A magnetically separable, highly stable enzyme system based on nanocomposites of enzymes and magnetic nanoparticles shipped in hierarchically ordered, mesocellular, mesoporous silica

被引:101
作者
Kim, J [1 ]
Lee, J
Na, HB
Kim, BC
Youn, JK
Kwak, JH
Moon, K
Lee, E
Kim, J [1 ]
Park, J
Dohnalkova, A
Park, HG
Gu, MB
Chang, HN
Grate, JW
Hyeon, T
机构
[1] Pacific NW Natl Lab, Richland, WA 99352 USA
[2] Seoul Natl Univ, Natl Creat Res Initiat Ctr Oxide Nanocrystalline, Seoul 151744, South Korea
[3] Seoul Natl Univ, Sch Chem & Biol Engn, Seoul 151744, South Korea
[4] Gwangju Inst Sci & Technol, Adv Environm Monitoring Res Ctr, Kwangju 500712, South Korea
[5] Korea Adv Inst Sci & Technol, Dept Chem & Biomol Engn, Taejon 305701, South Korea
[6] Korea Univ, Grad Sch Biotechnol, Seoul 136701, South Korea
关键词
enzyme catalysis; magnetic nanoparticles; magnetic separation; mesoporous materials; silica;
D O I
10.1002/smll.200500245
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The development of a magnetically separable and highly stable enzyme system, using nanoparticles and mesoporous silica, was investigated. Nanometer-scale composites of enzyme molecules and hierarchically ordered magnetite nanoparticles were immobilized via a ship-in-a-bottle approach, which used co-adsorption of enzymes and magnetite (Fe3O4) nanoparticles. The enzyme molecules were crosslinked via glutaraldehyde (GA) treatment resulting in the effective entrapment of neighboring magnetite nanoparticles. These nanocomposites, called M-CLEAs, were found magnetically separable, highly loaded with enzymes, stable under harsh conditions, resistant to proteolytic digestion, and recyclable for iterative use with negligible loss of enzyme activity. The ship-in-a-bottle approach can be expanded to many other enzymes and has applications in bioremediation and bioconversion.
引用
收藏
页码:1203 / 1207
页数:5
相关论文
共 46 条
[1]   Utilization of enzymes for environmental applications [J].
Ahuja, SK ;
Ferreira, GM ;
Moreira, AR .
CRITICAL REVIEWS IN BIOTECHNOLOGY, 2004, 24 (2-3) :125-154
[2]  
[Anonymous], 2003, ANGEW CHEM
[3]   The search for the ideal biocatalyst [J].
Burton, SG ;
Cowan, DA ;
Woodley, JM .
NATURE BIOTECHNOLOGY, 2002, 20 (01) :37-45
[4]   Mechanistic and structural features of protein adsorption onto mesoporous silicates [J].
Deere, J ;
Magner, E ;
Wall, JG ;
Hodnett, BK .
JOURNAL OF PHYSICAL CHEMISTRY B, 2002, 106 (29) :7340-7347
[5]   Enzyme immobilization in MCM-41 molecular sieve [J].
Diaz, JF ;
Balkus, KJ .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 1996, 2 (2-3) :115-126
[6]   Unprecedented crystalline super-lattices of monodisperse cobalt nanorods [J].
Dumestre, F ;
Chaudret, B ;
Amiens, C ;
Respaud, M ;
Fejes, P ;
Renaud, P ;
Zurcher, P .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2003, 42 (42) :5213-5216
[7]  
DUMESTRE F, 2003, ANGEW CHEM, V115, P5371
[8]   Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment:: a review [J].
Durán, N ;
Esposito, E .
APPLIED CATALYSIS B-ENVIRONMENTAL, 2000, 28 (02) :83-99
[9]   Activity of Candida rugosa lipase immobilized on γ-Fe2O3 magnetic nanoparticles [J].
Dyal, A ;
Loos, K ;
Noto, M ;
Chang, SW ;
Spagnoli, C ;
Shafi, KVPM ;
Ulman, A ;
Cowman, M ;
Gross, RA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (07) :1684-1685
[10]   Cubic mesoporous silica with large controllable entrance sizes and advanced adsorption properties [J].
Fan, J ;
Yu, CZ ;
Gao, T ;
Lei, J ;
Tian, BZ ;
Wang, LM ;
Luo, Q ;
Tu, B ;
Zhou, WZ ;
Zhao, DY .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2003, 42 (27) :3146-3150