메뉴 건너뛰기




Volumn 32, Issue 3, 2010, Pages 341-350

Carrier-free immobilized enzymes for biocatalysis

Author keywords

Biocatalysis; Carrier free immobilization; Cross linked enzyme aggregate; Pull down domain; Self assembling systems

Indexed keywords

BATCHWISE REACTIONS; BIOCATALYSIS; BIOCATALYTIC PROCESS; CROSS-LINKED ENZYME AGGREGATES; FREE ENZYME; FUSION PROTEINS; GAINING MOMENTUM; IMMOBILIZED ENZYME; INSOLUBLE PARTICLES; INSOLUBLE PROTEINS; LOW RESISTANCE; MECHANICAL STRESS; SELECTIVE AGGREGATION; SELF-ASSEMBLING;

EID: 77649336425     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-009-0173-4     Document Type: Review
Times cited : (116)

References (78)
  • 1
    • 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: 125-131.
    • (2008) Process Biochem , vol.43 , pp. 125-131
    • Aytar, B.S.1    Bakir, U.2
  • 2
    • 4444315219 scopus 로고    scopus 로고
    • Engineered nanopores
    • C. M. Niemeyer and C. A. Mirkin (Eds.), Weinheim: Wiley-VCH
    • Bayley H, Braha O, Cheley S, Gu L-Q (2004) Engineered nanopores. In: Niemeyer CM, Mirkin CA (eds) Nanobiotechnology. Wiley-VCH, Weinheim, pp 93-112.
    • (2004) Nanobiotechnology , pp. 93-112
    • Bayley, H.1    Braha, O.2    Cheley, S.3    Gu, L.-Q.4
  • 3
    • 51249110348 scopus 로고    scopus 로고
    • Bioinspired enzyme encapsulation for biocatalysis
    • Betancor L, Luckarift HR (2008) Bioinspired enzyme encapsulation for biocatalysis. Trends Biotechnol 26: 566-572.
    • (2008) Trends Biotechnol , vol.26 , pp. 566-572
    • Betancor, L.1    Luckarift, H.R.2
  • 4
    • 27644543684 scopus 로고    scopus 로고
    • Expression and cytosolic assembly of the S-layer fusion protein mSbsC-EGFP in eukaryotic cells
    • Blecha A, Zarschler K, Sjollema KA, Veenhuis M, Rödel G (2005) Expression and cytosolic assembly of the S-layer fusion protein mSbsC-EGFP in eukaryotic cells. Microb Cell Fact 4: 28.
    • (2005) Microb Cell Fact , vol.4 , pp. 28
    • Blecha, A.1    Zarschler, K.2    Sjollema, K.A.3    Veenhuis, M.4    Rödel, G.5
  • 7
    • 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
  • 8
    • 55049131930 scopus 로고    scopus 로고
    • Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: A recyclable enantioselective catalyst
    • Cabirol FL, Tan PL, Tay B, Cheng S, Hanefeld U, Sheldon RA (2008) Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: a recyclable enantioselective catalyst. Adv Synth Catal 350: 2329-2338.
    • (2008) Adv Synth Catal , vol.350 , pp. 2329-2338
    • Cabirol, F.L.1    Tan, P.L.2    Tay, B.3    Cheng, S.4    Hanefeld, U.5    Sheldon, R.A.6
  • 10
    • 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: 1361-1364.
    • (2000) Org Lett , vol.2 , pp. 1361-1364
    • Cao, L.1    van Rantwijk, F.2    Sheldon, R.A.3
  • 11
    • 0041430560 scopus 로고    scopus 로고
    • Immobilised enzymes: Carrier-bound or carrier-free?
    • Cao L, van Langen L, Sheldon RA (2003) Immobilised enzymes: carrier-bound or carrier-free? Curr Opin Biotechnol 14: 387-394.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 387-394
    • Cao, L.1    van Langen, L.2    Sheldon, R.A.3
  • 14
    • 44449128680 scopus 로고    scopus 로고
    • Biosilicification of dual-fusion enzyme immobilized on magnetic nanoparticle
    • Chien L-J, Lee C-K (2007) Biosilicification of dual-fusion enzyme immobilized on magnetic nanoparticle. Biotechnol Bioeng 100: 223-230.
    • (2007) Biotechnol Bioeng , vol.100 , pp. 223-230
    • Chien, L.-J.1    Lee, C.-K.2
  • 15
    • 34547350610 scopus 로고    scopus 로고
    • A multipurpose immobilized biocatalyst with pectinase, xylanase and cellulase activities
    • Dalal S, Sharma A, Gupta MN (2007) A multipurpose immobilized biocatalyst with pectinase, xylanase and cellulase activities. Chem Cent J 1: 16.
    • (2007) Chem Cent J , vol.1 , pp. 16
    • Dalal, S.1    Sharma, A.2    Gupta, M.N.3
  • 16
    • 67349269502 scopus 로고    scopus 로고
    • Construction of nanoscale protein particle using temperature-sensitive elastin-like peptide and polyaspartic acid chain
    • Fujita Y, Mie M, Kobatake E (2009) Construction of nanoscale protein particle using temperature-sensitive elastin-like peptide and polyaspartic acid chain. Biomaterials 30: 3450-3457.
    • (2009) Biomaterials , vol.30 , pp. 3450-3457
    • Fujita, Y.1    Mie, M.2    Kobatake, E.3
  • 17
    • 3142673759 scopus 로고    scopus 로고
    • Polymer nanocontainers
    • C. M. Niemeyer and C. A. Mirkin (Eds.), Weinheim: Wiley-VCH
    • Graff A, Benito SM, Verbert C, Meier W (2004) Polymer nanocontainers. In: Niemeyer CM, Mirkin CA (eds) Nanobiotechnology. Wiley-VCH, Weinheim, pp 168-184.
    • (2004) Nanobiotechnology , pp. 168-184
    • Graff, A.1    Benito, S.M.2    Verbert, C.3    Meier, W.4
  • 18
    • 38949135957 scopus 로고    scopus 로고
    • In vivo production of scFv-displaying biopolymer beads using a self-assembly-promoting fusion partner
    • Grage K, Rehm BHA (2008) In vivo production of scFv-displaying biopolymer beads using a self-assembly-promoting fusion partner. Bioconjug Chem 19: 254-262.
    • (2008) Bioconjug Chem , vol.19 , pp. 254-262
    • Grage, K.1    Rehm, B.H.A.2
  • 19
    • 0345055315 scopus 로고    scopus 로고
    • Novel biocatalysts by chemical modification of known enzymes: Cross-linked microcrystals of the semisynthetic peroxidase seleno-subtilisin
    • Haering D, Schreier P (1998) Novel biocatalysts by chemical modification of known enzymes: cross-linked microcrystals of the semisynthetic peroxidase seleno-subtilisin. Angew Chem Int Ed 37: 2471-2473.
    • (1998) Angew Chem Int Ed , vol.37 , pp. 2471-2473
    • Haering, D.1    Schreier, P.2
  • 20
    • 33745949097 scopus 로고    scopus 로고
    • Bacteriorhodopsin and its potential in technical applications
    • C. M. Niemeyer and C. A. Mirkin (Eds.), Weinheim: Wiley-VCH
    • Hampp N, Oesterhelt D (2004) Bacteriorhodopsin and its potential in technical applications. In: Niemeyer CM, Mirkin CA (eds) Nanobiotechnology. Wiley-VCH, Weinheim, pp 146-167.
    • (2004) Nanobiotechnology , pp. 146-167
    • Hampp, N.1    Oesterhelt, D.2
  • 22
    • 37049015378 scopus 로고    scopus 로고
    • Sol-gels and cross-linked aggregates of lipase PS from Burkholderia cepacia and their application in dry organic solvents
    • Hara P, Hanefeld U, Kanerva LT (2007) Sol-gels and cross-linked aggregates of lipase PS from Burkholderia cepacia and their application in dry organic solvents. J Mol Catal B 50: 80-86.
    • (2007) J Mol Catal B , vol.50 , pp. 80-86
    • Hara, P.1    Hanefeld, U.2    Kanerva, L.T.3
  • 23
    • 34547327923 scopus 로고    scopus 로고
    • SP1 as a novel scaffold building block for self-assembly nanofabrication of submicron enzymatic structures
    • Heyman A, Levy I, Altman A, Shoseyov O (2007) SP1 as a novel scaffold building block for self-assembly nanofabrication of submicron enzymatic structures. Nano Lett 7: 1575-1579.
    • (2007) Nano Lett , vol.7 , pp. 1575-1579
    • Heyman, A.1    Levy, I.2    Altman, A.3    Shoseyov, O.4
  • 26
    • 0011470114 scopus 로고    scopus 로고
    • Neuartige Geleinschlußimmobilisate (LentiKats) in der Biotechnologie
    • Jekel M, Buhr A, Willke T, Vorlop K-D (1998) Neuartige Geleinschlußimmobilisate (LentiKats) in der Biotechnologie. Chem lngenieur Technik 70: 438-441.
    • (1998) Chem Lngenieur Technik , vol.70 , pp. 438-441
    • Jekel, M.1    Buhr, A.2    Willke, T.3    Vorlop, K.-D.4
  • 27
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust RB, Waugh DS (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8: 1668-1674.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 28
    • 0026129807 scopus 로고
    • Entrapment of proteins by aggregation within sephadex beads
    • Khare SK, Vaidya S, Gupta MN (1991) Entrapment of proteins by aggregation within sephadex beads. Appl Biochem Biotechnol 27: 205-216.
    • (1991) Appl Biochem Biotechnol , vol.27 , pp. 205-216
    • Khare, S.K.1    Vaidya, S.2    Gupta, M.N.3
  • 30
    • 0037131421 scopus 로고    scopus 로고
    • Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis
    • Kröger N, Lorenz S, Brunner E, Sumper M (2002) Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis. Science 298: 584-586.
    • (2002) Science , vol.298 , pp. 584-586
    • Kröger, N.1    Lorenz, S.2    Brunner, E.3    Sumper, M.4
  • 32
    • 34249867928 scopus 로고    scopus 로고
    • Rapid cross-linking of elastin-like polypeptides with hydroxymethylphosphines in aqueous solution
    • Lim DW, Nettles DL, Setton LA, Chilkoti A (2007) Rapid cross-linking of elastin-like polypeptides with hydroxymethylphosphines in aqueous solution. Biomacromolecules 8: 1463-1470.
    • (2007) Biomacromolecules , vol.8 , pp. 1463-1470
    • Lim, D.W.1    Nettles, D.L.2    Setton, L.A.3    Chilkoti, A.4
  • 34
    • 22944441316 scopus 로고    scopus 로고
    • Co-aggregation of enzymes and polyethyleneimine: A simple method to prepare stable and immobilized derivatives of glutaryl acylase
    • López-Gallego F, Betancor L, Hidalgo A, Alonso N, Fernández-Lafuente R, Guisán JM (2005) Co-aggregation of enzymes and polyethyleneimine: a simple method to prepare stable and immobilized derivatives of glutaryl acylase. Biomacromolecules 6: 1839-1842.
    • (2005) Biomacromolecules , vol.6 , pp. 1839-1842
    • López-Gallego, F.1    Betancor, L.2    Hidalgo, A.3    Alonso, N.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 35
    • 0036671720 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates with enhanced activity: Application to lipases
    • López-Serrano P, Cao L, van Rantwijk F, Sheldon RA (2002) Cross-linked enzyme aggregates with enhanced activity: application to lipases. Biotechnol Lett 24: 1379-1383.
    • (2002) Biotechnol Lett , vol.24 , pp. 1379-1383
    • López-Serrano, P.1    Cao, L.2    van Rantwijk, F.3    Sheldon, R.A.4
  • 36
    • 70449670915 scopus 로고    scopus 로고
    • Mini-review: Biosynthesis of poly(hydroxyalkanoates)
    • Lu J, Tappel RC, Nomura CT (2009) Mini-review: biosynthesis of poly(hydroxyalkanoates). J Macromol Sci C 49: 226-248.
    • (2009) J Macromol Sci C , vol.49 , pp. 226-248
    • Lu, J.1    Tappel, R.C.2    Nomura, C.T.3
  • 38
    • 0033046562 scopus 로고    scopus 로고
    • Metabolic engineering of poly(3-hydroxyalkanoates): From DNA to plastic
    • Madison LL, Huisman GW (1999) Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic. Microbiol Mol Biol Rev 63: 21-53.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 21-53
    • Madison, L.L.1    Huisman, G.W.2
  • 39
    • 0030185060 scopus 로고    scopus 로고
    • Novel crystalline catalysts
    • Margolin AL (1996) Novel crystalline catalysts. Trends Biotechnol 14: 223-230.
    • (1996) Trends Biotechnol , vol.14 , pp. 223-230
    • Margolin, A.L.1
  • 40
    • 66149185690 scopus 로고    scopus 로고
    • Enzyme immobilization via silaffin-mediated autoencapsulation in a biosilica support
    • Marner WD, Shaikh AS, Muller SJ, Keasling JD (2009) Enzyme immobilization via silaffin-mediated autoencapsulation in a biosilica support. Biotechnol Prog 25: 417-423.
    • (2009) Biotechnol Prog , vol.25 , pp. 417-423
    • Marner, W.D.1    Shaikh, A.S.2    Muller, S.J.3    Keasling, J.D.4
  • 42
    • 33644680778 scopus 로고    scopus 로고
    • Synthesis of enantiomerically pure (S)-mandelic acid using an oxynitrilase-nitrilase bienzymatic cascade: A nitrilase surprisingly shows nitrile hydratase activity
    • Mateo C, Chmura A, Rustler S, van Rantwijk F, Stolz A, Sheldon RA (2006) Synthesis of enantiomerically pure (S)-mandelic acid using an oxynitrilase-nitrilase bienzymatic cascade: a nitrilase surprisingly shows nitrile hydratase activity. Tetrahedron 17: 320-323.
    • (2006) Tetrahedron , vol.17 , pp. 320-323
    • Mateo, C.1    Chmura, A.2    Rustler, S.3    van Rantwijk, F.4    Stolz, A.5    Sheldon, R.A.6
  • 43
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • Meyer DE, Chilkoti A (1999) Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol 17: 1112-1115.
    • (1999) Nat Biotechnol , vol.17 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 44
    • 0034878076 scopus 로고    scopus 로고
    • Protein purification by fusion with an environmentally responsive elastin-like polypeptide: Effect of polypeptide length on the purification of thioredoxin
    • Meyer DE, Trabbic-Carlson K, Chilkoti A (2001) Protein purification by fusion with an environmentally responsive elastin-like polypeptide: effect of polypeptide length on the purification of thioredoxin. Biotechnol Prog 17: 720-728.
    • (2001) Biotechnol Prog , vol.17 , pp. 720-728
    • Meyer, D.E.1    Trabbic-Carlson, K.2    Chilkoti, A.3
  • 45
    • 2942558481 scopus 로고    scopus 로고
    • In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF
    • Moldes C, García P, García JL, Prieto MA (2004) In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF. Appl Environ Microbiol 70: 3205-3212.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3205-3212
    • Moldes, C.1    García, P.2    García, J.L.3    Prieto, M.A.4
  • 46
    • 46249091985 scopus 로고    scopus 로고
    • Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to α-d-glucose-1-phosphate
    • Nahálka J (2008) Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to α-d-glucose-1-phosphate. J Ind Microbiol Biotechnol 35: 219-223.
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 219-223
    • Nahálka, J.1
  • 47
    • 34249827218 scopus 로고    scopus 로고
    • Fusion to a pull-down domain: A novel approach of producing Trigonopsis variabilisd-amino acid oxidase as insoluble enzyme aggregates
    • Nahálka J, Nidetzky B (2007) Fusion to a pull-down domain: a novel approach of producing Trigonopsis variabilisd-amino acid oxidase as insoluble enzyme aggregates. Biotechnol Bioeng 97: 454-461.
    • (2007) Biotechnol Bioeng , vol.97 , pp. 454-461
    • Nahálka, J.1    Nidetzky, B.2
  • 48
    • 64549091873 scopus 로고    scopus 로고
    • Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3)
    • Nahálka J, Pätoprstý V (2009) Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3). Org Biomol Chem 7: 1778-1780.
    • (2009) Org Biomol Chem , vol.7 , pp. 1778-1780
    • Nahálka, J.1    Pätoprstý, V.2
  • 49
    • 39649109246 scopus 로고    scopus 로고
    • A cross-linked inclusion body process for sialic acid synthesis
    • Nahálka J, Vikartovská A, Hrabárová E (2008) A cross-linked inclusion body process for sialic acid synthesis. J Biotechnol 134: 146-153.
    • (2008) J Biotechnol , vol.134 , pp. 146-153
    • Nahálka, J.1    Vikartovská, A.2    Hrabárová, E.3
  • 50
    • 70349321704 scopus 로고    scopus 로고
    • Targeting lectin activity into inclusion bodies for the characterisation of glycoproteins
    • Nahálka J, Mislovičová D, Kavcová H (2009) Targeting lectin activity into inclusion bodies for the characterisation of glycoproteins. Mol Biosyst 5: 819-821.
    • (2009) Mol Biosyst , vol.5 , pp. 819-821
    • Nahálka, J.1    Mislovičová, D.2    Kavcová, H.3
  • 51
  • 52
    • 41949101592 scopus 로고    scopus 로고
    • Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules
    • Neumann L, Spinozzi F, Sinibaldi R, Rustichelli F, Pötter M, Steinbüchel A (2008) Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules. J Bacteriol 190: 2911-2919.
    • (2008) J Bacteriol , vol.190 , pp. 2911-2919
    • Neumann, L.1    Spinozzi, F.2    Sinibaldi, R.3    Rustichelli, F.4    Pötter, M.5    Steinbüchel, A.6
  • 53
    • 33644961915 scopus 로고    scopus 로고
    • In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase
    • Peters V, Rehm BHA (2006) In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase. Appl Environ Microbiol 72: 1777-1783.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1777-1783
    • Peters, V.1    Rehm, B.H.A.2
  • 54
    • 77649336358 scopus 로고    scopus 로고
    • Silica immobilization of an enzyme through genetic engineering of the diatom Thalassiosira pseudonana
    • Poulsen N, Berne C, Spain J, Kröger N (2007) Silica immobilization of an enzyme through genetic engineering of the diatom Thalassiosira pseudonana. Angew Chem 119: 1875-1878.
    • (2007) Angew Chem , vol.119 , pp. 1875-1878
    • Poulsen, N.1    Berne, C.2    Spain, J.3    Kröger, N.4
  • 55
    • 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: 833-839.
    • (1964) Pnas , vol.52 , pp. 833-839
    • Quiocho, F.A.1    Richards, F.M.2
  • 56
    • 38649123713 scopus 로고    scopus 로고
    • Studies on crystallization and cross-linking of lipase for biocatalysis
    • Rajan A, Abraham TE (2008) Studies on crystallization and cross-linking of lipase for biocatalysis. Bioprocess Biosyst Eng 31: 87-94.
    • (2008) Bioprocess Biosyst Eng , vol.31 , pp. 87-94
    • Rajan, A.1    Abraham, T.E.2
  • 57
    • 33845728453 scopus 로고    scopus 로고
    • Application of cross-linked enzyme aggregates of Bacillus badius penicillin G acylase for the production of 6-aminopenicillanic acid
    • Rajendhran J, Gunasekaran P (2007) Application of cross-linked enzyme aggregates of Bacillus badius penicillin G acylase for the production of 6-aminopenicillanic acid. Lett Appl Microbiol 44: 43-49.
    • (2007) Lett Appl Microbiol , vol.44 , pp. 43-49
    • Rajendhran, J.1    Gunasekaran, P.2
  • 58
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: Natural catalysts for plastics
    • Rehm BHA (2003) Polyester synthases: natural catalysts for plastics. Biochem J 376: 15-33.
    • (2003) Biochem J , vol.376 , pp. 15-33
    • Rehm, B.H.A.1
  • 59
    • 29744460087 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme crystals of laccase
    • Roy JJ, Abraham TE (2006) Preparation and characterization of cross-linked enzyme crystals of laccase. J Mol Catal B 38: 31-36.
    • (2006) J Mol Catal B , vol.38 , pp. 31-36
    • Roy, J.J.1    Abraham, T.E.2
  • 60
    • 34548792373 scopus 로고    scopus 로고
    • Novel biocatalysts based on S-layer self-assembly of Geobacillus stearothermophilus NRS 2004/3a: A nanobiotechnological approach
    • Schäffer C, Novotny R, Küpcü S, Zayni S, Scheberl A, Friedmann J, Sleytr UB, Messner P (2007) Novel biocatalysts based on S-layer self-assembly of Geobacillus stearothermophilus NRS 2004/3a: a nanobiotechnological approach. Small 3: 1549-1559.
    • (2007) Small , vol.3 , pp. 1549-1559
    • Schäffer, C.1    Novotny, R.2    Küpcü, S.3    Zayni, S.4    Scheberl, A.5    Friedmann, J.6    Sleytr, U.B.7    Messner, P.8
  • 62
  • 63
    • 67650825702 scopus 로고    scopus 로고
    • Enzymatic synthesis of β-glucosylglycerol using a continuous-flow microreactor containing thermostable β-glycoside hydrolase CelB immobilized on coated microchannel walls
    • Schwarz A, Thomsen MS, Nidetzky B (2009) Enzymatic synthesis of β-glucosylglycerol using a continuous-flow microreactor containing thermostable β-glycoside hydrolase CelB immobilized on coated microchannel walls. Biotechnol Bioeng 103: 865-872.
    • (2009) Biotechnol Bioeng , vol.103 , pp. 865-872
    • Schwarz, A.1    Thomsen, M.S.2    Nidetzky, B.3
  • 64
    • 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: 207-213.
    • (2006) Anal Biochem , vol.351 , pp. 207-213
    • Shah, S.1    Sharma, A.2    Gupta, M.N.3
  • 65
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: The quest for optimum performance
    • Sheldon RA (2007a) Enzyme immobilization: the quest for optimum performance. Adv Synth Catal 349: 1289-1307.
    • (2007) Adv Synth Catal , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 66
    • 37749006119 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs): Stable and recyclable biocatalysts
    • Sheldon RA (2007b) Cross-linked enzyme aggregates (CLEAs): stable and recyclable biocatalysts. Biochem Soc Trans 35: 1583-1587.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1583-1587
    • Sheldon, R.A.1
  • 70
    • 64549089736 scopus 로고    scopus 로고
    • Coated-wall microreactor for continuous biocatalytic transformations using immobilized enzymes
    • Thomsen MS, Nidetzky B (2009) Coated-wall microreactor for continuous biocatalytic transformations using immobilized enzymes. Biotechnol J 4: 98-107.
    • (2009) Biotechnol J , vol.4 , pp. 98-107
    • Thomsen, M.S.1    Nidetzky, B.2
  • 71
    • 37349026887 scopus 로고    scopus 로고
    • Exploitation of the S-layer self-assembly system for site directed immobilization of enzymes demonstrated for an extremophilic laminarinase from Pyrococcus furiosus
    • Tschiggerl H, Breitwieser A, de Roo G, Verwoerd T, Schäffer C, Sleytr UB (2008) Exploitation of the S-layer self-assembly system for site directed immobilization of enzymes demonstrated for an extremophilic laminarinase from Pyrococcus furiosus. J Biotechnol 133: 403-411.
    • (2008) J Biotechnol , vol.133 , pp. 403-411
    • Tschiggerl, H.1    Breitwieser, A.2    de Roo, G.3    Verwoerd, T.4    Schäffer, C.5    Sleytr, U.B.6
  • 72
    • 44649151272 scopus 로고    scopus 로고
    • Preparation of multipurpose cross-linked enzyme aggregates and their application to production of alkyl ferulates
    • Vafiadi C, Topakas E, Christakopoulos P (2008) Preparation of multipurpose cross-linked enzyme aggregates and their application to production of alkyl ferulates. J Mol Catal B 54: 35-41.
    • (2008) J Mol Catal B , vol.54 , pp. 35-41
    • Vafiadi, C.1    Topakas, E.2    Christakopoulos, P.3
  • 73
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: Biological role of inclusion bodies
    • Villaverde A, Carrió MM (2003) Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 25: 1385-1395.
    • (2003) Biotechnol Lett , vol.25 , pp. 1385-1395
    • Villaverde, A.1    Carrió, M.M.2
  • 74
    • 0036773161 scopus 로고    scopus 로고
    • Characterization of SP1, a stress-responsive, boiling-soluble, homo-oligomeric protein from aspen
    • Wang W-X, Pelah D, Alergand T, Shoseyov O, Altman A (2002) Characterization of SP1, a stress-responsive, boiling-soluble, homo-oligomeric protein from aspen. Plant Physiol 130: 865-875.
    • (2002) Plant Physiol , vol.130 , pp. 865-875
    • Wang, W.-X.1    Pelah, D.2    Alergand, T.3    Shoseyov, O.4    Altman, A.5
  • 75
    • 33748418721 scopus 로고    scopus 로고
    • Aspen SP1, an exceptional thermal, protease and detergent-resistant self-assembled nano-particle
    • Wang W, Dgany O, Wolf SG, Levy I, Algom R, Pouny Y et al (2006) Aspen SP1, an exceptional thermal, protease and detergent-resistant self-assembled nano-particle. Biotechnol Bioeng 95: 161-168.
    • (2006) Biotechnol Bioeng , vol.95 , pp. 161-168
    • Wang, W.1    Dgany, O.2    Wolf, S.G.3    Levy, I.4    Algom, R.5    Pouny, Y.6
  • 76
    • 2542492110 scopus 로고    scopus 로고
    • Encapsulation of cross-linked penicillin G acylase aggregates in lentikats: Evaluation of a novel biocatalyst in organic media
    • Wilson L, Illanes A, Pessela BCC, Abian O, Fernández-Lafuente R, Guisán JM (2004) Encapsulation of cross-linked penicillin G acylase aggregates in lentikats: evaluation of a novel biocatalyst in organic media. Biotechnol Bioeng 86(5): 558-562.
    • (2004) Biotechnol Bioeng , vol.86 , Issue.5 , pp. 558-562
    • Wilson, L.1    Illanes, A.2    Pessela, B.C.C.3    Abian, O.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 77
    • 33751100404 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs) with controlled particles: Application to Candida rugosa lipase
    • Yu HW, Chen H, Wang X, Yang YY, Ching CB (2006) Cross-linked enzyme aggregates (CLEAs) with controlled particles: application to Candida rugosa lipase. J Mol Catal B 43: 124-127.
    • (2006) J Mol Catal B , vol.43 , pp. 124-127
    • Yu, H.W.1    Chen, H.2    Wang, X.3    Yang, Y.Y.4    Ching, C.B.5
  • 78
    • 44649189336 scopus 로고    scopus 로고
    • Resolution of N-(2-ethyl-6-methylphenyl) alanine via cross-linked aggregates of Pseudomonas sp. lipase
    • Zhao L, Zheng L, Gao G, Jia F, Cao S (2008) Resolution of N-(2-ethyl-6-methylphenyl) alanine via cross-linked aggregates of Pseudomonas sp. lipase. J Mol Catal B 54: 7-12.
    • (2008) J Mol Catal B , vol.54 , pp. 7-12
    • Zhao, L.1    Zheng, L.2    Gao, G.3    Jia, F.4    Cao, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.