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Volumn 240, Issue , 2014, Pages 426-433

Enhanced stability and catalytic activity of immobilized α-amylase on modified Fe3O4 nanoparticles

Author keywords

Amylase; Enzyme activity; Immobilization; Magnetite nanoparticles; Stability

Indexed keywords

3-AMINOPROPYLTRIETHOXYSILANE; COPRECIPITATION METHOD; ENHANCED STABILITY; IMMOBILIZATION PROCESS; IMMOBILIZED ENZYME; MAGNETIC IRON OXIDE NANOPARTICLES; MAGNETICALLY ACTIVES; OPTIMUM CONCENTRATION;

EID: 84890925539     PISSN: 13858947     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cej.2013.11.059     Document Type: Article
Times cited : (124)

References (42)
  • 2
    • 0029049222 scopus 로고
    • Dodecanoic acid inhibition of a lipase from Acinetobacter sp. OPA 55
    • Markweghanke M., Lang S., Wanger F. Dodecanoic acid inhibition of a lipase from Acinetobacter sp. OPA 55. Enzyme Microb. Technol. 1995, 17:512-516.
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 512-516
    • Markweghanke, M.1    Lang, S.2    Wanger, F.3
  • 5
    • 1642492905 scopus 로고    scopus 로고
    • α-Amylases of medical and industrial importance
    • Kandra L. α-Amylases of medical and industrial importance. J. Mol. Struct. 2003, 666:487-498.
    • (2003) J. Mol. Struct. , vol.666 , pp. 487-498
    • Kandra, L.1
  • 8
    • 34249049259 scopus 로고    scopus 로고
    • Alpha-amylase immobilization on functionalized glass beads by covalent attachment
    • Kahraman M.V., Bayramoglu G., Kayaman N.A., Gungor A. Alpha-amylase immobilization on functionalized glass beads by covalent attachment. Food Chem. 2007, 104:1385-1392.
    • (2007) Food Chem. , vol.104 , pp. 1385-1392
    • Kahraman, M.V.1    Bayramoglu, G.2    Kayaman, N.A.3    Gungor, A.4
  • 9
    • 77952295951 scopus 로고    scopus 로고
    • Amylase-functionalized mesoporous silica thin films as robust biocatalyst platforms
    • Bellino M.G., Regazzoni A.E. Amylase-functionalized mesoporous silica thin films as robust biocatalyst platforms. Appl. Mater. Interf. 2010, 2:360-365.
    • (2010) Appl. Mater. Interf. , vol.2 , pp. 360-365
    • Bellino, M.G.1    Regazzoni, A.E.2
  • 10
    • 35448934474 scopus 로고    scopus 로고
    • Immobilization of α-amylase from mung beans on amberlite MB 150 and chitosan beads: a comparative study
    • Tripathi P., Kumari A., Rath P., Kayastha A.M. Immobilization of α-amylase from mung beans on amberlite MB 150 and chitosan beads: a comparative study. J. Mol. Catal. B: Enzym. 2007, 49:69-74.
    • (2007) J. Mol. Catal. B: Enzym. , vol.49 , pp. 69-74
    • Tripathi, P.1    Kumari, A.2    Rath, P.3    Kayastha, A.M.4
  • 12
    • 33749250158 scopus 로고    scopus 로고
    • Entrapment of α-amylase in alginate beads: single step protocol for purification and thermal stabilization
    • Kumar R.S.S., Vishwanath K.S., Singh S.A., Rao A.G.A. Entrapment of α-amylase in alginate beads: single step protocol for purification and thermal stabilization. Process. Biochem. 2006, 41:2282-2288.
    • (2006) Process. Biochem. , vol.41 , pp. 2282-2288
    • Kumar, R.S.S.1    Vishwanath, K.S.2    Singh, S.A.3    Rao, A.G.A.4
  • 14
    • 0043014714 scopus 로고    scopus 로고
    • Thermal stability of alpha-amylase from Aspergillus oryzae entrapped in polyacrylamide gel
    • Raviyan P., Tang J., Rasco B.A. Thermal stability of alpha-amylase from Aspergillus oryzae entrapped in polyacrylamide gel. J. Agric. Food Chem. 2003, 51:5462-5466.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 5462-5466
    • Raviyan, P.1    Tang, J.2    Rasco, B.A.3
  • 15
    • 0031213603 scopus 로고    scopus 로고
    • Immobilization of α-amylase to temperature-responsive polymers by single or multiple point attachments
    • Chen J.P., Chu D.H., Sun Y.M. Immobilization of α-amylase to temperature-responsive polymers by single or multiple point attachments. J. Chem. Technol. Biotechnol. 1997, 69:421-428.
    • (1997) J. Chem. Technol. Biotechnol. , vol.69 , pp. 421-428
    • Chen, J.P.1    Chu, D.H.2    Sun, Y.M.3
  • 16
    • 80054821680 scopus 로고    scopus 로고
    • Immobilisation of α-amylase from Aspergillus niger onto polyaniline
    • Pascoal A.M., Mitidieri S., Fernandes K.F. Immobilisation of α-amylase from Aspergillus niger onto polyaniline. Food Bioprod. Process. 2011, 89:300-306.
    • (2011) Food Bioprod. Process. , vol.89 , pp. 300-306
    • Pascoal, A.M.1    Mitidieri, S.2    Fernandes, K.F.3
  • 18
    • 84856349341 scopus 로고    scopus 로고
    • Silver nanoparticle (AgNPs) doped gum acacia-gelatin-silica nanohybrid: an effective support for diastase immobilization
    • Singh V., Ahmed S. Silver nanoparticle (AgNPs) doped gum acacia-gelatin-silica nanohybrid: an effective support for diastase immobilization. Int. J. Bio. Macromol. 2012, 50:353-361.
    • (2012) Int. J. Bio. Macromol. , vol.50 , pp. 353-361
    • Singh, V.1    Ahmed, S.2
  • 19
    • 79952818416 scopus 로고    scopus 로고
    • Carboxy methyl tamarind gum-silica nanohybrids for effective immobilization of amylase
    • Singh V., Kumar P. Carboxy methyl tamarind gum-silica nanohybrids for effective immobilization of amylase. J. Mol. Catal. B: Enzym. 2011, 70:67-73.
    • (2011) J. Mol. Catal. B: Enzym. , vol.70 , pp. 67-73
    • Singh, V.1    Kumar, P.2
  • 20
    • 78751644793 scopus 로고    scopus 로고
    • 4-Chitosan nanoparticles prepared by co-precipitation under the magnetic field for lipase immobilization
    • 4-Chitosan nanoparticles prepared by co-precipitation under the magnetic field for lipase immobilization. Catal. Commun. 2011, 12:717-720.
    • (2011) Catal. Commun. , vol.12 , pp. 717-720
    • Liu, Y.1    Jia, S.2    Wu, Q.3    Ran, J.4    Zhang, W.5    Wu, S.6
  • 21
    • 34247179477 scopus 로고    scopus 로고
    • Magnetic Nanoparticles: synthesis, protection, functionalization, and application
    • Lu A.H., Salabas E.L., Schuth F. Magnetic Nanoparticles: synthesis, protection, functionalization, and application. Angew. Chem. Int. Ed. 2007, 46:1222-1244.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 1222-1244
    • Lu, A.H.1    Salabas, E.L.2    Schuth, F.3
  • 22
    • 84860390504 scopus 로고    scopus 로고
    • Selective removal of chromium from different aqueous systems using magnetic MCM-41 nanosorbents
    • King Lun
    • Xinqing C., Koon Fung L., King Lun Selective removal of chromium from different aqueous systems using magnetic MCM-41 nanosorbents. Chem. Eng. J. 2011, 172:728-734.
    • (2011) Chem. Eng. J. , vol.172 , pp. 728-734
    • Xinqing, C.1    Koon Fung, L.2
  • 23
    • 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., Aribol 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.4    Aribol, J.5    Santamaria, J.6    Yeung, K.L.7
  • 24
    • 84879814814 scopus 로고    scopus 로고
    • Immobilization of α-amylase on gum acacia stabilized magnetite nanoparticles, an easily recoverable and reusable support
    • Swarnalatha V., Esther R.A., Dhamodharan R. Immobilization of α-amylase on gum acacia stabilized magnetite nanoparticles, an easily recoverable and reusable support. J. Mol. Catal. B: Enzym. 2013, 96:6-13.
    • (2013) J. Mol. Catal. B: Enzym. , vol.96 , pp. 6-13
    • Swarnalatha, V.1    Esther, R.A.2    Dhamodharan, R.3
  • 25
    • 64649096755 scopus 로고    scopus 로고
    • Immobilization of α-amylase onto cellulose-coated magnetite (CCM) nanoparticles and preliminary starch degradation study
    • Namdeo M., Bajpai S.K. Immobilization of α-amylase onto cellulose-coated magnetite (CCM) nanoparticles and preliminary starch degradation study. J. Mol. Catal. B: Enzym. 2009, 59:134-139.
    • (2009) J. Mol. Catal. B: Enzym. , vol.59 , pp. 134-139
    • Namdeo, M.1    Bajpai, S.K.2
  • 26
    • 84862785635 scopus 로고    scopus 로고
    • Preparation of magnetic nanoparticles and their use for immobilization of C-terminally lysine-tagged Bacillus sp. TS-23 α-amylase
    • Chen Y.H., Chi M.C., Wang T.F., Chen J.C., Lin L.L. Preparation of magnetic nanoparticles and their use for immobilization of C-terminally lysine-tagged Bacillus sp. TS-23 α-amylase. Appl. Biochem. Biotechnol. 2012, 7:1711-1722.
    • (2012) Appl. Biochem. Biotechnol. , vol.7 , pp. 1711-1722
    • Chen, Y.H.1    Chi, M.C.2    Wang, T.F.3    Chen, J.C.4    Lin, L.L.5
  • 29
    • 71649115367 scopus 로고    scopus 로고
    • Characterization analytical application of surface modified magnetic nanoparticles
    • Jang J., Lim H. Characterization analytical application of surface modified magnetic nanoparticles. Microchem. J. 2010, 94:148-158.
    • (2010) Microchem. J. , vol.94 , pp. 148-158
    • Jang, J.1    Lim, H.2
  • 31
    • 20444406055 scopus 로고
    • Controlled growth of monodisperse silica spheres in the micron size range
    • Stober W., Fink A., Bohn E.J. Controlled growth of monodisperse silica spheres in the micron size range. J. Coll. Interf. Sci. 1968, 26:62-69.
    • (1968) J. Coll. Interf. Sci. , vol.26 , pp. 62-69
    • Stober, W.1    Fink, A.2    Bohn, E.J.3
  • 32
    • 67349211241 scopus 로고    scopus 로고
    • Conjugated polymer as a signal amplifier for novel silica nanoparticle-based fluoro immunoassay
    • Wang Y., Liu B. Conjugated polymer as a signal amplifier for novel silica nanoparticle-based fluoro immunoassay. Biosens. Bioelectron. 2009, 24:3293-3298.
    • (2009) Biosens. Bioelectron. , vol.24 , pp. 3293-3298
    • Wang, Y.1    Liu, B.2
  • 33
    • 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
  • 34
    • 33748037939 scopus 로고
    • α and β amylases
    • Bernfeld P. α and β amylases. Methods Enzymol. 1955, 1:149-158.
    • (1955) Methods Enzymol. , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 36
    • 50049135156 scopus 로고    scopus 로고
    • Immobilization of alpha-amylase onto cyclic carbonate bearing hybrid material
    • Turunc O., Kahraman M.V., Akdemir Z.S., Kayaman-Apohan N., Gungor A. Immobilization of alpha-amylase onto cyclic carbonate bearing hybrid material. Food Chem. 2009, 112(4):992-997.
    • (2009) Food Chem. , vol.112 , Issue.4 , pp. 992-997
    • Turunc, O.1    Kahraman, M.V.2    Akdemir, Z.S.3    Kayaman-Apohan, N.4    Gungor, A.5
  • 37
    • 1842834012 scopus 로고    scopus 로고
    • Immobilization of alpha-amylase from Bacillus circulans grs 313 on coconut fiber
    • Dey G., Nagpal V., Banerjee R. Immobilization of alpha-amylase from Bacillus circulans grs 313 on coconut fiber. Appl. Biochem. Microbiol. 2002, 102:303-313.
    • (2002) Appl. Biochem. Microbiol. , vol.102 , pp. 303-313
    • Dey, G.1    Nagpal, V.2    Banerjee, R.3
  • 38
    • 0019586531 scopus 로고
    • Immobilization of bacillus subtilis alpha-amylase on zirconia-coated alkylamine glass with glutaraldehyde
    • Ramesh V., Singh C. Immobilization of bacillus subtilis alpha-amylase on zirconia-coated alkylamine glass with glutaraldehyde. Enzyme Microb. Technol. 1981, 3:246-248.
    • (1981) Enzyme Microb. Technol. , vol.3 , pp. 246-248
    • Ramesh, V.1    Singh, C.2
  • 39
    • 34249049259 scopus 로고    scopus 로고
    • Alpha-amylase immobilization on functionalized glass beads by covalent attachment
    • Kahraman M.V., Bayramoglu G., Kayaman-Apohan N., Gungor A. Alpha-amylase immobilization on functionalized glass beads by covalent attachment. Food Chem. 2007, 104:1385-1392.
    • (2007) Food Chem. , vol.104 , pp. 1385-1392
    • Kahraman, M.V.1    Bayramoglu, G.2    Kayaman-Apohan, N.3    Gungor, A.4
  • 40
    • 0032484961 scopus 로고    scopus 로고
    • Stability of alpha-amylase immobilized on poly(methyl methacrylate-acrylic acid) microspheres
    • Aksoy S., Tumturk H., Hasirci N. Stability of alpha-amylase immobilized on poly(methyl methacrylate-acrylic acid) microspheres. J. Biotechnol. 1998, 60:37-46.
    • (1998) J. Biotechnol. , vol.60 , pp. 37-46
    • Aksoy, S.1    Tumturk, H.2    Hasirci, N.3
  • 41
    • 70349756614 scopus 로고    scopus 로고
    • Immobilization of alpha-amylase on Na-bentonite and modified bentonite
    • Sedaghat M.E., Ghiaci M., Aghaei H., Soleimanian-Zad S. Immobilization of alpha-amylase on Na-bentonite and modified bentonite. Appl. Clay Sci. 2009, 46:125-130.
    • (2009) Appl. Clay Sci. , vol.46 , pp. 125-130
    • Sedaghat, M.E.1    Ghiaci, M.2    Aghaei, H.3    Soleimanian-Zad, S.4
  • 42
    • 84879814814 scopus 로고    scopus 로고
    • Immobilized of α-amylase on gum acacia stabilized magnetite nanoparticles, an easily recoverable and reusable support
    • Swarnalatha V., Esther R.A., Dhamodharan R. Immobilized of α-amylase on gum acacia stabilized magnetite nanoparticles, an easily recoverable and reusable support. J. Mol. Catal. B: Enzym. 2013, 96:6-13.
    • (2013) J. Mol. Catal. B: Enzym. , vol.96 , pp. 6-13
    • Swarnalatha, V.1    Esther, R.A.2    Dhamodharan, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.