메뉴 건너뛰기




Volumn 90, Issue , 2014, Pages 170-177

Direct affinity immobilization of recombinant heparinase I fused to maltose binding protein on maltose-coated magnetic nanoparticles

Author keywords

Adsorption; Affinity; Enzyme biocatalysis; Heparinase I; Immobilization; Magnetic nanoparticles

Indexed keywords

ADSORPTION; BIOSYNTHESIS; ENZYME IMMOBILIZATION; MALTOSE; MOLECULAR WEIGHT DISTRIBUTION; NANOMAGNETICS; POLYETHYLENE OXIDES; POLYSACCHARIDES; RADIOACTIVE WASTE VITRIFICATION; RECOMBINANT PROTEINS; REUSABILITY;

EID: 84903139918     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2014.05.021     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 0004117876 scopus 로고    scopus 로고
    • Immobilized biocatalysts
    • Marcel Dekker Inc., New York
    • Blanch H.W., Clark D.S. Immobilized biocatalysts. Biochemical Engineering 1996, 103-161. Marcel Dekker Inc., New York.
    • (1996) Biochemical Engineering , pp. 103-161
    • Blanch, H.W.1    Clark, D.S.2
  • 2
    • 66149185690 scopus 로고    scopus 로고
    • Enzyme immobilization via silaffin-mediated autoencapsulation in a biosilica support
    • Marner W.D., Shaikh A.S., Muller S.J., Keasling J.D. Enzyme immobilization via silaffin-mediated autoencapsulation in a biosilica support. Biotechnol. Prog. 2009, 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
  • 3
    • 59349097393 scopus 로고    scopus 로고
    • A molecularly imprinted polymer-coated nanocomposite of magnetic nanoparticles for estrone recognition
    • Wang X., Wang L., He X., Zhang Y., Chen L. A molecularly imprinted polymer-coated nanocomposite of magnetic nanoparticles for estrone recognition. Talanta 2009, 78:327-332.
    • (2009) Talanta , vol.78 , pp. 327-332
    • Wang, X.1    Wang, L.2    He, X.3    Zhang, Y.4    Chen, L.5
  • 4
    • 70349089061 scopus 로고    scopus 로고
    • Recyclable nanobiocatalyst for enantioselective sulfoxidation: facile fabrication and high performance of chloroperoxidase-coated magnetic nanoparticles with iron oxide core and polymer shell
    • Wang W., Xu Y., Wang D.I., Li Z. Recyclable nanobiocatalyst for enantioselective sulfoxidation: facile fabrication and high performance of chloroperoxidase-coated magnetic nanoparticles with iron oxide core and polymer shell. J. Am. Chem. Soc. 2009, 131:12892-12893.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12892-12893
    • Wang, W.1    Xu, Y.2    Wang, D.I.3    Li, Z.4
  • 5
    • 78349261260 scopus 로고    scopus 로고
    • Bifunctional nanocomposites with magnetic and luminescence properties
    • Vollath D. Bifunctional nanocomposites with magnetic and luminescence properties. Adv. Mater. 2010, 22:4410-4415.
    • (2010) Adv. Mater. , vol.22 , pp. 4410-4415
    • Vollath, D.1
  • 6
    • 66149156506 scopus 로고    scopus 로고
    • Synthesis of core/shell colloidal magnetic zeolite microspheres for the immobilization of trypsin
    • Deng Y.H., Deng C.H., Qi D.W., Liu C., Liu J., Zhang X.M., Zhao D.Y. Synthesis of core/shell colloidal magnetic zeolite microspheres for the immobilization of trypsin. Adv. Mater. 2009, 21:1377-1382.
    • (2009) Adv. Mater. , vol.21 , pp. 1377-1382
    • Deng, Y.H.1    Deng, C.H.2    Qi, D.W.3    Liu, C.4    Liu, J.5    Zhang, X.M.6    Zhao, D.Y.7
  • 7
    • 67649873312 scopus 로고    scopus 로고
    • 4-silica-NiO superstructures and their application as magnetically separable high-performance biocatalysts
    • 4-silica-NiO superstructures and their application as magnetically separable high-performance biocatalysts. Chem. Commun. 2009, (25):3641-3812.
    • (2009) Chem. Commun. , Issue.25 , pp. 3641-3812
    • Lee, K.S.1    Woo, M.H.2    Kim, H.S.3    Lee, E.Y.4    Lee, I.S.5
  • 9
    • 84860000296 scopus 로고    scopus 로고
    • Reversible clustering of magnetic nanobiocatalysts for high-performance biocatalysis and easy catalyst recycling
    • Ngo T.P., Zhang W., Wang W., Li Z. Reversible clustering of magnetic nanobiocatalysts for high-performance biocatalysis and easy catalyst recycling. Chem. Commun. (Camb.) 2012, 48:4585-4587.
    • (2012) Chem. Commun. (Camb.) , vol.48 , pp. 4585-4587
    • Ngo, T.P.1    Zhang, W.2    Wang, W.3    Li, Z.4
  • 10
    • 47249140441 scopus 로고    scopus 로고
    • Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications
    • Laurent S., Forge D., Port M., Roch A., Robic C., Vander Elst L., Muller R.N. Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem. Rev. 2008, 108:2064-2110.
    • (2008) Chem. Rev. , vol.108 , pp. 2064-2110
    • Laurent, S.1    Forge, D.2    Port, M.3    Roch, A.4    Robic, C.5    Vander Elst, L.6    Muller, R.N.7
  • 11
    • 77955202927 scopus 로고    scopus 로고
    • Synthesis, functionalization, and biomedical applications of multifunctional magnetic nanoparticles
    • Hao R., Xing R., Xu Z., Hou Y., Gao S., Sun S. Synthesis, functionalization, and biomedical applications of multifunctional magnetic nanoparticles. Adv. Mater. 2010, 22:2729-2742.
    • (2010) Adv. Mater. , vol.22 , pp. 2729-2742
    • Hao, R.1    Xing, R.2    Xu, Z.3    Hou, Y.4    Gao, S.5    Sun, S.6
  • 12
    • 79959873908 scopus 로고    scopus 로고
    • Facile fabrication of recyclable and active nanobiocatalyst: purification and immobilization of enzyme in one pot with Ni-NTA functionalized magnetic nanoparticle
    • Wang W., Wang D.I.C., Li Z. Facile fabrication of recyclable and active nanobiocatalyst: purification and immobilization of enzyme in one pot with Ni-NTA functionalized magnetic nanoparticle. Chem. Commun. 2011, 47:8115-8117.
    • (2011) Chem. Commun. , vol.47 , pp. 8115-8117
    • Wang, W.1    Wang, D.I.C.2    Li, Z.3
  • 13
    • 79952275321 scopus 로고    scopus 로고
    • Beta-cyclodextrin-modified hybrid magnetic nanoparticles for catalysis and adsorption
    • Kang Y., Zhou L.L., Li X., Yuan J.Y. Beta-cyclodextrin-modified hybrid magnetic nanoparticles for catalysis and adsorption. J. Mater. Chem. 2011, 21:3704-3710.
    • (2011) J. Mater. Chem. , vol.21 , pp. 3704-3710
    • Kang, Y.1    Zhou, L.L.2    Li, X.3    Yuan, J.Y.4
  • 14
    • 79951594762 scopus 로고    scopus 로고
    • Core-shell structural iron oxide hybrid nanoparticles: from controlled synthesis to biomedical applications
    • Zhou L.L., Yuan J.Y., Wei Y. Core-shell structural iron oxide hybrid nanoparticles: from controlled synthesis to biomedical applications. J. Mater. Chem. 2011, 21:2823-2840.
    • (2011) J. Mater. Chem. , vol.21 , pp. 2823-2840
    • Zhou, L.L.1    Yuan, J.Y.2    Wei, Y.3
  • 15
    • 84863360020 scopus 로고    scopus 로고
    • Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes
    • Zhou L.L., Wu J.J., Zhang H.J., Kang Y., Guo J., Zhang C., Yuan J.Y., Xing X.H. Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes. J. Mater. Chem. 2012, 22:6813-6818.
    • (2012) J. Mater. Chem. , vol.22 , pp. 6813-6818
    • Zhou, L.L.1    Wu, J.J.2    Zhang, H.J.3    Kang, Y.4    Guo, J.5    Zhang, C.6    Yuan, J.Y.7    Xing, X.H.8
  • 16
    • 0021920714 scopus 로고
    • Purification and characterization of heparinase from Flavobacterium heparinum
    • Yang V.C., Linhardt R.J., Bernstein H., Cooney C.L., Langer R. Purification and characterization of heparinase from Flavobacterium heparinum. J. Biol. Chem. 1985, 260:1849-1857.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1849-1857
    • Yang, V.C.1    Linhardt, R.J.2    Bernstein, H.3    Cooney, C.L.4    Langer, R.5
  • 19
    • 57849153892 scopus 로고    scopus 로고
    • Advances in the separation, sensitive detection, and characterization of heparin and heparan sulfate
    • Korir A.K., Larive C.K. Advances in the separation, sensitive detection, and characterization of heparin and heparan sulfate. Anal. Bioanal. Chem. 2009, 393:155-169.
    • (2009) Anal. Bioanal. Chem. , vol.393 , pp. 155-169
    • Korir, A.K.1    Larive, C.K.2
  • 21
    • 0033525396 scopus 로고    scopus 로고
    • Investigation of a whole blood fluidized bed Taylor-Couette flow device for enzymatic heparin neutralization
    • Ameer G.A., Harmon W., Sasisekharan R., Langer R. Investigation of a whole blood fluidized bed Taylor-Couette flow device for enzymatic heparin neutralization. Biotechnol. Bioeng. 1999, 62:602-608.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 602-608
    • Ameer, G.A.1    Harmon, W.2    Sasisekharan, R.3    Langer, R.4
  • 22
    • 0028855668 scopus 로고
    • Preparation and structural characterization of large heparin-derived oligosaccharides
    • Pervin A., Gallo C., Jandik K.A., Han X.J., Linhardt R.J. Preparation and structural characterization of large heparin-derived oligosaccharides. Glycobiology 1995, 5:83-95.
    • (1995) Glycobiology , vol.5 , pp. 83-95
    • Pervin, A.1    Gallo, C.2    Jandik, K.A.3    Han, X.J.4    Linhardt, R.J.5
  • 25
    • 67749130626 scopus 로고    scopus 로고
    • Characteristics of low molecular weight heparin production by an ultrafiltration membrane bioreactor using maltose binding protein fused heparinase I
    • Ye F.C., Kuang Y., Chen S., Zhang C., Chen Y., Xing X.H. Characteristics of low molecular weight heparin production by an ultrafiltration membrane bioreactor using maltose binding protein fused heparinase I. Biochem. Eng. J. 2009, 46:193-198.
    • (2009) Biochem. Eng. J. , vol.46 , pp. 193-198
    • Ye, F.C.1    Kuang, Y.2    Chen, S.3    Zhang, C.4    Chen, Y.5    Xing, X.H.6
  • 26
    • 84886051954 scopus 로고    scopus 로고
    • Controllable production of low molecular weight heparins by combinations of heparinase I/II/III
    • Wu J., Zhang C., Mei X., Li Y., Xing X.H. Controllable production of low molecular weight heparins by combinations of heparinase I/II/III. Carbohydr. Polym. 2014, 101:484-492.
    • (2014) Carbohydr. Polym. , vol.101 , pp. 484-492
    • Wu, J.1    Zhang, C.2    Mei, X.3    Li, Y.4    Xing, X.H.5
  • 28
    • 0029876949 scopus 로고    scopus 로고
    • Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum
    • Ernst S., Venkataraman G., Winkler S., Godavarti R., Langer R., Cooney C.L., Sasisekharan R. Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum. Biochem. J. 1996, 315:589-597.
    • (1996) Biochem. J. , vol.315 , pp. 589-597
    • Ernst, S.1    Venkataraman, G.2    Winkler, S.3    Godavarti, R.4    Langer, R.5    Cooney, C.L.6    Sasisekharan, R.7
  • 29
    • 1842339902 scopus 로고    scopus 로고
    • Process simulation for recombinant protein production: cost estimation and sensitivity analysis for heparinase I expressed in Escherichia coli
    • Ernst S., Garro O.A., Winkler S., Venkataraman G., Langer R., Cooney C.L., Sasisekharan R. Process simulation for recombinant protein production: cost estimation and sensitivity analysis for heparinase I expressed in Escherichia coli. Biotechnol. Bioeng. 1997, 53:575-582.
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 575-582
    • Ernst, S.1    Garro, O.A.2    Winkler, S.3    Venkataraman, G.4    Langer, R.5    Cooney, C.L.6    Sasisekharan, R.7
  • 30
    • 13244268462 scopus 로고    scopus 로고
    • Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein
    • Chen Y., Xing X.H., Lou K. Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein. Biochem. Eng. J. 2005, 23:155-159.
    • (2005) Biochem. Eng. J. , vol.23 , pp. 155-159
    • Chen, Y.1    Xing, X.H.2    Lou, K.3
  • 31
    • 33947305443 scopus 로고    scopus 로고
    • Production of MBP-HepA fusion protein in recombinant Escherichia coli by optimization of culture medium
    • Chen Y., Xing X.H., Ye F.C., Kuang Y., Luo M.F. Production of MBP-HepA fusion protein in recombinant Escherichia coli by optimization of culture medium. Biochem. Eng. J. 2007, 34:114-121.
    • (2007) Biochem. Eng. J. , vol.34 , pp. 114-121
    • Chen, Y.1    Xing, X.H.2    Ye, F.C.3    Kuang, Y.4    Luo, M.F.5
  • 32
    • 84876683143 scopus 로고    scopus 로고
    • Combination of site-directed mutagenesis and calcium ion addition for enhanced production of thermostable MBP-fused heparinase I in recombinant Escherichia coli
    • Chen S., Huang Z.L., Wu J.J., Chen Y., Ye F.C., Zhang C., Yatsunami R., Nakamura S., Xing X.H. Combination of site-directed mutagenesis and calcium ion addition for enhanced production of thermostable MBP-fused heparinase I in recombinant Escherichia coli. Appl. Microbiol. Biotechnol. 2013, 97:2907-2916.
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 2907-2916
    • Chen, S.1    Huang, Z.L.2    Wu, J.J.3    Chen, Y.4    Ye, F.C.5    Zhang, C.6    Yatsunami, R.7    Nakamura, S.8    Xing, X.H.9
  • 33
    • 33750633211 scopus 로고    scopus 로고
    • Production of heparin oligosaccharides by fusion protein of MBP-heparinase I and the enzyme thermostability
    • Ying K.A., Xing X.H., Chen Y., Ye F.C., Chen Y., Yan Y.Y., Liu Z., Bi R.C. Production of heparin oligosaccharides by fusion protein of MBP-heparinase I and the enzyme thermostability. J. Mol. Catal. B-Enzym. 2006, 43:90-95.
    • (2006) J. Mol. Catal. B-Enzym. , vol.43 , pp. 90-95
    • Ying, K.A.1    Xing, X.H.2    Chen, Y.3    Ye, F.C.4    Chen, Y.5    Yan, Y.Y.6    Liu, Z.7    Bi, R.C.8
  • 34
    • 79959199497 scopus 로고    scopus 로고
    • Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: implications for a comprehensive thermostabilization strategy
    • Chen S., Ye F.C., Chen Y., Chen Y., Zhao H.X., Yatsunami R., Nakamura S., Arisaka F., Xing X.H. Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: implications for a comprehensive thermostabilization strategy. Biotechnol. Bioeng. 2011, 108:1841-1851.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1841-1851
    • Chen, S.1    Ye, F.C.2    Chen, Y.3    Chen, Y.4    Zhao, H.X.5    Yatsunami, R.6    Nakamura, S.7    Arisaka, F.8    Xing, X.H.9
  • 35
    • 0023711722 scopus 로고
    • Immobilized heparin lyase system for blood deheparinization
    • Bernstein H., Yang V.C., Cooney C.L., Langer R. Immobilized heparin lyase system for blood deheparinization. Methods Enzymol. 1988, 137:515-529.
    • (1988) Methods Enzymol. , vol.137 , pp. 515-529
    • Bernstein, H.1    Yang, V.C.2    Cooney, C.L.3    Langer, R.4
  • 38
    • 0024955211 scopus 로고
    • Heparinase immobilization. Characterization and optimization
    • Yang V.C., Bernstein H., Langer R. Heparinase immobilization. Characterization and optimization. Ann. N.Y. Acad. Sci. 1988, 542:515-520.
    • (1988) Ann. N.Y. Acad. Sci. , vol.542 , pp. 515-520
    • Yang, V.C.1    Bernstein, H.2    Langer, R.3
  • 40
    • 0024817095 scopus 로고
    • Immobilized enzyme cellulose hollow fibers. 1. Immobilization of heparinase
    • Comfort A.R., Albert E.C., Langer R. Immobilized enzyme cellulose hollow fibers. 1. Immobilization of heparinase. Biotechnol. Bioeng. 1989, 34:1366-1373.
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 1366-1373
    • Comfort, A.R.1    Albert, E.C.2    Langer, R.3
  • 42
    • 0343247806 scopus 로고    scopus 로고
    • The roles and function of cellulose-binding domains
    • Linder M., Teeri T.T. The roles and function of cellulose-binding domains. J. Biotechnol. 1997, 57:15-28.
    • (1997) J. Biotechnol. , vol.57 , pp. 15-28
    • Linder, M.1    Teeri, T.T.2
  • 43
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho F.A., Spurlino J.C., Rodseth L.E. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure 1997, 5:997-1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 44
    • 84903193548 scopus 로고    scopus 로고
    • (2014).
    • (2014). http://online.edqm.eu/.
  • 45
    • 78751655946 scopus 로고    scopus 로고
    • Heparin mapping using heparin lyases and the generation of a novel low molecular weight heparin
    • Xiao Z.P., Tappen B.R., Ly M., Zhao W.J., Canova L.P., Guan H.S., Linhardt R.J. Heparin mapping using heparin lyases and the generation of a novel low molecular weight heparin. J. Med. Chem. 2011, 54:603-610.
    • (2011) J. Med. Chem. , vol.54 , pp. 603-610
    • Xiao, Z.P.1    Tappen, B.R.2    Ly, M.3    Zhao, W.J.4    Canova, L.P.5    Guan, H.S.6    Linhardt, R.J.7
  • 46
    • 62149105066 scopus 로고    scopus 로고
    • Mechanism of mild acid hydrolysis of galactan polysaccharides with highly ordered disaccharide repeats leading to a complete series of exclusively odd-numbered oligosaccharides
    • Yang B., Yu G., Zhao X., Jiao G., Ren S., Chai W. Mechanism of mild acid hydrolysis of galactan polysaccharides with highly ordered disaccharide repeats leading to a complete series of exclusively odd-numbered oligosaccharides. FEBS J. 2009, 276:2125-2137.
    • (2009) FEBS J. , vol.276 , pp. 2125-2137
    • Yang, B.1    Yu, G.2    Zhao, X.3    Jiao, G.4    Ren, S.5    Chai, W.6
  • 48
    • 33745748175 scopus 로고    scopus 로고
    • Increasing protein stability through control of the nanoscale environment
    • Asuri P., Karajanagi S.S., Yang H., Yim T.J., Kane R.S., Dordick J.S. Increasing protein stability through control of the nanoscale environment. Langmuir 2006, 22:5833-5836.
    • (2006) Langmuir , vol.22 , pp. 5833-5836
    • Asuri, P.1    Karajanagi, S.S.2    Yang, H.3    Yim, T.J.4    Kane, R.S.5    Dordick, J.S.6
  • 49
    • 79960846411 scopus 로고    scopus 로고
    • Effect of gold nanoparticle morphology on adsorbed protein structure and function
    • Gagner J.E., Lopez M.D., Dordick J.S., Siegel R.W. Effect of gold nanoparticle morphology on adsorbed protein structure and function. Biomaterials 2011, 32:7241-7252.
    • (2011) Biomaterials , vol.32 , pp. 7241-7252
    • Gagner, J.E.1    Lopez, M.D.2    Dordick, J.S.3    Siegel, R.W.4
  • 50
    • 84858240349 scopus 로고    scopus 로고
    • Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles
    • Shrivastava S., Nuffer J.S., Siegel R.W., Dordick J.S. Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles. Nano Lett. 2012, 12:1583-1587.
    • (2012) Nano Lett. , vol.12 , pp. 1583-1587
    • Shrivastava, S.1    Nuffer, J.S.2    Siegel, R.W.3    Dordick, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.