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Volumn 270, Issue , 2015, Pages 235-243

Covalent attachment of xylanase on functionalized magnetic nanoparticles and determination of its activity and stability

Author keywords

Enzyme activity; Enzyme stability; Functionalized magnetite nanoparticles; Immobilization; Xylan; Xylanase

Indexed keywords

CATALYST ACTIVITY; CHLORINE COMPOUNDS; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GRAVIMETRIC ANALYSIS; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; IRON OXIDES; MAGNETIC STORAGE; MAGNETITE; MAGNETITE NANOPARTICLES; PHOTOELECTRON SPECTROSCOPY; RADIOACTIVE WASTE VITRIFICATION; REUSABILITY; SATURATION MAGNETIZATION; SILICA; STABILITY; THERMOGRAVIMETRIC ANALYSIS; X RAY PHOTOELECTRON SPECTROSCOPY;

EID: 84923667125     PISSN: 13858947     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cej.2015.02.032     Document Type: Article
Times cited : (120)

References (49)
  • 1
    • 84870885611 scopus 로고    scopus 로고
    • Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: toward useful applications in biofuel production process
    • Goh W.J., Makam V.S., Hu J., Kang L., Zheng M., Yoong S.L., Udalagama C.N., Pastorin G. Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: toward useful applications in biofuel production process. Langmuir 2012, 28:16864-16873.
    • (2012) Langmuir , vol.28 , pp. 16864-16873
    • Goh, W.J.1    Makam, V.S.2    Hu, J.3    Kang, L.4    Zheng, M.5    Yoong, S.L.6    Udalagama, C.N.7    Pastorin, G.8
  • 3
    • 58149154817 scopus 로고    scopus 로고
    • Hyper production of cellulase-free xylanase by Thermomyces lanuginosus SSBP on bagasse pulp and its application in bioleaching
    • Manimaran A., Kumar K.S., Permaul K., Singh S. Hyper production of cellulase-free xylanase by Thermomyces lanuginosus SSBP on bagasse pulp and its application in bioleaching. Appl. Microbiol. Biotechnol. 2009, 81:887-893.
    • (2009) Appl. Microbiol. Biotechnol. , vol.81 , pp. 887-893
    • Manimaran, A.1    Kumar, K.S.2    Permaul, K.3    Singh, S.4
  • 4
    • 21344435552 scopus 로고    scopus 로고
    • Characterization of a xylanase from the newly isolated thermophilic Thermomyces lanuginosus CAU44 and its application in bread making
    • Jiang Z., Yang S., Tan S., Li L., Li X. Characterization of a xylanase from the newly isolated thermophilic Thermomyces lanuginosus CAU44 and its application in bread making. Lett. Appl. Microbiol. 2005, 41:69-76.
    • (2005) Lett. Appl. Microbiol. , vol.41 , pp. 69-76
    • Jiang, Z.1    Yang, S.2    Tan, S.3    Li, L.4    Li, X.5
  • 6
    • 4444277888 scopus 로고    scopus 로고
    • Effect of supplementation of xylanase and phospholipase to a wheat-based diet for weanling pigs on nutrient digestibility and concentrations of microbial metabolites in ileal digesta and feces
    • Diebold G., Mosenthin R., Piepho H.-P., Sauer W. Effect of supplementation of xylanase and phospholipase to a wheat-based diet for weanling pigs on nutrient digestibility and concentrations of microbial metabolites in ileal digesta and feces. J. Anim. Sci. 2004, 82:2647-2656.
    • (2004) J. Anim. Sci. , vol.82 , pp. 2647-2656
    • Diebold, G.1    Mosenthin, R.2    Piepho, H.-P.3    Sauer, W.4
  • 7
    • 84866389071 scopus 로고    scopus 로고
    • Production and characterization of xylanase from Bacillus licheniformis P11 (C) with potential for fruit juice and bakery industry
    • Bajaj B.K., Manhas K. Production and characterization of xylanase from Bacillus licheniformis P11 (C) with potential for fruit juice and bakery industry. Biocatal. Agric. Biotechnol. 2012, 1:330-337.
    • (2012) Biocatal. Agric. Biotechnol. , vol.1 , pp. 330-337
    • Bajaj, B.K.1    Manhas, K.2
  • 9
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • Biely P. Microbial xylanolytic systems. Trends Biotechnol. 1985, 3:286-290.
    • (1985) Trends Biotechnol. , vol.3 , pp. 286-290
    • Biely, P.1
  • 11
    • 35048853474 scopus 로고    scopus 로고
    • Immobilization of xylanase from Bacillus pumilus strain MK001 and its application in production of xylo-oligosaccharides
    • Kapoor M., Kuhad R.C. Immobilization of xylanase from Bacillus pumilus strain MK001 and its application in production of xylo-oligosaccharides. Appl. Biochem. Biotechnol. 2007, 142:125-138.
    • (2007) Appl. Biochem. Biotechnol. , vol.142 , pp. 125-138
    • Kapoor, M.1    Kuhad, R.C.2
  • 12
    • 3142763845 scopus 로고    scopus 로고
    • Application of chitin-and chitosan-based materials for enzyme immobilizations: a review
    • Krajewska B. Application of chitin-and chitosan-based materials for enzyme immobilizations: a review. Enzyme Microb. Technol. 2004, 35:126-139.
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 126-139
    • Krajewska, B.1
  • 14
    • 80051793850 scopus 로고    scopus 로고
    • Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
    • Cowan D.A., Fernandez-Lafuente R. Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzyme. Microb. Technol. 2011, 49:326-346.
    • (2011) Enzyme. Microb. Technol. , vol.49 , pp. 326-346
    • Cowan, D.A.1    Fernandez-Lafuente, R.2
  • 15
    • 84921882960 scopus 로고    scopus 로고
    • Immobilization of xylanase purified from Bacillus pumilus VLK-1 and its application in enrichment of orange and grape juices
    • Kumar L., Nagar S., Mittal A., Garg N., Gupta V.K. Immobilization of xylanase purified from Bacillus pumilus VLK-1 and its application in enrichment of orange and grape juices. J. Food Sci. Technol. 2014, 51:1737-1749.
    • (2014) J. Food Sci. Technol. , vol.51 , pp. 1737-1749
    • Kumar, L.1    Nagar, S.2    Mittal, A.3    Garg, N.4    Gupta, V.K.5
  • 16
    • 84861898733 scopus 로고    scopus 로고
    • Xylanase immobilized nanoporous gold as a highly active and stable biocatalyst
    • Yan X., Wang X., Zhao P., Xu P., Ding Y. Xylanase immobilized nanoporous gold as a highly active and stable biocatalyst. Micropor. Mesopor. Mat. 2012, 161:1-6.
    • (2012) Micropor. Mesopor. Mat. , vol.161 , pp. 1-6
    • Yan, X.1    Wang, X.2    Zhao, P.3    Xu, P.4    Ding, Y.5
  • 17
    • 0344073996 scopus 로고    scopus 로고
    • Preparation, characterization and application of Aspergillus sp. xylanase immobilized on Eudragit S-100
    • Gawande P., Kamat M. Preparation, characterization and application of Aspergillus sp. xylanase immobilized on Eudragit S-100. J. Biotechnol. 1998, 66:165-175.
    • (1998) J. Biotechnol. , vol.66 , pp. 165-175
    • Gawande, P.1    Kamat, M.2
  • 19
    • 84873606993 scopus 로고    scopus 로고
    • Xylanase immobilization on functionalized polyaniline support by covalent attachment
    • Madakbaş S., Daniş Ö., Demir S., Kahraman M.V. Xylanase immobilization on functionalized polyaniline support by covalent attachment. Starch-Stärke 2013, 65:146-150.
    • (2013) Starch-Stärke , vol.65 , pp. 146-150
    • Madakbaş, S.1    Daniş, Ö.2    Demir, S.3    Kahraman, M.V.4
  • 20
    • 79955603076 scopus 로고    scopus 로고
    • Covalent immobilization of xylanase on glutaraldehyde activated alginate beads using response surface methodology: characterization of immobilized enzyme
    • Pal A., Khanum F. Covalent immobilization of xylanase on glutaraldehyde activated alginate beads using response surface methodology: characterization of immobilized enzyme. Process Biochem. 2011, 46:1315-1322.
    • (2011) Process Biochem. , vol.46 , pp. 1315-1322
    • Pal, A.1    Khanum, F.2
  • 21
    • 77952892173 scopus 로고    scopus 로고
    • Immobilization of aspergillus niger xylanase on chitosan using dialdehyde starch as a coupling agent
    • Chen H., Liu L., Lv S., Liu X., Wang M., Song A., Jia X. Immobilization of aspergillus niger xylanase on chitosan using dialdehyde starch as a coupling agent. Appl. Biochem. Biotechnol. 2010, 162:24-32.
    • (2010) Appl. Biochem. Biotechnol. , vol.162 , pp. 24-32
    • Chen, H.1    Liu, L.2    Lv, S.3    Liu, X.4    Wang, M.5    Song, A.6    Jia, X.7
  • 22
    • 33646514237 scopus 로고    scopus 로고
    • New method for the covalent immobilization of a xylanase by radical grafting of acrylamide on cellulose acetate membranes
    • Sarbu A., De Pinho M.N., Freixo M.D.R., Goncalves F., Udrea I. New method for the covalent immobilization of a xylanase by radical grafting of acrylamide on cellulose acetate membranes. Enzyme Microb. Technol. 2006, 39:125-130.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 125-130
    • Sarbu, A.1    De Pinho, M.N.2    Freixo, M.D.R.3    Goncalves, F.4    Udrea, I.5
  • 23
    • 33745936352 scopus 로고    scopus 로고
    • Immobilization of endo-1,4-β-xylanase on polysulfone acrylate membranes: synthesis and characterization
    • Cano À., Minguillón C., Palet C. Immobilization of endo-1,4-β-xylanase on polysulfone acrylate membranes: synthesis and characterization. J. Membr. Sci. 2006, 280:383-388.
    • (2006) J. Membr. Sci. , vol.280 , pp. 383-388
    • Cano, À.1    Minguillón, C.2    Palet, C.3
  • 24
    • 0036452522 scopus 로고    scopus 로고
    • Catalytic properties of the immobilized Aspergillus tamarii xylanase
    • Gouda M.K., Abdel-Naby M.A. Catalytic properties of the immobilized Aspergillus tamarii xylanase. Microbiol. Res. 2002, 157:275-281.
    • (2002) Microbiol. Res. , vol.157 , pp. 275-281
    • Gouda, M.K.1    Abdel-Naby, M.A.2
  • 26
    • 77957935112 scopus 로고    scopus 로고
    • A comparison of covalent immobilization and physical adsorption of a cellulase enzyme mixture
    • Hirsh S., Bilek M., Nosworthy N., Kondyurin A., Remedios C.D., McKenzie D.A. A comparison of covalent immobilization and physical adsorption of a cellulase enzyme mixture. Langmuir 2010, 26:14380-14388.
    • (2010) Langmuir , vol.26 , pp. 14380-14388
    • Hirsh, S.1    Bilek, M.2    Nosworthy, N.3    Kondyurin, A.4    Remedios, C.D.5    McKenzie, D.A.6
  • 27
    • 84910153125 scopus 로고    scopus 로고
    • Immobilization of antibodies and enzymes on 3-aminopropyltriethoxysilane-functionalized bioanalytical platforms for biosensors and diagnostics
    • Vashist S.K., Lam E., Hrapovic S., Male K.B., Luong J.H. Immobilization of antibodies and enzymes on 3-aminopropyltriethoxysilane-functionalized bioanalytical platforms for biosensors and diagnostics. Chem. Rev. 2014, 114:11083-11130.
    • (2014) Chem. Rev. , vol.114 , pp. 11083-11130
    • Vashist, S.K.1    Lam, E.2    Hrapovic, S.3    Male, K.B.4    Luong, J.H.5
  • 28
    • 84882945349 scopus 로고    scopus 로고
    • Progress in enzyme immobilization in ordered mesoporous materials and related applications
    • Zhou Z., Hartmann M. Progress in enzyme immobilization in ordered mesoporous materials and related applications. Chem. Soc. Rev. 2013, 42:3894-3912.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 3894-3912
    • Zhou, Z.1    Hartmann, M.2
  • 29
    • 65249154043 scopus 로고    scopus 로고
    • Noncovalent immobilization of enantioselective catalysts
    • Fraile J.M., García J.I., Mayoral J.A. Noncovalent immobilization of enantioselective catalysts. Chem. Rev. 2008, 109:360-417.
    • (2008) Chem. Rev. , vol.109 , pp. 360-417
    • Fraile, J.M.1    García, J.I.2    Mayoral, J.A.3
  • 30
    • 84908611407 scopus 로고    scopus 로고
    • Well-defined bioarchitecture for immobilization of chloroperoxidase on magnetic nanoparticles and its application in dye decolorization
    • Cui R., Bai C., Jiang Y., Hu M., Li S., Zhai Q. Well-defined bioarchitecture for immobilization of chloroperoxidase on magnetic nanoparticles and its application in dye decolorization. Chem. Eng. J. 2015, 259:640-646.
    • (2015) Chem. Eng. J. , vol.259 , pp. 640-646
    • Cui, R.1    Bai, C.2    Jiang, Y.3    Hu, M.4    Li, S.5    Zhai, Q.6
  • 31
    • 84896897096 scopus 로고    scopus 로고
    • Covalent immobilization of porcine pancreatic lipase on carboxyl-activated magnetic nanoparticles: characterization and application for enzymatic inhibition assays
    • Zhu Y.-T., Ren X.-Y., Liu Y.-M., Wei Y., Qing L.-S., Liao X. Covalent immobilization of porcine pancreatic lipase on carboxyl-activated magnetic nanoparticles: characterization and application for enzymatic inhibition assays. Mater. Sci. Eng. C 2014, 38:278-285.
    • (2014) Mater. Sci. Eng. C , vol.38 , pp. 278-285
    • Zhu, Y.-T.1    Ren, X.-Y.2    Liu, Y.-M.3    Wei, Y.4    Qing, L.-S.5    Liao, X.6
  • 33
    • 84155194944 scopus 로고    scopus 로고
    • Enhancement of stability and catalytic activity of immobilized lipase on silica-coated modified magnetite nanoparticles
    • Ranjbakhsh E., Bordbar A., Abbasi M., Khosropour A., Shams E. Enhancement of stability and catalytic activity of immobilized lipase on silica-coated modified magnetite nanoparticles. Chem. Eng. J. 2012, 179:272-276.
    • (2012) Chem. Eng. J. , vol.179 , pp. 272-276
    • Ranjbakhsh, E.1    Bordbar, A.2    Abbasi, M.3    Khosropour, A.4    Shams, E.5
  • 34
    • 84857501798 scopus 로고    scopus 로고
    • Potential applications of enzymes immobilized on/in nano materials: a review
    • Ansari S.A., Husain Q. Potential applications of enzymes immobilized on/in nano materials: a review. Biotechnol. Adv. 2012, 30:512-523.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 512-523
    • Ansari, S.A.1    Husain, Q.2
  • 35
  • 36
    • 67049145154 scopus 로고    scopus 로고
    • Controlled synthesis of magnetite-silica nanocomposites via a seeded sol-gel approach
    • Yang D., Hu J., Fu S. Controlled synthesis of magnetite-silica nanocomposites via a seeded sol-gel approach. J. Phys. Chem. C 2009, 113:7646-7651.
    • (2009) J. Phys. Chem. C , vol.113 , pp. 7646-7651
    • Yang, D.1    Hu, J.2    Fu, S.3
  • 37
    • 38949207915 scopus 로고    scopus 로고
    • Preparation of magnetic nanoparticles encapsulated by an ultrathin silica shell via transformation of magnetic Fe-MCM-41
    • Arruebo M., Ho W.Y., Lam K.F., Chen X.G., Arbiol J., Santamaria J., Yeung K.L. Preparation of magnetic nanoparticles encapsulated by an ultrathin silica shell via transformation of magnetic Fe-MCM-41. Chem. Mater. 2008, 20:486-493.
    • (2008) Chem. Mater. , vol.20 , pp. 486-493
    • Arruebo, M.1    Ho, W.Y.2    Lam, K.F.3    Chen, X.G.4    Arbiol, J.5    Santamaria, J.6    Yeung, K.L.7
  • 38
    • 0028282273 scopus 로고
    • Magnetic silica dispersions: preparation and stability of surface-modified silica particles with a magnetic core
    • Philipse A.P., Van Bruggen M.P., Pathmamanoharan C. Magnetic silica dispersions: preparation and stability of surface-modified silica particles with a magnetic core. Langmuir 1994, 10:92-99.
    • (1994) Langmuir , vol.10 , pp. 92-99
    • Philipse, A.P.1    Van Bruggen, M.P.2    Pathmamanoharan, C.3
  • 39
    • 67650492686 scopus 로고    scopus 로고
    • Cu(II)-Azabis(oxazoline)-complexes immobilized on superparamagnetic magnetite@silica-nanoparticles: a highly selective and recyclable catalyst for the kinetic resolution of 1,2-diols
    • Schätz A., Hager M., Reiser O. Cu(II)-Azabis(oxazoline)-complexes immobilized on superparamagnetic magnetite@silica-nanoparticles: a highly selective and recyclable catalyst for the kinetic resolution of 1,2-diols. Adv. Funct. Mater. 2009, 19:2109-2115.
    • (2009) Adv. Funct. Mater. , vol.19 , pp. 2109-2115
    • Schätz, A.1    Hager, M.2    Reiser, O.3
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation 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
  • 41
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey M.J., Biely P., Poutanen K. Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 1992, 23:257-270.
    • (1992) J. Biotechnol. , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 42
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 43
    • 0037295457 scopus 로고    scopus 로고
    • Differential scanning calorimetric, circular dichroism, and Fourier transform infrared spectroscopic characterization of the thermal unfolding of xylanase A from Streptomyces lividans
    • Roberge M., Lewis R.N., Shareck F., Morosoli R., Kluepfel D., Dupont C., McElhaney R.N. Differential scanning calorimetric, circular dichroism, and Fourier transform infrared spectroscopic characterization of the thermal unfolding of xylanase A from Streptomyces lividans. Proteins: Struct. Funct. Bioinf. 2003, 50:341-354.
    • (2003) Proteins: Struct. Funct. Bioinf. , vol.50 , pp. 341-354
    • Roberge, M.1    Lewis, R.N.2    Shareck, F.3    Morosoli, R.4    Kluepfel, D.5    Dupont, C.6    McElhaney, R.N.7
  • 45
    • 60549112165 scopus 로고    scopus 로고
    • Bienzyme functionalized three-layer composite magnetic nanoparticles for electrochemical immunosensors
    • Zhuo Y., Yuan P.X., Yuan R., Chai Y.Q., Hong C.L. Bienzyme functionalized three-layer composite magnetic nanoparticles for electrochemical immunosensors. Biomaterials 2009, 30:2284-2290.
    • (2009) Biomaterials , vol.30 , pp. 2284-2290
    • Zhuo, Y.1    Yuan, P.X.2    Yuan, R.3    Chai, Y.Q.4    Hong, C.L.5
  • 46
    • 45449092602 scopus 로고    scopus 로고
    • Immobilization of lipase in ordered mesoporous materials: effect of textural and structural parameters
    • Serra E., Mayoral Á., Sakamoto Y., Blanco R.M., Díaz I. Immobilization of lipase in ordered mesoporous materials: effect of textural and structural parameters. Micropor. Mesopor. Mat. 2008, 114:201-213.
    • (2008) Micropor. Mesopor. Mat. , vol.114 , pp. 201-213
    • Serra, E.1    Mayoral, Á.2    Sakamoto, Y.3    Blanco, R.M.4    Díaz, I.5
  • 47
    • 0027345141 scopus 로고
    • Immobilization of Aspergillus niger NRC 107 xylanase and β-xylosidase, and properties of the immobilized enzymes
    • Abdel-Naby M.A. Immobilization of Aspergillus niger NRC 107 xylanase and β-xylosidase, and properties of the immobilized enzymes. Appl. Biochem. Biotechnol. 1993, 38:69-81.
    • (1993) Appl. Biochem. Biotechnol. , vol.38 , pp. 69-81
    • Abdel-Naby, M.A.1
  • 48
    • 84870823347 scopus 로고    scopus 로고
    • Biochemical characterization, cloning and molecular modeling of a detergent and organic solvent-stable family 11 xylanase from the newly isolated Aspergillus niger US368 strain
    • Hmida-Sayari A., Taktek S., Elgharbi F., Bejar S. Biochemical characterization, cloning and molecular modeling of a detergent and organic solvent-stable family 11 xylanase from the newly isolated Aspergillus niger US368 strain. Process Biochem. 2012, 47:1839-1847.
    • (2012) Process Biochem. , vol.47 , pp. 1839-1847
    • Hmida-Sayari, A.1    Taktek, S.2    Elgharbi, F.3    Bejar, S.4
  • 49
    • 84876469088 scopus 로고    scopus 로고
    • Covalent immobilization of xylanase produced from Bacillus pumilus SV-85S on electrospun polymethyl methacrylate nanofiber membrane
    • Kumar P., Gupta A., Dhakate S.R., Mathur R.B., Nagar S., Gupta V.K. Covalent immobilization of xylanase produced from Bacillus pumilus SV-85S on electrospun polymethyl methacrylate nanofiber membrane. Biotechnol. Appl. Biochem. 2013, 60:162-169.
    • (2013) Biotechnol. Appl. Biochem. , vol.60 , pp. 162-169
    • Kumar, P.1    Gupta, A.2    Dhakate, S.R.3    Mathur, R.B.4    Nagar, S.5    Gupta, V.K.6


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