메뉴 건너뛰기




Volumn 34, Issue , 2015, Pages 242-250

Increasing the activity of immobilized enzymes with nanoparticle conjugation

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; ENZYME IMMOBILIZATION; ENZYMES; METAL NANOPARTICLES; NANOCRYSTALS; NANOPARTICLES; SEMICONDUCTOR QUANTUM DOTS; SURFACE CHEMISTRY; YARN;

EID: 84940207531     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2015.04.005     Document Type: Review
Times cited : (234)

References (61)
  • 1
    • 0028918401 scopus 로고
    • A proficient enzyme
    • Radzicka A., Wolfenden R. A proficient enzyme. Science 1995, 267:90-93.
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 4
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • Koeller K.M., Wong C.H. Enzymes for chemical synthesis. Nature 2001, 409:232-240.
    • (2001) Nature , vol.409 , pp. 232-240
    • Koeller, K.M.1    Wong, C.H.2
  • 5
    • 2542563521 scopus 로고    scopus 로고
    • Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: library construction methods for directed evolution
    • Neylon C. Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: library construction methods for directed evolution. Nucleic Acids Res 2004, 32:1448-1459.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1448-1459
    • Neylon, C.1
  • 6
    • 84902306144 scopus 로고    scopus 로고
    • Spectroscopic investigations on the effect of n-acetyl-l-cysteine-capped CDTE quantum dots on catalase
    • Sun H., Yang B., Cui E., Liu R. Spectroscopic investigations on the effect of n-acetyl-l-cysteine-capped CDTE quantum dots on catalase. Spectrochim Acta A 2014, 132:692-699.
    • (2014) Spectrochim Acta A , vol.132 , pp. 692-699
    • Sun, H.1    Yang, B.2    Cui, E.3    Liu, R.4
  • 7
    • 84885548639 scopus 로고    scopus 로고
    • Improved activity of immobilized horseradish peroxidase on gold nanoparticles in the presence of bovine serum albumin
    • Ni Y., Li J., Huang Z., He K., Zhuang J., Yang W. Improved activity of immobilized horseradish peroxidase on gold nanoparticles in the presence of bovine serum albumin. J Nanopart Res 2013, 15:1-10.
    • (2013) J Nanopart Res , vol.15 , pp. 1-10
    • Ni, Y.1    Li, J.2    Huang, Z.3    He, K.4    Zhuang, J.5    Yang, W.6
  • 9
    • 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
  • 10
    • 0032029399 scopus 로고    scopus 로고
    • Immobilisation of trypsin on acrylic copolymers
    • Bryjak J., Kolarz B.N. Immobilisation of trypsin on acrylic copolymers. Process Biochem 1998, 33:409-417.
    • (1998) Process Biochem , vol.33 , pp. 409-417
    • Bryjak, J.1    Kolarz, B.N.2
  • 12
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: strategies to prevent sub-unit dissociation
    • Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent sub-unit dissociation. Enzyme Microb Technol 2009, 45:405-418.
    • (2009) Enzyme Microb Technol , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 14
    • 84864258079 scopus 로고    scopus 로고
    • The effect of nanoparticle size, shape, and surface chemistry on biological systems
    • Albanese A., Tang P.S., Chan W.C. The effect of nanoparticle size, shape, and surface chemistry on biological systems. Annu Rev Biomed Eng 2012, 14:1-16.
    • (2012) Annu Rev Biomed Eng , vol.14 , pp. 1-16
    • Albanese, A.1    Tang, P.S.2    Chan, W.C.3
  • 15
    • 84872415717 scopus 로고    scopus 로고
    • Enzyme stabilization by nano/microsized hybrid materials
    • Hwang E.T., Gu M.B. Enzyme stabilization by nano/microsized hybrid materials. Eng Life Sci 2013, 13:49-61.
    • (2013) Eng Life Sci , vol.13 , pp. 49-61
    • Hwang, E.T.1    Gu, M.B.2
  • 17
    • 84904419291 scopus 로고    scopus 로고
    • Nano-designed enzyme-functionalized hierarchical metal-oxide mesoporous thin films: En route to versatile biofuel cells
    • Bellino M.G., Soler-Illia G.J.A.A. Nano-designed enzyme-functionalized hierarchical metal-oxide mesoporous thin films: En route to versatile biofuel cells. Small 2014, 10:2834-2839.
    • (2014) Small , vol.10 , pp. 2834-2839
    • Bellino, M.G.1    Soler-Illia, G.J.A.A.2
  • 18
    • 56349086047 scopus 로고    scopus 로고
    • Buelent. Enzymetic production of biodiesel from canola oil using immobilized lipase
    • Dizge N.K. Buelent. Enzymetic production of biodiesel from canola oil using immobilized lipase. Biomass Bioenerg 2008, 32:1274-1278.
    • (2008) Biomass Bioenerg , vol.32 , pp. 1274-1278
    • Dizge, N.K.1
  • 19
    • 84873737627 scopus 로고    scopus 로고
    • A novel therapeutic system for malignant glioma: nanoformulation, pharmacokinetic, and anticancer properties of cell-nano-drug delivery
    • Tao Y., Ning M., Dou H. A novel therapeutic system for malignant glioma: nanoformulation, pharmacokinetic, and anticancer properties of cell-nano-drug delivery. Nanomed-Nanotechnol 2013, 9:222-232.
    • (2013) Nanomed-Nanotechnol , vol.9 , pp. 222-232
    • Tao, Y.1    Ning, M.2    Dou, H.3
  • 20
    • 84914689387 scopus 로고    scopus 로고
    • Flexible gold electrode array for multiplexed immunoelectrochemical measurement of three protein biomarkers for prostate cancer
    • Liu J., Lu C.Y., Zhou H., Xu J.J., Chen H.Y. Flexible gold electrode array for multiplexed immunoelectrochemical measurement of three protein biomarkers for prostate cancer. ACS Appl Mater Interfaces 2014, 6:20137-20143.
    • (2014) ACS Appl Mater Interfaces , vol.6 , pp. 20137-20143
    • Liu, J.1    Lu, C.Y.2    Zhou, H.3    Xu, J.J.4    Chen, H.Y.5
  • 21
    • 84898889702 scopus 로고    scopus 로고
    • Understanding enzymatic acceleration at nanoparticle interfaces: approaches and challenges
    • Johnson B.J., Russ Algar W., Malanoski A.P., Ancona M.G., Medintz I.L. Understanding enzymatic acceleration at nanoparticle interfaces: approaches and challenges. Nano Today 2014, 9:102-131.
    • (2014) Nano Today , vol.9 , pp. 102-131
    • Johnson, B.J.1    Russ Algar, W.2    Malanoski, A.P.3    Ancona, M.G.4    Medintz, I.L.5
  • 22
    • 84859895764 scopus 로고    scopus 로고
    • Rational nanoconjugation improves biocatalytic performance of enzymes: aldol addition catalyzed by immobilized rhamnulose-1-phosphate aldolase
    • Ardao I., Comenge J., Benaiges M.D., Álvaro G., Puntes V.F. Rational nanoconjugation improves biocatalytic performance of enzymes: aldol addition catalyzed by immobilized rhamnulose-1-phosphate aldolase. Langmuir 2012, 28:6461-6467.
    • (2012) Langmuir , vol.28 , pp. 6461-6467
    • Ardao, I.1    Comenge, J.2    Benaiges, M.D.3    Álvaro, G.4    Puntes, V.F.5
  • 23
    • 84859200684 scopus 로고    scopus 로고
    • Regulation of catalytic behaviour of hydrolases through interactions with functionalized carbon-based nanomaterials
    • Pavlidis I., Vorhaben T., Gournis D., Papadopoulos G., Bornscheuer U., Stamatis H. Regulation of catalytic behaviour of hydrolases through interactions with functionalized carbon-based nanomaterials. J Nanopart Res 2012, 14:1-10.
    • (2012) J Nanopart Res , vol.14 , pp. 1-10
    • Pavlidis, I.1    Vorhaben, T.2    Gournis, D.3    Papadopoulos, G.4    Bornscheuer, U.5    Stamatis, H.6
  • 24
    • 80055033102 scopus 로고    scopus 로고
    • Effects of carbon nanotube-tethered nanosphere density on amperometric biosensing: simulation and experiment
    • Claussen J.C., Hengenius J.B., Wickner M.M., Fisher T.S., Umulis D.M., Porterfield D.M. Effects of carbon nanotube-tethered nanosphere density on amperometric biosensing: simulation and experiment. J Phys Chem C 2011, 115:20896-20904.
    • (2011) J Phys Chem C , vol.115 , pp. 20896-20904
    • Claussen, J.C.1    Hengenius, J.B.2    Wickner, M.M.3    Fisher, T.S.4    Umulis, D.M.5    Porterfield, D.M.6
  • 25
    • 79960743654 scopus 로고    scopus 로고
    • Transforming the fabrication and biofunctionalization of gold nanoelectrode arrays into versatile electrochemical glucose biosensors
    • Claussen J.C., Wickner M.M., Fisher T.S., Porterfield D.M. Transforming the fabrication and biofunctionalization of gold nanoelectrode arrays into versatile electrochemical glucose biosensors. ACS Appl Mater Interfaces 2011, 3:1765-1770.
    • (2011) ACS Appl Mater Interfaces , vol.3 , pp. 1765-1770
    • Claussen, J.C.1    Wickner, M.M.2    Fisher, T.S.3    Porterfield, D.M.4
  • 27
    • 84855465141 scopus 로고    scopus 로고
    • Effect of substrate (ZnO) morphology on enzyme immobilization and its catalytic activity
    • Zhang Y., Wu H., Huang X., Zhang J., Guo S. Effect of substrate (ZnO) morphology on enzyme immobilization and its catalytic activity. Nanoscale Res Lett 2011, 6:1-7.
    • (2011) Nanoscale Res Lett , vol.6 , pp. 1-7
    • Zhang, Y.1    Wu, H.2    Huang, X.3    Zhang, J.4    Guo, S.5
  • 30
    • 0142073274 scopus 로고    scopus 로고
    • Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility
    • Jia H., Zhu G., Wang P. Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility. Biotechnol Bioeng 2003, 84:406-414.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 406-414
    • Jia, H.1    Zhu, G.2    Wang, P.3
  • 32
    • 79951846084 scopus 로고    scopus 로고
    • Selective enhancement of nucleases by polyvalent DNA-functionalized gold nanoparticles
    • Prigodich A.E., Alhasan A.H., Mirkin C.A. Selective enhancement of nucleases by polyvalent DNA-functionalized gold nanoparticles. J Am Chem Soc 2011, 133:2120-2123.
    • (2011) J Am Chem Soc , vol.133 , pp. 2120-2123
    • Prigodich, A.E.1    Alhasan, A.H.2    Mirkin, C.A.3
  • 33
    • 84862852658 scopus 로고    scopus 로고
    • Functionalized graphene oxide in enzyme engineering: a selective modulator for enzyme activity and thermostability
    • Jin L., Yang K., Yao K., Zhang S., Tao H., Lee S.-T., Liu Z., Peng R. Functionalized graphene oxide in enzyme engineering: a selective modulator for enzyme activity and thermostability. ACS Nano 2012, 6:4864-4875.
    • (2012) ACS Nano , vol.6 , pp. 4864-4875
    • Jin, L.1    Yang, K.2    Yao, K.3    Zhang, S.4    Tao, H.5    Lee, S.-T.6    Liu, Z.7    Peng, R.8
  • 34
    • 79952649224 scopus 로고    scopus 로고
    • Graphene based gene transfection
    • Feng L., Zhang S., Liu Z. Graphene based gene transfection. Nanoscale 2011, 3:1252-1257.
    • (2011) Nanoscale , vol.3 , pp. 1252-1257
    • Feng, L.1    Zhang, S.2    Liu, Z.3
  • 36
    • 77954989762 scopus 로고    scopus 로고
    • Physical properties of carbon nanotubes
    • Saito R.G.D., Dresselhaus M.S. Physical properties of carbon nanotubes. World Sci 1998, 35-89.
    • (1998) World Sci , pp. 35-89
    • Saito, R.G.D.1    Dresselhaus, M.S.2
  • 37
    • 0031279830 scopus 로고    scopus 로고
    • Molecular adaptations of enzymes from psychrophilic organisms
    • Feller G., Arpigny J.L., Narinx E., Gerday C. Molecular adaptations of enzymes from psychrophilic organisms. Comp Biochem Phys A 1997, 118:495-499.
    • (1997) Comp Biochem Phys A , vol.118 , pp. 495-499
    • Feller, G.1    Arpigny, J.L.2    Narinx, E.3    Gerday, C.4
  • 38
    • 84868133237 scopus 로고    scopus 로고
    • Preparation and characterization of magnetic Fe3O4/CRGO nanocomposites for enzyme immobilization
    • Wu X., Zhang Y., Wu C., Wu H. Preparation and characterization of magnetic Fe3O4/CRGO nanocomposites for enzyme immobilization. T Nonferr Metal Soc 2012, 22:s162-s168.
    • (2012) T Nonferr Metal Soc , vol.22 , pp. s162-s168
    • Wu, X.1    Zhang, Y.2    Wu, C.3    Wu, H.4
  • 40
    • 84855447240 scopus 로고    scopus 로고
    • Assembly of graphene oxide-enzyme conjugates through hydrophobic interaction
    • Zhang Y., Zhang J., Huang X., Zhou X., Wu H., Guo S. Assembly of graphene oxide-enzyme conjugates through hydrophobic interaction. Small 2012, 8:154-159.
    • (2012) Small , vol.8 , pp. 154-159
    • Zhang, Y.1    Zhang, J.2    Huang, X.3    Zhou, X.4    Wu, H.5    Guo, S.6
  • 41
    • 79952444750 scopus 로고    scopus 로고
    • Activity and stability comparison of immobilized nadh oxidase on multi-walled carbon nanotubes, carbon nanospheres, and single-walled carbon nanotubes
    • Wang L., Xu R., Chen Y., Jiang R. Activity and stability comparison of immobilized nadh oxidase on multi-walled carbon nanotubes, carbon nanospheres, and single-walled carbon nanotubes. J Mol Catal B-Enzym 2011, 69:120-126.
    • (2011) J Mol Catal B-Enzym , vol.69 , pp. 120-126
    • Wang, L.1    Xu, R.2    Chen, Y.3    Jiang, R.4
  • 42
    • 84884228761 scopus 로고    scopus 로고
    • Glad assisted synthesis of NiO nanorods for realization of enzymatic reagentless urea biosensor
    • Tyagi M., Tomar M., Gupta V. Glad assisted synthesis of NiO nanorods for realization of enzymatic reagentless urea biosensor. Biosens Bioelectron 2014, 52:196-201.
    • (2014) Biosens Bioelectron , vol.52 , pp. 196-201
    • Tyagi, M.1    Tomar, M.2    Gupta, V.3
  • 43
    • 84893324144 scopus 로고    scopus 로고
    • Pt-cuo nanoparticles decorated reduced graphene oxide for the fabrication of highly sensitive non-enzymatic disposable glucose sensor
    • Dhara K., Stanley J., T R., Nair B.G., TG S.B. Pt-cuo nanoparticles decorated reduced graphene oxide for the fabrication of highly sensitive non-enzymatic disposable glucose sensor. Sensor Actuat B-Chem 2014, 195:197-205.
    • (2014) Sensor Actuat B-Chem , vol.195 , pp. 197-205
    • Dhara, K.1    Stanley, J.2    Nair, T.R.B.G.3    TG, S.B.4
  • 44
    • 77954864054 scopus 로고    scopus 로고
    • Enzymatic transesterification of soybean oil by using immobilized lipase on magnetic nano-particles
    • Xie W., Ma N. Enzymatic transesterification of soybean oil by using immobilized lipase on magnetic nano-particles. Biomass Bioenerg 2010, 34:890-896.
    • (2010) Biomass Bioenerg , vol.34 , pp. 890-896
    • Xie, W.1    Ma, N.2
  • 45
    • 84906094819 scopus 로고    scopus 로고
    • Size-dependent effects of nanoparticles on enzymes in the blood coagulation cascade
    • Sanfins E., Augustsson C., Dahlbäck B., Linse S., Cedervall T. Size-dependent effects of nanoparticles on enzymes in the blood coagulation cascade. Nano Letters 2014, 14:4736-4744.
    • (2014) Nano Letters , vol.14 , pp. 4736-4744
    • Sanfins, E.1    Augustsson, C.2    Dahlbäck, B.3    Linse, S.4    Cedervall, T.5
  • 46
    • 71549171434 scopus 로고    scopus 로고
    • Enhanced activity of enzymes immobilized in thermoresponsive core-shell microgels
    • Welsch N., Wittemann A., Ballauff M. Enhanced activity of enzymes immobilized in thermoresponsive core-shell microgels. J Phys Chem B 2009, 113:16039-16045.
    • (2009) J Phys Chem B , vol.113 , pp. 16039-16045
    • Welsch, N.1    Wittemann, A.2    Ballauff, M.3
  • 47
    • 84861058714 scopus 로고    scopus 로고
    • Gold nanoparticles in chemical and biological sensing
    • Saha K., Agasti S.S., Kim C., Li X., Rotello V.M. Gold nanoparticles in chemical and biological sensing. Chem Rev 2012, 112:2739-2779.
    • (2012) Chem Rev , vol.112 , pp. 2739-2779
    • Saha, K.1    Agasti, S.S.2    Kim, C.3    Li, X.4    Rotello, V.M.5
  • 48
    • 84934922665 scopus 로고    scopus 로고
    • Immobilization of lipase on silver nanoparticles via adhesive polydopamine for biodiesel production
    • Dumri K., Hung Anh D. Immobilization of lipase on silver nanoparticles via adhesive polydopamine for biodiesel production. Enzyme Res 2014, 2014:9.
    • (2014) Enzyme Res , vol.2014 , pp. 9
    • Dumri, K.1    Hung Anh, D.2
  • 49
    • 55349136999 scopus 로고    scopus 로고
    • An enzymatic kinetics investigation into the significantly enhanced activity of functionalized gold nanoparticles
    • Wu C.-S., Wu C.-T., Yang Y.-S., Ko F.-H. An enzymatic kinetics investigation into the significantly enhanced activity of functionalized gold nanoparticles. Chem Commun 2008, 42:5327-5329.
    • (2008) Chem Commun , vol.42 , pp. 5327-5329
    • Wu, C.-S.1    Wu, C.-T.2    Yang, Y.-S.3    Ko, F.-H.4
  • 50
    • 79959449060 scopus 로고    scopus 로고
    • Size-modulated catalytic activity of enzyme-nanoparticle conjugates: a combined kinetic and theoretical study
    • Wu C.-S., Lee C.-C., Wu C.-T., Yang Y.-S., Ko F.-H. Size-modulated catalytic activity of enzyme-nanoparticle conjugates: a combined kinetic and theoretical study. Chem Commun 2011, 47:7446-7448.
    • (2011) Chem Commun , vol.47 , pp. 7446-7448
    • Wu, C.-S.1    Lee, C.-C.2    Wu, C.-T.3    Yang, Y.-S.4    Ko, F.-H.5
  • 51
    • 84940182416 scopus 로고    scopus 로고
    • Construction of a high-performance magnetic enzyme nanosystem for rapid tryptic digestion
    • Cheng G., Zheng S.-Y. Construction of a high-performance magnetic enzyme nanosystem for rapid tryptic digestion. Sci Rep 2014, 4.
    • (2014) Sci Rep , pp. 4
    • Cheng, G.1    Zheng, S.-Y.2
  • 52
    • 84873821085 scopus 로고    scopus 로고
    • A new nanobiocatalytic system based on allosteric effect with dramatically enhanced enzymatic performance
    • Wang L.-B., Wang Y.-C., He R., Zhuang A., Wang X., Zeng J., Hou J.G. A new nanobiocatalytic system based on allosteric effect with dramatically enhanced enzymatic performance. J Am Chem Soc 2013, 135:1272-1275.
    • (2013) J Am Chem Soc , vol.135 , pp. 1272-1275
    • Wang, L.-B.1    Wang, Y.-C.2    He, R.3    Zhuang, A.4    Wang, X.5    Zeng, J.6    Hou, J.G.7
  • 53
    • 84888389570 scopus 로고    scopus 로고
    • Biophotonic logic devices based on quantum dots and temporally-staggered forster energy transfer relays
    • Claussen J.C., Algar W.R., Hildebrandt N., Susumu K., Ancona M.G., Medintz I.L. Biophotonic logic devices based on quantum dots and temporally-staggered forster energy transfer relays. Nanoscale 2013, 5:12156-12170.
    • (2013) Nanoscale , vol.5 , pp. 12156-12170
    • Claussen, J.C.1    Algar, W.R.2    Hildebrandt, N.3    Susumu, K.4    Ancona, M.G.5    Medintz, I.L.6
  • 55
    • 20144379798 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for imaging, labelling and sensing
    • Medintz I.L., Uyeda H.T., Goldman E.R., Mattoussi H. Quantum dot bioconjugates for imaging, labelling and sensing. Nat Mater 2005, 4:435-446.
    • (2005) Nat Mater , vol.4 , pp. 435-446
    • Medintz, I.L.1    Uyeda, H.T.2    Goldman, E.R.3    Mattoussi, H.4
  • 56
    • 84875421868 scopus 로고    scopus 로고
    • Quantum dots in bioanalysis: a review of applications across various platforms for fluorescence spectroscopy and imaging
    • Petryayeva E., Algar W.R., Medintz I.L. Quantum dots in bioanalysis: a review of applications across various platforms for fluorescence spectroscopy and imaging. Appl Spectrosc 2013, 67:215-252.
    • (2013) Appl Spectrosc , vol.67 , pp. 215-252
    • Petryayeva, E.1    Algar, W.R.2    Medintz, I.L.3
  • 57
    • 84873472142 scopus 로고    scopus 로고
    • Size-modulated synergy of cellulase clustering for enhanced cellulose hydrolysis
    • Tsai S.-L., Park M., Chen W. Size-modulated synergy of cellulase clustering for enhanced cellulose hydrolysis. Biotechnol J 2013, 8:257-261.
    • (2013) Biotechnol J , vol.8 , pp. 257-261
    • Tsai, S.-L.1    Park, M.2    Chen, W.3
  • 60
    • 33750463714 scopus 로고    scopus 로고
    • Universal tools for biomolecular attachment to surfaces
    • Medintz I. Universal tools for biomolecular attachment to surfaces. Nat Mater 2006, 5:842.
    • (2006) Nat Mater , vol.5 , pp. 842
    • Medintz, I.1
  • 61
    • 84875206491 scopus 로고    scopus 로고
    • Functionalizing nanoparticles with biological molecules: developing chemistries that facilitate nanotechnology
    • Sapsford K.E., Algar W.R., Berti L., Gemmill K.B., Casey B.J., Oh E., Stewart M.H., Medintz I.L. Functionalizing nanoparticles with biological molecules: developing chemistries that facilitate nanotechnology. Chem Rev 2013, 113:1904-2074.
    • (2013) Chem Rev , vol.113 , pp. 1904-2074
    • Sapsford, K.E.1    Algar, W.R.2    Berti, L.3    Gemmill, K.B.4    Casey, B.J.5    Oh, E.6    Stewart, M.H.7    Medintz, I.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.