Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins -: art. no. 27

被引:247
作者
García-Fruitós, E
González-Montalbán, N
Morell, M
Vera, A
Ferraz, RM
Arís, A
Ventura, S
Villaverde, A [1 ]
机构
[1] Univ Autonoma Barcelona, Inst Biotecnol & Biomed, E-08193 Barcelona, Spain
[2] Univ Autonoma Barcelona, Dept Genet & Microbiol, E-08193 Barcelona, Spain
[3] Univ Autonoma Barcelona, Dept Bioquim & Biol Mol, E-08193 Barcelona, Spain
关键词
D O I
10.1186/1475-2859-4-27
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Background: Many enzymes of industrial interest are not in the market since they are bio-produced as bacterial inclusion bodies, believed to be biologically inert aggregates of insoluble protein. Results: By using two structurally and functionally different model enzymes and two fluorescent proteins we show that physiological aggregation in bacteria might only result in a moderate loss of biological activity and that inclusion bodies can be used in reaction mixtures for efficient catalysis. Conclusion: This observation offers promising possibilities for the exploration of inclusion bodies as catalysts for industrial purposes, without any previous protein-refolding step.
引用
收藏
页数:6
相关论文
共 28 条
[1]   Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy [J].
Ami, D ;
Natalello, A ;
Gatti-Lafranconi, P ;
Lotti, M ;
Doglia, SM .
FEBS LETTERS, 2005, 579 (16) :3433-3436
[2]   Recombinant protein folding and misfolding in Escherichia coli [J].
Baneyx, F ;
Mujacic, M .
NATURE BIOTECHNOLOGY, 2004, 22 (11) :1399-1408
[3]  
Baneyx Francois, 2003, Methods Mol Biol, V205, P171
[4]   Amyloid-like properties of bacterial inclusion bodies [J].
Carrió, M ;
González-Montalbán, N ;
Vera, A ;
Villaverde, A ;
Ventura, S .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (05) :1025-1037
[5]   Protein aggregation as bacterial inclusion bodies is reversible [J].
Carrió, MM ;
Villaverde, A .
FEBS LETTERS, 2001, 489 (01) :29-33
[6]   Fine architecture of bacterial inclusion bodies [J].
Carrió, MM ;
Cubarsi, R ;
Villaverde, A .
FEBS LETTERS, 2000, 471 (01) :7-11
[7]  
Cazorla D, 2001, BIOTECHNOL BIOENG, V72, P255, DOI 10.1002/1097-0290(20010205)72:3<255::AID-BIT1>3.0.CO
[8]  
2-#
[9]   Kinetic partitioning of protein folding and aggregation [J].
Chiti, F ;
Taddei, N ;
Baroni, F ;
Capanni, C ;
Stefani, M ;
Ramponi, G ;
Dobson, CM .
NATURE STRUCTURAL BIOLOGY, 2002, 9 (02) :137-143
[10]   CRYSTAL-STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE-REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZAFOLATE [J].
DAVIES, JF ;
DELCAMP, TJ ;
PRENDERGAST, NJ ;
ASHFORD, VA ;
FREISHEIM, JH ;
KRAUT, J .
BIOCHEMISTRY, 1990, 29 (40) :9467-9479