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Volumn 123, Issue , 2012, Pages 542-547

Novel magnetic cross-linked enzyme aggregates (magnetic CLEAs) of alpha amylase

Author keywords

Alpha amylase; Amino functionalized magnetite nanoparticles; Immobilization; Magnetic cross linked enzyme aggregates

Indexed keywords

ALPHA AMYLASE; ALPHA-AMYLASE ACTIVITY; CHEMICAL CROSS-LINKING; CROSS-LINKED ENZYME AGGREGATES; FREE ENZYME; FUNCTIONALIZED; INITIAL ACTIVITY; OPTIMAL TEMPERATURE; REACTION MIXTURE; SCANNING ELECTRONS; SPHERICAL STRUCTURES; STORAGE STABILITY; SUBSTRATE AFFINITY;

EID: 84865536720     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2012.07.044     Document Type: Article
Times cited : (233)

References (33)
  • 1
    • 38049085641 scopus 로고    scopus 로고
    • Preparation of cross-linked tyrosinase aggregates
    • Aytar B.S., Bakir U. Preparation of cross-linked tyrosinase aggregates. Process Biochem. 2008, 43:125-131.
    • (2008) Process Biochem. , vol.43 , pp. 125-131
    • Aytar, B.S.1    Bakir, U.2
  • 2
    • 34848883383 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals
    • Cabana H., Jones J.P., Agathos S.N. Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. J. Biotechnol. 2007, 132:23-31.
    • (2007) J. Biotechnol. , vol.132 , pp. 23-31
    • Cabana, H.1    Jones, J.P.2    Agathos, S.N.3
  • 3
    • 84860591460 scopus 로고    scopus 로고
    • Optimized preparation of CALB-CLEAs by response surface methodology: The necessity to employ a feeder to have an effective cross-linking
    • Cruz J., Barbosa O., Rodrigues R.C., Fernandez-Lafuentec R., Torres R., Ortiz C. Optimized preparation of CALB-CLEAs by response surface methodology: The necessity to employ a feeder to have an effective cross-linking. J. Mol. Catal. B: Enzym. 2012, 80:7-14.
    • (2012) J. Mol. Catal. B: Enzym. , vol.80 , pp. 7-14
    • Cruz, J.1    Barbosa, O.2    Rodrigues, R.C.3    Fernandez-Lafuentec, R.4    Torres, R.5    Ortiz, C.6
  • 4
    • 33846489558 scopus 로고    scopus 로고
    • Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions
    • Dalal S., Kapoor M., Gupta M.N. Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions. J. Mol. Catal. B: Enzym. 2007, 44:128-132.
    • (2007) J. Mol. Catal. B: Enzym. , vol.44 , pp. 128-132
    • Dalal, S.1    Kapoor, M.2    Gupta, M.N.3
  • 5
    • 0003751067 scopus 로고
    • Worthington Biochemical Corp, Freehold NJ
    • Dekker L.A. Worthington Enzyme Manual 1977, Worthington Biochemical Corp, Freehold NJ, p. 173.
    • (1977) Worthington Enzyme Manual , pp. 173
    • Dekker, L.A.1
  • 6
    • 77955496659 scopus 로고    scopus 로고
    • Preparation of cross-linked aggregates of aminoacylase from Aspergillus melleus by using bovine serum albumin as an inert additive
    • Dong T., Zhao L., Huang Y., Tan X. Preparation of cross-linked aggregates of aminoacylase from Aspergillus melleus by using bovine serum albumin as an inert additive. Bioresour. Technol. 2010, 101:6569-6571.
    • (2010) Bioresour. Technol. , vol.101 , pp. 6569-6571
    • Dong, T.1    Zhao, L.2    Huang, Y.3    Tan, X.4
  • 8
    • 67349234081 scopus 로고    scopus 로고
    • Characterization of cross-linked immobilized lipase from thermophilic mould Thermomyces lanuginosa using glutaraldehyde
    • Gupta P., Dutt K., Misra S., Raghuwanshi S., Saxena R.K. Characterization of cross-linked immobilized lipase from thermophilic mould Thermomyces lanuginosa using glutaraldehyde. Bioresour. Technol. 2009, 100:4074-4076.
    • (2009) Bioresour. Technol. , vol.100 , pp. 4074-4076
    • Gupta, P.1    Dutt, K.2    Misra, S.3    Raghuwanshi, S.4    Saxena, R.K.5
  • 9
    • 33750524054 scopus 로고    scopus 로고
    • Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface
    • Honda T., Miyazaki M., Nakamura H., Maeda H. Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface. Adv. Synth. Catal. 2006, 348:2163-2171.
    • (2006) Adv. Synth. Catal. , vol.348 , pp. 2163-2171
    • Honda, T.1    Miyazaki, M.2    Nakamura, H.3    Maeda, H.4
  • 10
    • 84861456071 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates (CLEAs) of recombinant poly-3-hydroxybutyrate depolymerase from Streptomyces exfoliates
    • Hormigo D., García-Hidalgo J., Acebal C., de la Mata I., Arroyo M. Preparation and characterization of cross-linked enzyme aggregates (CLEAs) of recombinant poly-3-hydroxybutyrate depolymerase from Streptomyces exfoliates. Bioresour. Technol. 2012, 115:177-182.
    • (2012) Bioresour. Technol. , vol.115 , pp. 177-182
    • Hormigo, D.1    García-Hidalgo, J.2    Acebal, C.3    de la Mata, I.4    Arroyo, M.5
  • 11
    • 67650257448 scopus 로고    scopus 로고
    • Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate
    • Hu B., Pan J., Yu H.-L., Liu J.-W., Xu J.-H. Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate. Process Biochem. 2009, 44:1019-1024.
    • (2009) Process Biochem. , vol.44 , pp. 1019-1024
    • Hu, B.1    Pan, J.2    Yu, H.-L.3    Liu, J.-W.4    Xu, J.-H.5
  • 12
    • 79957992187 scopus 로고    scopus 로고
    • Hen egg white as a feeder protein for lipase immobilization
    • Karimpil J.J., Melo J.S., D'Souza S.F. Hen egg white as a feeder protein for lipase immobilization. J. Mol. Catal. B: Enzym. 2011, 71:113-118.
    • (2011) J. Mol. Catal. B: Enzym. , vol.71 , pp. 113-118
    • Karimpil, J.J.1    Melo, J.S.2    D'Souza, S.F.3
  • 13
    • 78649906228 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis
    • Kumar S., Mohan U., Kamble A.L., Pawar S., Banerjee U.C. Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis. Bioresour. Technol. 2010, 101:6856-6858.
    • (2010) Bioresour. Technol. , vol.101 , pp. 6856-6858
    • Kumar, S.1    Mohan, U.2    Kamble, A.L.3    Pawar, S.4    Banerjee, U.C.5
  • 14
    • 22944441316 scopus 로고    scopus 로고
    • Co-aggregation of enzymes and polyethyleneimine: a simple method to prepare stable and immobilized derivatives of glutaryl acylase
    • Lopez-Gallego F., Betancor L., Hidalgo A., Alonso N., Fernandez-Lafuente R., Guisan J.M. Co-aggregation of enzymes and polyethyleneimine: a simple method to prepare stable and immobilized derivatives of glutaryl acylase. Biomacromolecules 2005, 6:1839-1842.
    • (2005) Biomacromolecules , vol.6 , pp. 1839-1842
    • Lopez-Gallego, F.1    Betancor, L.2    Hidalgo, A.3    Alonso, N.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 15
    • 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, 31:725-729.
    • (1959) Anal. Chem. , vol.31 , pp. 725-729
    • Miller, G.L.1
  • 17
    • 78651379960 scopus 로고    scopus 로고
    • Cross-linking of enzyme coaggregate with polyethyleneimine: a simple and promising method for preparing stable biocatalyst of Serratia marcescens lipase
    • Pan J., Kong X.-D., Li C.-X., Ye Q., Xu J.-H., Imanaka T. Cross-linking of enzyme coaggregate with polyethyleneimine: a simple and promising method for preparing stable biocatalyst of Serratia marcescens lipase. J. Mol. Catal. B: Enzym. 2011, 68:256-261.
    • (2011) J. Mol. Catal. B: Enzym. , vol.68 , pp. 256-261
    • Pan, J.1    Kong, X.-D.2    Li, C.-X.3    Ye, Q.4    Xu, J.-H.5    Imanaka, T.6
  • 18
    • 71249098174 scopus 로고    scopus 로고
    • Immobilization of the cross-linked para-nitrobenzyl esterase of Bacillus subtilis aggregates onto magnetic beads
    • Park J.-M., Kim M., Park J.-Y., Lee D.-H., Lee K.-H., Min J., Kim Y.-H. Immobilization of the cross-linked para-nitrobenzyl esterase of Bacillus subtilis aggregates onto magnetic beads. Process Biochem. 2010, 45:259-263.
    • (2010) Process Biochem. , vol.45 , pp. 259-263
    • Park, J.-M.1    Kim, M.2    Park, J.-Y.3    Lee, D.-H.4    Lee, K.-H.5    Min, J.6    Kim, Y.-H.7
  • 20
    • 56049101154 scopus 로고    scopus 로고
    • Preparation and application of cross-linked aggregates of chloroperoxidase with enhanced hydrogen peroxide tolerance
    • Roberge C., Amos D., Pollard D., Devine D. Preparation and application of cross-linked aggregates of chloroperoxidase with enhanced hydrogen peroxide tolerance. J. Mol. Catal. B: Enzym. 2009, 56:41-45.
    • (2009) J. Mol. Catal. B: Enzym. , vol.56 , pp. 41-45
    • Roberge, C.1    Amos, D.2    Pollard, D.3    Devine, D.4
  • 21
    • 50049088751 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications
    • Sangeetha K., Abraham T.E. Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications. Int. J. Biol. Macromol. 2008, 43:314-319.
    • (2008) Int. J. Biol. Macromol. , vol.43 , pp. 314-319
    • Sangeetha, K.1    Abraham, T.E.2
  • 23
    • 33645298457 scopus 로고    scopus 로고
    • Preparation of cross-linked enzyme aggregates by using bovine serum albumin as a protein feeder
    • Shah S., Sharma A., Gupta M.N. Preparation of cross-linked enzyme aggregates by using bovine serum albumin as a protein feeder. Anal. Biochem. 2006, 351:207-213.
    • (2006) Anal. Biochem. , vol.351 , pp. 207-213
    • Shah, S.1    Sharma, A.2    Gupta, M.N.3
  • 24
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: the quest for optimum performance
    • Sheldon R.A. Enzyme immobilization: the quest for optimum performance. Adv. Synth. Catal. 2007, 349:1289-1307.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 25
    • 79251469073 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates as industrial biocatalysts
    • Sheldon R.A. Cross-linked enzyme aggregates as industrial biocatalysts. Org. Process Res. Develop. 2011, 15:213-223.
    • (2011) Org. Process Res. Develop. , vol.15 , pp. 213-223
    • Sheldon, R.A.1
  • 26
    • 0020691269 scopus 로고
    • Amino acid sequence of α-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene
    • Takkinen K., Pettersson R.F., Kalkkinen N., Palva I., Soderlund H., Kaariainen L. Amino acid sequence of α-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J. Biol. Chem. 1983, 258:1007-1013.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1007-1013
    • Takkinen, K.1    Pettersson, R.F.2    Kalkkinen, N.3    Palva, I.4    Soderlund, H.5    Kaariainen, L.6
  • 27
    • 82755197063 scopus 로고    scopus 로고
    • Preparation of cross-linked enzyme aggregates of l-aminoacylase via co-aggregation with polyethyleneimine
    • Vaidya B.K., Kuwar S.S., Golegaonkar S.B., Nene S.N. Preparation of cross-linked enzyme aggregates of l-aminoacylase via co-aggregation with polyethyleneimine. J. Mol. Catal. B: Enzym. 2012, 74:184-191.
    • (2012) J. Mol. Catal. B: Enzym. , vol.74 , pp. 184-191
    • Vaidya, B.K.1    Kuwar, S.S.2    Golegaonkar, S.B.3    Nene, S.N.4
  • 28
    • 13444287971 scopus 로고    scopus 로고
    • Cross-linked aggregates of (R)-oxynitrilase: a stable, recyclable biocatalyst for enantioselective hydrocyanation
    • van Langen L.M., Selassa R.P., van Rantwijk F., Sheldon R.A. Cross-linked aggregates of (R)-oxynitrilase: a stable, recyclable biocatalyst for enantioselective hydrocyanation. Org. Lett. 2005, 7:327-329.
    • (2005) Org. Lett. , vol.7 , pp. 327-329
    • van Langen, L.M.1    Selassa, R.P.2    van Rantwijk, F.3    Sheldon, R.A.4
  • 29
    • 77957958242 scopus 로고    scopus 로고
    • Cross-linking enzyme aggregates in the macropores of silica gel: a practical and efficient method for enzyme stabilization
    • Wang M., Qi W., Yu Q., Su R., He Z. Cross-linking enzyme aggregates in the macropores of silica gel: a practical and efficient method for enzyme stabilization. Biochem. Eng. J. 2010, 52:168-174.
    • (2010) Biochem. Eng. J. , vol.52 , pp. 168-174
    • Wang, M.1    Qi, W.2    Yu, Q.3    Su, R.4    He, Z.5
  • 30
    • 78650817240 scopus 로고    scopus 로고
    • Porous-CLEAs of papain: application to enzymatic hydrolysis of macromolecules
    • Wang M., Jia C., Qi W., Yu Q., Peng X., Su R., He Z. Porous-CLEAs of papain: application to enzymatic hydrolysis of macromolecules. Bioresour. Technol. 2011, 102:3541-3545.
    • (2011) Bioresour. Technol. , vol.102 , pp. 3541-3545
    • Wang, M.1    Jia, C.2    Qi, W.3    Yu, Q.4    Peng, X.5    Su, R.6    He, Z.7
  • 31
    • 2542579376 scopus 로고    scopus 로고
    • Co-aggregation of penicillin G acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media
    • Wilson L., Illanes A., Abian O., Pessela B.C.C., Fernandez-Lafuente R., Guisan J.M. Co-aggregation of penicillin G acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media. Biomacromolecules 2005, 5:852-857.
    • (2005) Biomacromolecules , vol.5 , pp. 852-857
    • Wilson, L.1    Illanes, A.2    Abian, O.3    Pessela, B.C.C.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 32
    • 80052984019 scopus 로고    scopus 로고
    • Poly-lysine supported cross-linked enzyme aggregates with efficient enzymatic activity and high operational stability
    • Yamaguchi H., Miyazaki M., Asanomi Y., Maeda H. Poly-lysine supported cross-linked enzyme aggregates with efficient enzymatic activity and high operational stability. Catal. Sci. Technol. 2011, 1:1256-1261.
    • (2011) Catal. Sci. Technol. , vol.1 , pp. 1256-1261
    • Yamaguchi, H.1    Miyazaki, M.2    Asanomi, Y.3    Maeda, H.4
  • 33
    • 44649189336 scopus 로고    scopus 로고
    • Resolution of N-(2-ethyl-6-methylphenyl)alanine via cross-linked aggregates of Pseudomonas sp. lipase
    • Zhao L.F., Zheng L.Y., Gao G., Ha F., Cao S.G. Resolution of N-(2-ethyl-6-methylphenyl)alanine via cross-linked aggregates of Pseudomonas sp. lipase. J. Mol. Catal. B: Enzym. 2008, 54:7-12.
    • (2008) J. Mol. Catal. B: Enzym. , vol.54 , pp. 7-12
    • Zhao, L.F.1    Zheng, L.Y.2    Gao, G.3    Ha, F.4    Cao, S.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.