메뉴 건너뛰기




Volumn 50, Issue 9, 2015, Pages 1394-1399

Immobilization of α-amylase on gold nanorods: An ideal system for starch processing

Author keywords

Gold nanorods; Ideal system; Immobilization; Starch processing; Amylase

Indexed keywords

ENZYMES; GOLD; HYDROPHOBICITY; ION EXCHANGE; NANORIBBONS; NANORODS; PH; PLASMONS; RADIOACTIVE WASTE VITRIFICATION; STARCH;

EID: 84937515029     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2015.06.002     Document Type: Article
Times cited : (63)

References (47)
  • 4
    • 84910092673 scopus 로고    scopus 로고
    • Improving the activity and stability of actinidin by immobilization on gold nanorods
    • A. Homaei, and R. Etemadipour Improving the activity and stability of actinidin by immobilization on gold nanorods Int. J. Biol. Macromol. 72 2015 1176 1181
    • (2015) Int. J. Biol. Macromol. , vol.72 , pp. 1176-1181
    • Homaei, A.1    Etemadipour, R.2
  • 6
    • 84904793107 scopus 로고    scopus 로고
    • Immobilization as a strategy for improving enzyme properties-application to oxidoreductases
    • U. Guzik, K. Hupert-Kocurek, and D. Wojcieszyńska Immobilization as a strategy for improving enzyme properties-application to oxidoreductases Molecules 19 2014 8995 9018
    • (2014) Molecules , vol.19 , pp. 8995-9018
    • Guzik, U.1    Hupert-Kocurek, K.2    Wojcieszyńska, D.3
  • 7
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilization
    • D. Brady, and J. Jordaan Advances in enzyme immobilization Biotechnol. Lett. 31 2009 1639 1650
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 8
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization - Aqueous and non-aqueous environment
    • P.V. Iyer, and L. Ananthanarayan Enzyme stability and stabilization - aqueous and non-aqueous environment Process Biochem. 43 2008 1019 1032
    • (2008) Process Biochem. , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 10
    • 84872415717 scopus 로고    scopus 로고
    • Enzyme stabilization by nano/microsized hybrid materials
    • E.T. Hwang, and M.B. Gu Enzyme stabilization by nano/microsized hybrid materials Eng. Life Sci. 13 2013 49 61
    • (2013) Eng. Life Sci. , vol.13 , pp. 49-61
    • Hwang, E.T.1    Gu, M.B.2
  • 12
    • 78650818528 scopus 로고    scopus 로고
    • Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
    • K. Hernandez, and R. Fernandez-Lafuente Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance Enzyme Microb. Technol. 48 2011 107 122
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 107-122
    • Hernandez, K.1    Fernandez-Lafuente, R.2
  • 14
    • 8144224612 scopus 로고    scopus 로고
    • Purification, characterization, and structural investigation of a new moderately thermophilic and partially calcium-independent extracellular α-amylase from Bacillus sp. TM1
    • R.H. Sajedi, H. Naderi-Manesh, K. Khajeh, B. Ranjbar, N. Ghaemi, and M. Naderi-Manesh Purification, characterization, and structural investigation of a new moderately thermophilic and partially calcium-independent extracellular α-amylase from Bacillus sp. TM1 Appl. Biochem. Biotechnol. 119 2004 41 50
    • (2004) Appl. Biochem. Biotechnol. , vol.119 , pp. 41-50
    • Sajedi, R.H.1    Naderi-Manesh, H.2    Khajeh, K.3    Ranjbar, B.4    Ghaemi, N.5    Naderi-Manesh, M.6
  • 15
    • 77956806266 scopus 로고    scopus 로고
    • Application of microbial α-amylase in industry - A review
    • P.M. de Souza, and P. de Oliveira Magalhães Application of microbial α-amylase in industry - a review Braz. J. Microbiol. 41 2010 850 861
    • (2010) Braz. J. Microbiol. , vol.41 , pp. 850-861
    • De Souza, P.M.1    De Oliveira Magalhães, P.2
  • 16
    • 35448934474 scopus 로고    scopus 로고
    • Immobilization of α-amylase from mung beans on Amberlite MB 150 and chitosan beads: A comparative study
    • P. Tripathi, A. Kumari, P. Rath, and A.M. Kayastha Immobilization of α-amylase from mung beans on Amberlite MB 150 and chitosan beads: a comparative study J. Mol. Catal. B: Enzym. 49 2007 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
  • 17
    • 77952295951 scopus 로고    scopus 로고
    • Amylase-functionalized mesoporous silica thin films as robust biocatalyst platforms
    • M.G. Bellino, and A.E. Regazzoni Amylase-functionalized mesoporous silica thin films as robust biocatalyst platforms Appl. Mater. Interfaces 2 2010 360 365
    • (2010) Appl. Mater. Interfaces , vol.2 , pp. 360-365
    • Bellino, M.G.1    Regazzoni, A.E.2
  • 18
    • 80054821680 scopus 로고    scopus 로고
    • Immobilisation of α-amylase from Aspergillus niger onto polyaniline
    • A.M. Pascoal, S. Mitidieri, and K.F. Fernandes Immobilisation of α-amylase from Aspergillus niger onto polyaniline Food Bioprod. Process. 89 2011 300 306
    • (2011) Food Bioprod. Process. , vol.89 , pp. 300-306
    • Pascoal, A.M.1    Mitidieri, S.2    Fernandes, K.F.3
  • 20
    • 84898458625 scopus 로고    scopus 로고
    • Optimal immobilization of α-amylase from wheat (Triticum aestivum) onto DEAE-cellulose using response surface methodology and its characterization
    • K. Singh, and A.M. Kayastha Optimal immobilization of α-amylase from wheat (Triticum aestivum) onto DEAE-cellulose using response surface methodology and its characterization J. Mol. Catal. B: Enzym. 104 2014 75 81
    • (2014) J. Mol. Catal. B: Enzym. , vol.104 , pp. 75-81
    • Singh, K.1    Kayastha, A.M.2
  • 21
    • 84880050642 scopus 로고    scopus 로고
    • Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme
    • O.L. Tavano, R. Fernandez-Lafuente, A.J. Goulart, and R. Monti Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme Process Biochem. 48 2013 1054 1058
    • (2013) Process Biochem. , vol.48 , pp. 1054-1058
    • Tavano, O.L.1    Fernandez-Lafuente, R.2    Goulart, A.J.3    Monti, R.4
  • 22
    • 84904355892 scopus 로고    scopus 로고
    • Immobilization of thermostable α-amylase from Bacillus licheniformis by cross-linked enzyme aggregates method using calcium and sodium ions as additives
    • H. Torabizadeh, M. Tavakoli, and M. Safari Immobilization of thermostable α-amylase from Bacillus licheniformis by cross-linked enzyme aggregates method using calcium and sodium ions as additives J. Mol. Catal. B: Enzym. 108 2014 13 20
    • (2014) J. Mol. Catal. B: Enzym. , vol.108 , pp. 13-20
    • Torabizadeh, H.1    Tavakoli, M.2    Safari, M.3
  • 23
    • 84890925539 scopus 로고    scopus 로고
    • Enhanced stability and catalytic activity of immobilized α-amylase on modified Fe3O4 nanoparticles
    • N. Sohrabi, N. Rasouli, and M. Torkzadeh Enhanced stability and catalytic activity of immobilized α-amylase on modified Fe3O4 nanoparticles Chem. Eng. J. 240 2014 426 433
    • (2014) Chem. Eng. J. , vol.240 , pp. 426-433
    • Sohrabi, N.1    Rasouli, N.2    Torkzadeh, M.3
  • 24
    • 84904307695 scopus 로고    scopus 로고
    • New insights into the effectiveness of alpha-amylase enzyme presentation on the Bacillus subtilis spore surface by adsorption and covalent immobilization
    • F. Gashtasbi, G. Ahmadian, and K. Akbari Noghabi New insights into the effectiveness of alpha-amylase enzyme presentation on the Bacillus subtilis spore surface by adsorption and covalent immobilization Enzyme Microb. Technol. 64-65 2014 17 23
    • (2014) Enzyme Microb. Technol. , vol.64-65 , pp. 17-23
    • Gashtasbi, F.1    Ahmadian, G.2    Akbari Noghabi, K.3
  • 26
    • 33748037939 scopus 로고
    • Amylase α and β
    • P. Bernfeld Amylase α and β Methods Enzymol. 1 1955 149 151
    • (1955) Methods Enzymol. , vol.1 , pp. 149-151
    • Bernfeld, P.1
  • 27
    • 0020454937 scopus 로고
    • Mechanism of action of human pancreatic and salivary α-amylase on α-4-nitrophenyl maltoheptaoside substrate
    • E. Hagele, E. Schaich, P. Lehmann, H. Burk, and A.W. Wahlefeld Mechanism of action of human pancreatic and salivary α-amylase on α-4-nitrophenyl maltoheptaoside substrate Clin. Chem. 28 1982 2201 2205
    • (1982) Clin. Chem. , vol.28 , pp. 2201-2205
    • Hagele, E.1    Schaich, E.2    Lehmann, P.3    Burk, H.4    Wahlefeld, A.W.5
  • 28
    • 0000304044 scopus 로고
    • A new procedure for the measurement of fungal and bacterial α-amylase
    • H. Sheehan, and B.V. McCleary A new procedure for the measurement of fungal and bacterial α-amylase Biotechnol. Tech. 2 1988 289 292
    • (1988) Biotechnol. Tech. , vol.2 , pp. 289-292
    • Sheehan, H.1    McCleary, B.V.2
  • 29
    • 0000937143 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1968 48 254
    • (1968) Anal. Biochem. , vol.72 , pp. 48-254
    • Bradford, M.M.1
  • 32
    • 84883192484 scopus 로고    scopus 로고
    • Surface chemistry of gold nanorods: Origin of cell membrane damage and cytotoxicity
    • L. Wang, X. Jiang, Y. Ji, R. Bai, Y. Zhao, X. Wu, and C. Chen Surface chemistry of gold nanorods: origin of cell membrane damage and cytotoxicity Nanoscale 5 2013 8384 8391
    • (2013) Nanoscale , vol.5 , pp. 8384-8391
    • Wang, L.1    Jiang, X.2    Ji, Y.3    Bai, R.4    Zhao, Y.5    Wu, X.6    Chen, C.7
  • 33
    • 84896965053 scopus 로고    scopus 로고
    • Replacement of CTAB with peptidic ligands at the surface of gold nanorods and their self-assembling properties
    • C. Hamon, T. Bizien, F. Artzner, P. Even-Hernandez, and V. Marchi Replacement of CTAB with peptidic ligands at the surface of gold nanorods and their self-assembling properties J. Colloid Interface Sci. 424 2014 90 97
    • (2014) J. Colloid Interface Sci. , vol.424 , pp. 90-97
    • Hamon, C.1    Bizien, T.2    Artzner, F.3    Even-Hernandez, P.4    Marchi, V.5
  • 34
    • 84903700284 scopus 로고    scopus 로고
    • Improved enzyme immobilization for enhanced bioelectrocatalytic activity of choline sensor and acetylcholine sensor
    • L. Zhang, J. Chen, Y. Wang, L. Yu, J. Wang, H. Peng, and J. Zhu Improved enzyme immobilization for enhanced bioelectrocatalytic activity of choline sensor and acetylcholine sensor Sens. Actuators A 193 2014 904 910
    • (2014) Sens. Actuators A , vol.193 , pp. 904-910
    • Zhang, L.1    Chen, J.2    Wang, Y.3    Yu, L.4    Wang, J.5    Peng, H.6    Zhu, J.7
  • 35
    • 70350695954 scopus 로고    scopus 로고
    • Bioconjugates of glucose oxidase and gold nanorods based on electrostatic interaction with enhanced thermostability
    • Z. Ma, and T. Ding Bioconjugates of glucose oxidase and gold nanorods based on electrostatic interaction with enhanced thermostability Nanoscale Res. Lett. 4 2009 1236 1240
    • (2009) Nanoscale Res. Lett. , vol.4 , pp. 1236-1240
    • Ma, Z.1    Ding, T.2
  • 36
    • 84864859777 scopus 로고    scopus 로고
    • Functionalized gold nanoparticles and their biomedical applications
    • M.P. Tiwari, K. Vig, V.A. Dennis, and S.R. Singh Functionalized gold nanoparticles and their biomedical applications Nanomaterials 1 2011 31 63
    • (2011) Nanomaterials , vol.1 , pp. 31-63
    • Tiwari, M.P.1    Vig, K.2    Dennis, V.A.3    Singh, S.R.4
  • 37
    • 33745204216 scopus 로고    scopus 로고
    • Enzymatic activities of proteases immobilized on tri(4-formyl phenoxy) cyanurate
    • R.S. Rao, P.S. Borkar, C.N. Khobragade, and A.D. Sagar Enzymatic activities of proteases immobilized on tri(4-formyl phenoxy) cyanurate Enzyme Microb. Technol. 39 2006 958 962
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 958-962
    • Rao, R.S.1    Borkar, P.S.2    Khobragade, C.N.3    Sagar, A.D.4
  • 38
    • 84893822432 scopus 로고    scopus 로고
    • Gold nanorod-based localized surface plasmon resonance biosensors: A review
    • J. Cao, T. Sun, and K. Grattan Gold nanorod-based localized surface plasmon resonance biosensors: a review Sens. Actuators B: Chem. 195 2014 332 351
    • (2014) Sens. Actuators B: Chem. , vol.195 , pp. 332-351
    • Cao, J.1    Sun, T.2    Grattan, K.3
  • 39
    • 84873019414 scopus 로고    scopus 로고
    • Fabrication of horseradish peroxidase immobilized poly(N-[3-(trimethoxy silyl)propyl]aniline) gold nanorods film modified electrode and electrochemical hydrogen peroxide sensing
    • S. Komathi, A.I. Gopalan, S. Kim, G.S. Anand, and K. Lee Fabrication of horseradish peroxidase immobilized poly(N-[3-(trimethoxy silyl)propyl]aniline) gold nanorods film modified electrode and electrochemical hydrogen peroxide sensing Electrochim. Acta 92 2013 71 78
    • (2013) Electrochim. Acta , vol.92 , pp. 71-78
    • Komathi, S.1    Gopalan, A.I.2    Kim, S.3    Anand, G.S.4    Lee, K.5
  • 40
    • 84896890841 scopus 로고    scopus 로고
    • Improvement of thermal stability of enzyme via immobilization on Langmuir-Blodgett films of organo-modified aluminosilicate with high coverage
    • A. Fujimori, S. Arai, Y. Soutome, and M. Hashimoto Improvement of thermal stability of enzyme via immobilization on Langmuir-Blodgett films of organo-modified aluminosilicate with high coverage Colloids Surf. A 448 2014 45 52
    • (2014) Colloids Surf. A , vol.448 , pp. 45-52
    • Fujimori, A.1    Arai, S.2    Soutome, Y.3    Hashimoto, M.4
  • 42
    • 84923033139 scopus 로고    scopus 로고
    • Enhanced activity and stability of papain immobilized on CNBr-activated sepharose
    • A. Homaei Enhanced activity and stability of papain immobilized on CNBr-activated sepharose Int. J. Biol. Macromol. 75 2015 373 377
    • (2015) Int. J. Biol. Macromol. , vol.75 , pp. 373-377
    • Homaei, A.1
  • 43
    • 1642492905 scopus 로고    scopus 로고
    • α-Amylases of medical and industrial importance
    • L. Kandra α-Amylases of medical and industrial importance J. Mol. Struct. 666 2003 487 498
    • (2003) J. Mol. Struct. , vol.666 , pp. 487-498
    • Kandra, L.1
  • 46
    • 84903608856 scopus 로고    scopus 로고
    • Immobilized papain on gold nanorods as heterogeneous biocatalysts
    • A. Homaei, H. Barkheh, R. Sariri, and R. Stevanato Immobilized papain on gold nanorods as heterogeneous biocatalysts Amino Acids 46 2014 1649 1657
    • (2014) Amino Acids , vol.46 , pp. 1649-1657
    • Homaei, A.1    Barkheh, H.2    Sariri, R.3    Stevanato, R.4
  • 47
    • 84930505757 scopus 로고    scopus 로고
    • Purification and biochemical properties of highly efficient alkaline phosphatase from Fenneropenaeus merguiensis brain
    • A. Homaei Purification and biochemical properties of highly efficient alkaline phosphatase from Fenneropenaeus merguiensis brain J. Mol. Catal. B: Enzym. 118 2015 16 22
    • (2015) J. Mol. Catal. B: Enzym. , vol.118 , pp. 16-22
    • Homaei, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.