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Volumn 365, Issue 1-2, 2010, Pages 59-67

Effect of enzyme location on activity and stability of trypsin and urease immobilized on porous membranes by using layer-by-layer self-assembly of polyelectrolyte

Author keywords

Catalytic membrane; Enzyme immobilization; Layer by layer self assembly; Polyelectrolyte

Indexed keywords

ASSEMBLY TECHNIQUES; CATALYTIC ACTIVITY; CATALYTIC MEMBRANE; ENZYME LAYERS; IMMOBILIZED ENZYME; LAYER BY LAYER SELF ASSEMBLY; MEMBRANE PORE SIZE; MEMBRANE SURFACE; OUTER LAYER; POROUS MEMBRANES; SANDWICHED LAYERS;

EID: 78049295053     PISSN: 03767388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.memsci.2010.08.042     Document Type: Article
Times cited : (51)

References (40)
  • 2
    • 5744235228 scopus 로고
    • Trypsinogens and trypsins of various species
    • Walsh K.A. Trypsinogens and trypsins of various species. Method Enzymol. 1970, 19:41-63.
    • (1970) Method Enzymol. , vol.19 , pp. 41-63
    • Walsh, K.A.1
  • 3
    • 0029900109 scopus 로고    scopus 로고
    • Trypsin immobilization on shrimp chitin with formaldehyde and its application to continuous hydrolysis of casein
    • Ge S.J., Bai H., Zhang L.X. Trypsin immobilization on shrimp chitin with formaldehyde and its application to continuous hydrolysis of casein. Biotechnol. Appl. Biochem. 1996, 24:1-6.
    • (1996) Biotechnol. Appl. Biochem. , vol.24 , pp. 1-6
    • Ge, S.J.1    Bai, H.2    Zhang, L.X.3
  • 5
    • 64649100132 scopus 로고    scopus 로고
    • Functional, catalytic and kinetic properties: a review
    • Krajewska B., Ureases I. Functional, catalytic and kinetic properties: a review. J. Mol. Catal. B: Enzym. 2009, 59:9-21.
    • (2009) J. Mol. Catal. B: Enzym. , vol.59 , pp. 9-21
    • Krajewska, B.1    Ureases, I.2
  • 6
    • 0036770811 scopus 로고    scopus 로고
    • Surface modification and blood compatibility of polyacrylonitrile membrane with immobilized chitosan-heparin conjugate
    • Yang M.C., Lin W.C. Surface modification and blood compatibility of polyacrylonitrile membrane with immobilized chitosan-heparin conjugate. J. Polym. Res. 2002, 9:201-206.
    • (2002) J. Polym. Res. , vol.9 , pp. 201-206
    • Yang, M.C.1    Lin, W.C.2
  • 7
    • 34548508705 scopus 로고    scopus 로고
    • Surface engineerings of polyacrylonitrile-based asymmetric membranes towards biomedical applications: an overview
    • Wang Z.-G., Wan L.-S., Xu Z.-K. Surface engineerings of polyacrylonitrile-based asymmetric membranes towards biomedical applications: an overview. J. Membr. Sci. 2007, 304:8-23.
    • (2007) J. Membr. Sci. , vol.304 , pp. 8-23
    • Wang, Z.-G.1    Wan, L.-S.2    Xu, Z.-K.3
  • 8
    • 0000092384 scopus 로고
    • Buildup of ultrathin multilayer films by a self-assembly process. I. Consecutive adsorption of anionic and cationc bipolar amphiphiles and polyelectrolytes on charged surfaces
    • Decher G., Hong J.D. Buildup of ultrathin multilayer films by a self-assembly process. I. Consecutive adsorption of anionic and cationc bipolar amphiphiles and polyelectrolytes on charged surfaces. Ber. Buns. Phys. Chem. 1991, 95:1430-1434.
    • (1991) Ber. Buns. Phys. Chem. , vol.95 , pp. 1430-1434
    • Decher, G.1    Hong, J.D.2
  • 9
    • 32644489486 scopus 로고    scopus 로고
    • Multilayer membranes for glucose biosensing via layer-by-layer assembly of multiwall carbon nanotubes and glucose oxidase
    • Zhao H., Ju H. Multilayer membranes for glucose biosensing via layer-by-layer assembly of multiwall carbon nanotubes and glucose oxidase. Anal. Biochem. 2006, 350:138-144.
    • (2006) Anal. Biochem. , vol.350 , pp. 138-144
    • Zhao, H.1    Ju, H.2
  • 11
    • 0034620344 scopus 로고    scopus 로고
    • In situ determination of the structural properties of initially deposited polyelectrolyte multilayers
    • Ladam G., Schaad P., Voegel J.-C., Schaaf P., Decher G., Cuisinier F. In situ determination of the structural properties of initially deposited polyelectrolyte multilayers. Langmuir 2000, 16:1249-1255.
    • (2000) Langmuir , vol.16 , pp. 1249-1255
    • Ladam, G.1    Schaad, P.2    Voegel, J.-C.3    Schaaf, P.4    Decher, G.5    Cuisinier, F.6
  • 12
    • 0035148750 scopus 로고    scopus 로고
    • Encapsulation of proteins by layer-by-layer adsorption of polyelectrolytes onto protein aggregates: factors regulating the protein release
    • Balabushevitch N.G., Sukhorukov G.B., Moroz N.A., Volodkin D.V., Larionova N.I., Donath E., Moehwald H. Encapsulation of proteins by layer-by-layer adsorption of polyelectrolytes onto protein aggregates: factors regulating the protein release. Biotechnol. Bioeng. 2001, 76:207-213.
    • (2001) Biotechnol. Bioeng. , vol.76 , pp. 207-213
    • Balabushevitch, N.G.1    Sukhorukov, G.B.2    Moroz, N.A.3    Volodkin, D.V.4    Larionova, N.I.5    Donath, E.6    Moehwald, H.7
  • 13
    • 33749508442 scopus 로고    scopus 로고
    • A strategy for enzyme immobilization on layer-by-layer dendrimer-gold nanoparticle electrocatalytic membrane incorporating redox mediator
    • Crespilho F.N., Ghica M.E., Florescu M., Nart F.C., Oliveira O.N., Brett C.M.A. A strategy for enzyme immobilization on layer-by-layer dendrimer-gold nanoparticle electrocatalytic membrane incorporating redox mediator. Electrochem. Commun. 2006, 8:1665-1670.
    • (2006) Electrochem. Commun. , vol.8 , pp. 1665-1670
    • Crespilho, F.N.1    Ghica, M.E.2    Florescu, M.3    Nart, F.C.4    Oliveira, O.N.5    Brett, C.M.A.6
  • 15
    • 38449088049 scopus 로고    scopus 로고
    • Activity of immobilized trypsin in layer structure of polyelectrolyte microcapsules (PEMC)
    • Garbers E., Mitlöhner R., Georgieva R., Baümler H. Activity of immobilized trypsin in layer structure of polyelectrolyte microcapsules (PEMC). Macomol. Biosci. 2007, 7:1243-1249.
    • (2007) Macomol. Biosci. , vol.7 , pp. 1243-1249
    • Garbers, E.1    Mitlöhner, R.2    Georgieva, R.3    Baümler, H.4
  • 16
    • 0037359867 scopus 로고    scopus 로고
    • Simple method for immobilization of biomacromolecules onto membranes of different types
    • Nguyen Q.T., Ping Z., Nguyen T., Rigal P. Simple method for immobilization of biomacromolecules onto membranes of different types. J. Membr. Sci. 2003, 213:85-95.
    • (2003) J. Membr. Sci. , vol.213 , pp. 85-95
    • Nguyen, Q.T.1    Ping, Z.2    Nguyen, T.3    Rigal, P.4
  • 17
    • 33846159089 scopus 로고    scopus 로고
    • Layer-by-layer-assembled microfiltration membranes for biomolecule immobilization and enzymatic catalysis
    • Smuleac V., Butterfield D.A., Bhattacharyya D. Layer-by-layer-assembled microfiltration membranes for biomolecule immobilization and enzymatic catalysis. Langmuir 2006, 22:10118-10124.
    • (2006) Langmuir , vol.22 , pp. 10118-10124
    • Smuleac, V.1    Butterfield, D.A.2    Bhattacharyya, D.3
  • 18
    • 49149149668 scopus 로고    scopus 로고
    • Functionalized membranes by layer-by-layer assembly of polyelectrolytes and in situ polymerization of acrylic acid for applications in enzymatic catalysis
    • Datta S., Cecil C., Bhattacharyya D. Functionalized membranes by layer-by-layer assembly of polyelectrolytes and in situ polymerization of acrylic acid for applications in enzymatic catalysis. Ind. Eng. Chem. Res. 2008, 47:4586-4597.
    • (2008) Ind. Eng. Chem. Res. , vol.47 , pp. 4586-4597
    • Datta, S.1    Cecil, C.2    Bhattacharyya, D.3
  • 19
    • 8344281999 scopus 로고    scopus 로고
    • Macroporous zeolitic membrane bioreactors
    • Wang Y., Caruso F. Macroporous zeolitic membrane bioreactors. Adv. Funct. Mater. 2004, 14:1012-1018.
    • (2004) Adv. Funct. Mater. , vol.14 , pp. 1012-1018
    • Wang, Y.1    Caruso, F.2
  • 20
    • 11844276552 scopus 로고    scopus 로고
    • Enzyme multilayer-modified porous membranes as biocatalysts
    • Yu A., Liang Z., Caruso F. Enzyme multilayer-modified porous membranes as biocatalysts. Chem. Mater. 2005, 17:171-175.
    • (2005) Chem. Mater. , vol.17 , pp. 171-175
    • Yu, A.1    Liang, Z.2    Caruso, F.3
  • 22
    • 0043264252 scopus 로고    scopus 로고
    • Two-Step sequential reaction catalyzed by layer-by-layer assembled urease and arginase multilayers
    • Disawal S., Qiu J., Elmore B.B., Lvov Y.M. Two-Step sequential reaction catalyzed by layer-by-layer assembled urease and arginase multilayers. Colloids Surf. B 2003, 32:145-156.
    • (2003) Colloids Surf. B , vol.32 , pp. 145-156
    • Disawal, S.1    Qiu, J.2    Elmore, B.B.3    Lvov, Y.M.4
  • 23
    • 64649100726 scopus 로고    scopus 로고
    • Ureases. II. Properties and their customizing by enzyme immobilizations: a review
    • Krajewska B. Ureases. II. Properties and their customizing by enzyme immobilizations: a review. J. Mol. Catal. B: Enzym. 2009, 59:22-40.
    • (2009) J. Mol. Catal. B: Enzym. , vol.59 , pp. 22-40
    • Krajewska, B.1
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0037401217 scopus 로고    scopus 로고
    • Adsorption of lysozyme on a hemodialysis sulfonated polyacrylonitrile membrane, with and without preadsorbed poly(ethyleneimine) on the external faces
    • Ethève J., Déjardin P., Boissière M. Adsorption of lysozyme on a hemodialysis sulfonated polyacrylonitrile membrane, with and without preadsorbed poly(ethyleneimine) on the external faces. Colloids Surf. B 2003, 28:285-293.
    • (2003) Colloids Surf. B , vol.28 , pp. 285-293
    • Ethève, J.1    Déjardin, P.2    Boissière, M.3
  • 26
    • 33947352794 scopus 로고
    • The isoelectric point of crystalline urease
    • Sumner J.B., Hand D.B. The isoelectric point of crystalline urease. J. Am. Chem. Soc. 1929, 51:1255-1260.
    • (1929) J. Am. Chem. Soc. , vol.51 , pp. 1255-1260
    • Sumner, J.B.1    Hand, D.B.2
  • 27
    • 85004630723 scopus 로고
    • Automated enzyme analysis by high-perfomance liquid chromatography postcolumn substrate reaction: application to trypsin and chymotrypsin
    • Edani M., Imai H. Automated enzyme analysis by high-perfomance liquid chromatography postcolumn substrate reaction: application to trypsin and chymotrypsin. Anal. Sci. 1993, 9:15-17.
    • (1993) Anal. Sci. , vol.9 , pp. 15-17
    • Edani, M.1    Imai, H.2
  • 28
    • 0014936037 scopus 로고
    • An effect of calcium ions on the activity, heat stability, and structure of trypsin
    • Sipos T., Merkel J.R. An effect of calcium ions on the activity, heat stability, and structure of trypsin. Biochemistry 1970, 9:2766.
    • (1970) Biochemistry , vol.9 , pp. 2766
    • Sipos, T.1    Merkel, J.R.2
  • 29
    • 33947332625 scopus 로고
    • Phenol-hypochlorite reaction for determination of ammonia
    • Weatherburn M.W. Phenol-hypochlorite reaction for determination of ammonia. Anal. Chem. 1967, 39:971-974.
    • (1967) Anal. Chem. , vol.39 , pp. 971-974
    • Weatherburn, M.W.1
  • 30
    • 0024288267 scopus 로고
    • The structure of jack bean urease - the complete amino-acid sequence, limited proteolysis and reactive cysteine residues
    • Takishima K., Suga T., Mamiya G. The structure of jack bean urease - the complete amino-acid sequence, limited proteolysis and reactive cysteine residues. Eur. J. Biochem. 1988, 175:151-165.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 151-165
    • Takishima, K.1    Suga, T.2    Mamiya, G.3
  • 32
    • 33947102664 scopus 로고    scopus 로고
    • Adsorption of trypsin on hydrophilic and hydrophobic surfaces
    • Koutsopoulos S., Patzsch K., Bosker W.T.E., Norde W. Adsorption of trypsin on hydrophilic and hydrophobic surfaces. Langmuir 2007, 23:2000-2006.
    • (2007) Langmuir , vol.23 , pp. 2000-2006
    • Koutsopoulos, S.1    Patzsch, K.2    Bosker, W.T.E.3    Norde, W.4
  • 33
    • 38749096663 scopus 로고    scopus 로고
    • Adsorption of urease on PE-MCM-41 and its catalytic effect on hydrolysis of urea
    • Hossain K., Monreal C.M., Sayari A. Adsorption of urease on PE-MCM-41 and its catalytic effect on hydrolysis of urea. Colloids Surf. B 2008, 62:42-50.
    • (2008) Colloids Surf. B , vol.62 , pp. 42-50
    • Hossain, K.1    Monreal, C.M.2    Sayari, A.3
  • 34
    • 1842843755 scopus 로고    scopus 로고
    • Change of the performance properties of nanofiltration cellulose acetate membranes by surface adsorption of polyelectrolyte multilayers
    • Hadj Lajimi R., Ben Abdallah A., Ferjani E., Roudesli M.S., Deratani A. Change of the performance properties of nanofiltration cellulose acetate membranes by surface adsorption of polyelectrolyte multilayers. Desalination 2004, 163:193-202.
    • (2004) Desalination , vol.163 , pp. 193-202
    • Hadj Lajimi, R.1    Ben Abdallah, A.2    Ferjani, E.3    Roudesli, M.S.4    Deratani, A.5
  • 37
    • 0033521508 scopus 로고    scopus 로고
    • The effect of phosphate buffer in the range of pH 5.80-8.07 on jack bean urease activity
    • Krajewska B., Zaborska W. The effect of phosphate buffer in the range of pH 5.80-8.07 on jack bean urease activity. J. Mol. Catal. B: Enzym. 1999, 6:75-81.
    • (1999) J. Mol. Catal. B: Enzym. , vol.6 , pp. 75-81
    • Krajewska, B.1    Zaborska, W.2
  • 40
    • 15744368372 scopus 로고    scopus 로고
    • Preparation and characterization of trypsin immobilized on silica gel supported macroporous chitosan bead
    • Xi F., Wu J., Jia Z., Lin X. Preparation and characterization of trypsin immobilized on silica gel supported macroporous chitosan bead. Process Biochem. 2005, 40:2833-2840.
    • (2005) Process Biochem. , vol.40 , pp. 2833-2840
    • Xi, F.1    Wu, J.2    Jia, Z.3    Lin, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.