66-73
    • Pollard, D.J.1    Woodley, J.M.2
  • 86
    • 78651149328 scopus 로고
    • Intermolecular cross-linking of a protein in the crystalline state: Carboxypeptidase A
    • Quiocho FA, Richards FM. (1964). Intermolecular cross-linking of a protein in the crystalline state: carboxypeptidase A. PNAS, 52, 833-9.
    • (1964) PNAS , vol.52 , pp. 833-839
    • Quiocho, F.A.1    Richards, F.M.2
  • 87
    • 0000639866 scopus 로고
    • The enzyme behaviors of carboxypeptidase-A in the solid state
    • Quiocho FA, Richards FM. (1966). The enzyme behaviors of carboxypeptidase-A in the solid state. Biochemistry, 5, 4062-76.
    • (1966) Biochemistry , vol.5 , pp. 4062-4076
    • Quiocho, F.A.1    Richards, F.M.2
  • 88
    • 84866849112 scopus 로고    scopus 로고
    • Improved biochemical characteristics of cross linked b-glucosidase on nanoporous silica foams
    • Reshmi R, Sugunan S. (2013). Improved biochemical characteristics of cross linked b-glucosidase on nanoporous silica foams. J Mol Catal B Enzym, 85-86, 111-8.
    • (2013) J Mol Catal B Enzym , vol.85-86 , pp. 111-118
    • Reshmi, R.1    Sugunan, S.2
  • 89
    • 84868153783 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of naringinase: Novel biocatalysts for naringin hydrolysis
    • Ribeiro MHL, Rabaça M. (2011). Cross-linked enzyme aggregates of naringinase: novel biocatalysts for naringin hydrolysis. Enzyme Res, 1, 1-8.
    • (2011) Enzyme Res , vol.1 , pp. 1-8
    • Ribeiro, M.H.L.1    Rabaça, M.2
  • 90
    • 80051787511 scopus 로고    scopus 로고
    • Coupling chemical modification and immobilization to improve the catalytic performance of enzymes
    • Rodrigues RC, Berenguer-Murcia A, Fernandez-Lafuente R. (2011). Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Adv Synth Catal, 353, 2216-38.
    • (2011) Adv Synth Catal , vol.353 , pp. 2216-2238
    • Rodrigues, R.C.1    Berenguer-Murcia, A.2    Fernandez-Lafuente, R.3
  • 91
    • 84873693763 scopus 로고    scopus 로고
    • Modifying enzyme activity and selectivity by immobilization
    • [Epub ahead of print]
    • Rodrigues RC, Ortiz C, Berenguer-Murcia A, et al. (2013). Modifying enzyme activity and selectivity by immobilization. Chem Soc Rev [Epub ahead of print], doi: 10.1039/C2CS35231A.
    • (2013) Chem Soc Rev
    • Rodrigues, R.C.1    Ortiz, C.2    Berenguer-Murcia, A.3
  • 92
    • 77649336425 scopus 로고    scopus 로고
    • Carrier-free immobilized enzymes for biocatalysis
    • Roessl U, Nahálká J, Nidetzky B. (2010). Carrier-free immobilized enzymes for biocatalysis. Biotechnol Lett, 32, 341-50.
    • (2010) Biotechnol Lett , vol.32 , pp. 341-350
    • Roessl, U.1    Nahálká, J.2    Nidetzky, B.3
  • 93
    • 0024297108 scopus 로고    scopus 로고
    • Inhibitor-induced enzyme activation in organic solvents
    • Russel A, Klibanov A. (1998). Inhibitor-induced enzyme activation in organic solvents. J Biol Chem, 263, 11624-6.
    • (1998) J Biol Chem , vol.263 , pp. 11624-11626
    • Russel, A.1    Klibanov, A.2
  • 94
    • 50049088751 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications
    • Sangeetha K, Abraham E. (2008). Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications. Int J Bio Macromol, 43, 314-9.
    • (2008) Int J Bio Macromol , vol.43 , pp. 314-319
    • Sangeetha, K.1    Abraham, E.2
  • 95
    • 4644232857 scopus 로고    scopus 로고
    • Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs)
    • Schoevaart R, Wolbers MW, Golubovic M, et al. (2004). Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs). Biotechnol Bioeng, 87, 754-62.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 754-762
    • Schoevaart, R.1    Wolbers, M.W.2    Golubovic, M.3
  • 96
    • 33645298457 scopus 로고    scopus 로고
    • Preparation of cross-linked enzyme aggregates by using bovine serum albumin as a proteic feeder
    • Shah S, Sharma A, Gupta MN. (2006). Preparation of cross-linked enzyme aggregates by using bovine serum albumin as a proteic feeder. Anal Biochem, 351, 207-13.
    • (2006) Anal Biochem , vol.351 , pp. 207-213
    • Shah, S.1    Sharma, A.2    Gupta, M.N.3
  • 97
    • 51149085668 scopus 로고    scopus 로고
    • Preparation and property of magnetic cross-Linked nuclease P1 aggregations
    • Shao WX, Mo XY, Li L. (2008). Preparation and property of magnetic cross-Linked nuclease P1 aggregations. Hsi-An Chiao Tung Ta Hsueh, 42, 1035-8.
    • (2008) Hsi-An Chiao Tung Ta Hsueh , vol.42 , pp. 1035-1038
    • Shao, W.X.1    Mo, X.Y.2    Li, L.3
  • 98
    • 37749006119 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs): Stable and recyclable biocatalysts
    • Sheldon RA. (2007). Cross-linked enzyme aggregates (CLEAs): stable and recyclable biocatalysts. Biochem Soc Trans, 35, 1583-7.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1583-1587
    • Sheldon, R.A.1
  • 99
    • 82355169635 scopus 로고    scopus 로고
    • Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs)
    • Sheldon RA. (2011a). Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Appl Microbiol Biotechnol, 92, 467-77.
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 467-477
    • Sheldon, R.A.1
  • 100
    • 79251469073 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates as industrial biocatalysts
    • Sheldon RA. (2011b). Cross-linked enzyme aggregates as industrial biocatalysts. Org Process Res Dev, 15, 213-23.
    • (2011) Org Process Res Dev , vol.15 , pp. 213-223
    • Sheldon, R.A.1
  • 101
    • 28244452921 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs): A novel and versatile method for enzyme immobilization (a review)
    • Sheldon RA, Schoevaart R, van Langen LM. (2005). Cross-linked enzyme aggregates (CLEAs): a novel and versatile method for enzyme immobilization (a review). Biocatal Biotransfor, 23, 141-7.
    • (2005) Biocatal Biotransfor , vol.23 , pp. 141-147
    • Sheldon, R.A.1    Schoevaart, R.2    Van Langen, L.M.3
  • 102
    • 84878656888 scopus 로고    scopus 로고
    • From protein engineering to immobilization: Promising strategies for the upgrade of industrial enzymes
    • Singh RK, Tiwari MK, Singh R, Lee JK. (2013). From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes. Int J Mol Sci, 14, 1232-77.
    • (2013) Int J Mol Sci , vol.14 , pp. 1232-1277
    • Singh, R.K.1    Tiwari, M.K.2    Singh, R.3    Lee, J.K.4
  • 103
    • 33745727403 scopus 로고    scopus 로고
    • Enzymatic modifications of cephalosporins by cephalosporin acylase and other enzymes
    • Sonawane VC. (2006). Enzymatic modifications of cephalosporins by cephalosporin acylase and other enzymes. Crit Rev Biotechnol, 26, 95-120.
    • (2006) Crit Rev Biotechnol , vol.26 , pp. 95-120
    • Sonawane, V.C.1
  • 104
    • 77956443206 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates in a membrane slurry reactor. Continuous production of 6-APA by enzymatic hydrolysis of penicillin
    • Sorgedrager MJ, Verdoes D, Van der Meer H, Sheldon RA. (2008). Cross-linked enzyme aggregates in a membrane slurry reactor. Continuous production of 6-APA by enzymatic hydrolysis of penicillin. Chim Oggi (Focus on Biocatalysis) 26, 23-25.
    • (2008) Chim Oggi (Focus on Biocatalysis) , vol.26 , pp. 23-25
    • Sorgedrager, M.J.1    Verdoes, D.2    Van Der Meer, H.3    Sheldon, R.A.4
  • 105
    • 79951517016 scopus 로고    scopus 로고
    • Immobilization of horseradish peroxidase as crosslinked enzyme aggregates (CLEAs)
    • S ulek F, Fernández DP, Knez Z Habulin M. (2011). Immobilization of horseradish peroxidase as crosslinked enzyme aggregates (CLEAs). Process Biochem, 46, 765-9.
    • (2011) Process Biochem , vol.46 , pp. 765-769
    • Ulek, F.S.1    Fernández, D.P.2    Knez, Z.3    Habulin, M.4
  • 106
    • 79955425303 scopus 로고    scopus 로고
    • Combined cross-linked enzyme aggregates from versatile peroxidase and glucose oxidase: Production, partial characterization and application for the elimination of endocrine disruptors
    • Taboada-Puig R, Junghabbs C, Demarche P, et al. (2011). Combined cross-linked enzyme aggregates from versatile peroxidase and glucose oxidase: production, partial characterization and application for the elimination of endocrine disruptors. Bioresour Technol, 102, 6593-9.
    • (2011) Bioresour Technol , vol.102 , pp. 6593-6599
    • Taboada-Puig, R.1    Junghabbs, C.2    Demarche, P.3
  • 107
    • 84865536720 scopus 로고    scopus 로고
    • Novel magnetic crosslinked enzyme aggregates (magnetic CLEAs) of alpha amylase
    • Talekar S, Ghodake V, Ghotage T, et al. (2012). Novel magnetic crosslinked enzyme aggregates (magnetic CLEAs) of alpha amylase. Bioresour Technol, 123, 542-7.
    • (2012) Bioresour Technol , vol.123 , pp. 542-547
    • Talekar, S.1    Ghodake, V.2    Ghotage, T.3
  • 108
    • 78649386749 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates of Saccharomyces cerevisiae invertase
    • Talekar S, Ghodake V, Kate A, et al. (2010). Preparation and characterization of cross-linked enzyme aggregates of Saccharomyces cerevisiae invertase. Aust J Basic Appl Sci, 4, 4760-5.
    • (2010) Aust J Basic Appl Sci , vol.4 , pp. 4760-4765
    • Talekar, S.1    Ghodake, V.2    Kate, A.3
  • 109
    • 84880551315 scopus 로고    scopus 로고
    • Preparation and characterization of cross linked enzyme aggregates (CLEAs) of Bacillus amyloliquefaciens alpha amylase
    • Talekar S, Waingade S, Gaikad V, et al. (2011). Preparation and characterization of cross linked enzyme aggregates (CLEAs) of Bacillus amyloliquefaciens alpha amylase. J Biochem Tech, 3, 1-5.
    • (2011) J Biochem Tech , vol.3 , pp. 1-5
    • Talekar, S.1    Waingade, S.2    Gaikad, V.3
  • 110
    • 84872410611 scopus 로고    scopus 로고
    • Effect of different parameters on the hydrolytic activity of cross-linked enzyme aggregates (CLEAs) of lipase from Thermomyces lanuginose
    • Torres MPG, Foresti ML, Ferreira ML. (2013). Effect of different parameters on the hydrolytic activity of cross-linked enzyme aggregates (CLEAs) of lipase from Thermomyces lanuginose. Biochem Eng J, 72, 18-23.
    • (2013) Biochem Eng J , vol.72 , pp. 18-23
    • Torres, M.P.G.1    Foresti, M.L.2    Ferreira, M.L.3
  • 111
    • 84874419432 scopus 로고    scopus 로고
    • Strategy of cross-linked enzyme aggregates onto magnetic particles adapted to the green design of biocatalytic synthesis of glycerol carbonate
    • Tudorache M, Nae A, Coman S, Parvulescu VI. (2013). Strategy of cross-linked enzyme aggregates onto magnetic particles adapted to the green design of biocatalytic synthesis of glycerol carbonate. RSC Adv, 3, 4052-8.
    • (2013) RSC Adv , vol.3 , pp. 4052-4058
    • Tudorache, M.1    Nae, A.2    Coman, S.3    Parvulescu, V.I.4
  • 112
    • 0347717661 scopus 로고    scopus 로고
    • Altering glucose oxidase to oxidize D-galactose through crosslinking of imprinted protein
    • Vaidya A, Borck A, Manns A, Ficher L. (2004). Altering glucose oxidase to oxidize D-galactose through crosslinking of imprinted protein. ChemBioChem, 5, 132-5.
    • (2004) ChemBioChem , vol.5 , pp. 132-135
    • Vaidya, A.1    Borck, A.2    Manns, A.3    Ficher, L.4
  • 113
    • 82755197063 scopus 로고    scopus 로고
    • Preparation of cross-linked enzyme aggregates of L-aminoacylase via co-aggregation with polyethyleneimine
    • Vaidya BK, Kuwar SS, Golegaonkar SB, Nene SN. (2012). Preparation of cross-linked enzyme aggregates of L-aminoacylase via co-aggregation with polyethyleneimine. J Mol Catal B Enzym, 74, 184-91.
    • (2012) J Mol Catal B Enzym , vol.74 , pp. 184-191
    • Vaidya, B.K.1    Kuwar, S.S.2    Golegaonkar, S.B.3    Nene, S.N.4
  • 114
    • 79956290422 scopus 로고    scopus 로고
    • Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia
    • Valdés EC, Soto LW, Arcaya GA. (2011). Influence of the pH of glutaraldehyde and the use of dextran aldehyde on the preparation of cross-linked enzyme aggregates (CLEAs) of lipase from Burkholderia cepacia. Electron J Biotechnol, 14, 1-7.
    • (2011) Electron J Biotechnol , vol.14 , pp. 1-7
    • Valdés, E.C.1    Soto, L.W.2    Arcaya, G.A.3
  • 115
  • 116
    • 60849116707 scopus 로고    scopus 로고
    • Synthesis of aliphatic (S)-A-Hydroxycarboxylic amides using a one-pot bienzymatic cascade of immobilised oxynitrilase and nitrile hydratase
    • Van Pelt S, van Rantwijk F, Sheldon RA. (2009). Synthesis of aliphatic (S)-a-hydroxycarboxylic amides using a one-pot bienzymatic cascade of immobilised oxynitrilase and nitrile hydratase. Adv Syn Catal, 351, 397-404.
    • (2009) Adv Syn Catal , vol.351 , pp. 397-404
    • Van Pelt, S.1    Van Rantwijk, F.2    Sheldon, R.A.3
  • 117
    • 84862331736 scopus 로고    scopus 로고
    • Preparation and characterization of porous cross linked laccase aggregates for the decolorization of triphenyl methane and reactive dyes
    • Vinoth Kumar V, Prem Kumar MP, Thiruvenkadaravi KV, et al. (2012). Preparation and characterization of porous cross linked laccase aggregates for the decolorization of triphenyl methane and reactive dyes. Bioresour Technol, 119, 28-34.
    • (2012) Bioresour Technol , vol.119 , pp. 28-34
    • Vinoth Kumar, V.1    Prem Kumar, M.P.2    Thiruvenkadaravi, K.V.3
  • 118
    • 79953687648 scopus 로고    scopus 로고
    • A facile technique to prepare cross-linked enzyme aggregates using p-benzoquinone as cross-linking agent
    • Wang AM, Zhang FK, Chen FF, et al. (2011a). A facile technique to prepare cross-linked enzyme aggregates using p-benzoquinone as cross-linking agent. Korean J Chem Eng, 28, 1090-5.
    • (2011) Korean J Chem Eng , vol.28 , pp. 1090-1095
    • Wang, A.M.1    Zhang, F.K.2    Chen, F.F.3
  • 119
    • 78650817240 scopus 로고    scopus 로고
    • Porous-CLEAs of papain: Application to enzymatic hydrolysis of macromolecules
    • Wang MF, Jia CX, Qi W, et al. (2011b). Porous-CLEAs of papain: application to enzymatic hydrolysis of macromolecules. Bioresour Technol, 102, 3541-5.
    • (2011) Bioresour Technol , vol.102 , pp. 3541-3545
    • Wang, M.F.1    Jia, C.X.2    Qi, W.3
  • 120
    • 80052891175 scopus 로고    scopus 로고
    • Enhancement of activity of cross-linked enzyme aggregates by a sugar-assisted precipitation strategy: Technical development and molecular mechanism
    • Wang MF, Qi W, Jia CX, et al. (2011c). Enhancement of activity of cross-linked enzyme aggregates by a sugar-assisted precipitation strategy: Technical development and molecular mechanism. J Biotechnol, 156, 30-8.
    • (2011) J Biotechnol , vol.156 , pp. 30-38
    • Wang, M.F.1    Qi, W.2    Jia, C.X.3
  • 121
    • 77957958242 scopus 로고    scopus 로고
    • Cross-linking enzyme aggregates in the macropores of silica gel: A practical and efficient method for enzyme stabilization
    • Wang MF, Qi W, Yu QX, et al. (2010). Cross-linking enzyme aggregates in the macropores of silica gel: a practical and efficient method for enzyme stabilization. Biochem Eng J, 52, 168-74.
    • (2010) Biochem Eng J , vol.52 , pp. 168-174
    • Wang, M.F.1    Qi, W.2    Yu, Q.X.3
  • 122
    • 33745222557 scopus 로고    scopus 로고
    • CLEAs of lipases and poly-ionic polymers: A simple way of preparing stable biocatalysts with improved properties
    • Wilson L, Fernández-Lorente G, Fernández-Lafuente R, et al. (2006). CLEAs of lipases and poly-ionic polymers: a simple way of preparing stable biocatalysts with improved properties. Enzyme Microb Technol, 39, 750-5.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 750-755
    • Wilson, L.1    Fernández-Lorente, G.2    Fernández-Lafuente, R.3
  • 123
    • 2542579376 scopus 로고    scopus 로고
    • Co-aggregation of penicillin G acylase and polyionic polymers: An easy methodology to prepare enzyme biocatalysts stable in organic media
    • Wilson L, Illanés A, Abián O, et al. (2004a). Co-aggregation of penicillin G acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media. Biomacromolecules, 5, 852-7.
    • (2004) Biomacromolecules , vol.5 , pp. 852-857
    • Wilson, L.1    Illanés, A.2    Abián, O.3
  • 124
    • 2542492110 scopus 로고    scopus 로고
    • Encapsulation of crosslinked penicillin G acylase aggregates in lentikats: Evaluation of a novel biocatalyst in organic media
    • Wilson L, Illanés A, Pessela BCC, et al. (2004b). Encapsulation of crosslinked penicillin G acylase aggregates in lentikats: evaluation of a novel biocatalyst in organic media. Biotechnol Bioeng, 86, 558-62.
    • (2004) Biotechnol Bioeng , vol.86 , pp. 558-562
    • Wilson, L.1    Illanés, A.2    Pessela, B.C.C.3
  • 125
    • 58249140161 scopus 로고    scopus 로고
    • Effect of the degree of cross-linking on the properties of different CLEAs of penicillin acylase
    • Wilson L, Illanés A, Soler L, HenrÍquez MJ. (2009). Effect of the degree of cross-linking on the properties of different CLEAs of penicillin acylase. Process Biochem, 44, 322-6.
    • (2009) Process Biochem , vol.44 , pp. 322-326
    • Wilson, L.1    Illanés, A.2    Soler, L.3    Henríquez, M.J.4
  • 126
    • 75349097996 scopus 로고    scopus 로고
    • A review on the effects of supercritical carbon dioxide on enzyme activity
    • Wimmer Z, Zarevúcka M. (2010). A review on the effects of supercritical carbon dioxide on enzyme activity. Int J Mol Sci, 11, 233-53.
    • (2010) Int J Mol Sci , vol.11 , pp. 233-253
    • Wimmer, Z.1    Zarevúcka, M.2
  • 127
    • 84866900049 scopus 로고    scopus 로고
    • An imprinted cross-linked enzyme aggregate (iCLEA) of sucrose phosphorylase: Combining improved stability with altered specificity
    • Winter KD, Soetaert W, Desmet T. (2012). An imprinted cross-linked enzyme aggregate (iCLEA) of sucrose phosphorylase: combining improved stability with altered specificity. Int J Mol Sci, 13, 11333-42.
    • (2012) Int J Mol Sci , vol.13 , pp. 11333-11342
    • Winter, K.D.1    Soetaert, W.2    Desmet, T.3
  • 128
    • 84867320435 scopus 로고    scopus 로고
    • Preparation of cross-linked cellulase aggregates onto magnetic chitosan microspheres
    • Xie XL, Li B, Wu ZQ, et al. (2012). Preparation of cross-linked cellulase aggregates onto magnetic chitosan microspheres. Adv Mater Res, 550-553, 1566-71.
    • (2012) Adv Mater Res , vol.550-553 , pp. 1566-1571
    • Xie, X.L.1    Li, B.2    Wu, Z.Q.3
  • 129
    • 84878109320 scopus 로고    scopus 로고
    • Cross-linked tyrosinase aggregates for elimination of phenolic compounds from wastewater
    • [Epub ahead of print]
    • Xu DY, Yang Z. (2013). Cross-linked tyrosinase aggregates for elimination of phenolic compounds from wastewater. Chemosphere [Epub ahead of print], doi: 10.1016/j.chemosphere.2012.12.076.
    • (2013) Chemosphere
    • Xu, D.Y.1    Yang, Z.2
  • 130
    • 80052984019 scopus 로고    scopus 로고
    • Poly-lysine supported cross-linked enzyme aggregates with efficient enzymatic activity and high operational stability
    • Yamaguchi H, Miyazaki M, Asanomi Y, Maeda H. (2011). Poly-lysine supported cross-linked enzyme aggregates with efficient enzymatic activity and high operational stability. Catal Sci Technol, 1, 1256-61.
    • (2011) Catal Sci Technol , vol.1 , pp. 1256-1261
    • Yamaguchi, H.1    Miyazaki, M.2    Asanomi, Y.3    Maeda, H.4
  • 131
    • 84858750322 scopus 로고    scopus 로고
    • Improving stability and activity of cross-linked enzyme aggregates based on polyethylenimine in hydrolysis of fish oil for enrichment of polyunsaturated fatty acids
    • Yan J, Gui X, Wang G, Yan Y. (2012). Improving stability and activity of cross-linked enzyme aggregates based on polyethylenimine in hydrolysis of fish oil for enrichment of polyunsaturated fatty acids. Appl Biochem Biotechnol, 166, 925-32.
    • (2012) Appl Biochem Biotechnol , vol.166 , pp. 925-932
    • Yan, J.1    Gui, X.2    Wang, G.3    Yan, Y.4
  • 132
    • 74149085150 scopus 로고    scopus 로고
    • Combination of bioimprinting and silane precursor alkyls improved the activity of sol-gel-encapsulated lipase
    • Yang JK, Liu LY, Cao XW. (2010). Combination of bioimprinting and silane precursor alkyls improved the activity of sol-gel-encapsulated lipase. Enzyme Microb Tech, 46, 257-61.
    • (2010) Enzyme Microb Tech , vol.46 , pp. 257-261
    • Yang, J.K.1    Liu, L.Y.2    Cao, X.W.3
  • 133
    • 84863472224 scopus 로고    scopus 로고
    • Highly efficient biosynthesis of sucrose-6-acetate with cross-linked aggregates of Lipozyme TL 100 L
    • Yang X, Zheng P, Ni Y, Sun Z. (2012). Highly efficient biosynthesis of sucrose-6-acetate with cross-linked aggregates of Lipozyme TL 100 L. J Biotechnol, 161, 27-33.
    • (2012) J Biotechnol , vol.161 , pp. 27-33
    • Yang, X.1    Zheng, P.2    Ni, Y.3    Sun, Z.4
  • 134
    • 0036788727 scopus 로고    scopus 로고
    • Combining the bioimprinting technique with lipase immobilization for interesterification
    • Yilmaz E. (2002). Combining the bioimprinting technique with lipase immobilization for interesterification. World J Microb Biot, 18, 621-5.
    • (2002) World J Microb Biot , vol.18 , pp. 621-625
    • Yilmaz, E.1
  • 135
    • 33751100404 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs) with controlled particles: Application to Candida rugosa lipase
    • Yu HW, Chen H, Wang X, et al. (2006). Cross-linked enzyme aggregates (CLEAs) with controlled particles: application to Candida rugosa lipase. J Mol Catal B Enzym, 43, 124-7.
    • (2006) J Mol Catal B Enzym , vol.43 , pp. 124-127
    • Yu, H.W.1    Chen, H.2    Wang, X.3
  • 136
    • 77949391703 scopus 로고    scopus 로고
    • Modeling and optimization of phenylalanine ammonia lyase stabilization in recombinant E. Coli for the continuous synthesis of L-phenylalanine on the statistical-based experimental designs
    • Zhang BZ, Cui JD. (2010). Modeling and optimization of phenylalanine ammonia lyase stabilization in recombinant E. coli for the continuous synthesis of L-phenylalanine on the statistical-based experimental designs. J Agric Food Chem, 58, 2795-800.
    • (2010) J Agric Food Chem , vol.58 , pp. 2795-2800
    • Zhang, B.Z.1    Cui, J.D.2
  • 137
    • 79954575679 scopus 로고    scopus 로고
    • Immobilization of Bacillus subtilis esterase by simple cross-linking for enzymatic resolution of DL-menthyl acetate
    • Zheng GW, Yu HL, Li CHX, et al. (2011). Immobilization of Bacillus subtilis esterase by simple cross-linking for enzymatic resolution of DL-menthyl acetate. J Mol Catal B Enzym, 70, 138-43.
    • (2011) J Mol Catal B Enzym , vol.70 , pp. 138-143
    • Zheng, G.W.1    Yu, H.L.2    Li, C.H.X.3
  • 138
    • 0030755707 scopus 로고    scopus 로고
    • Cross-linked enzyme crystals (CLECs): Efficient and stable biocatalysts for preparative organic chemistry
    • Zelinski T, Waldmann H. (2003). Cross-linked enzyme crystals (CLECs): efficient and stable biocatalysts for preparative organic chemistry. Angew Chem Int Ed Engl, 36, 722-4.
    • (2003) Angew Chem Int Ed Engl , vol.36 , pp. 722-724
    • Zelinski, T.1    Waldmann, H.2


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