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

被引:245
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.
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页数:6
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共 28 条
  • [1] Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    Ami, D
    Natalello, A
    Gatti-Lafranconi, P
    Lotti, M
    Doglia, SM
    [J]. FEBS LETTERS, 2005, 579 (16): : 3433 - 3436
  • [2] Recombinant protein folding and misfolding in Escherichia coli
    Baneyx, F
    Mujacic, M
    [J]. NATURE BIOTECHNOLOGY, 2004, 22 (11) : 1399 - 1408
  • [3] Baneyx Francois, 2003, Methods Mol Biol, V205, P171
  • [4] Amyloid-like properties of bacterial inclusion bodies
    Carrió, M
    González-Montalbán, N
    Vera, A
    Villaverde, A
    Ventura, S
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (05) : 1025 - 1037
  • [5] Protein aggregation as bacterial inclusion bodies is reversible
    Carrió, MM
    Villaverde, A
    [J]. FEBS LETTERS, 2001, 489 (01) : 29 - 33
  • [6] Fine architecture of bacterial inclusion bodies
    Carrió, MM
    Cubarsi, R
    Villaverde, A
    [J]. 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
    Chiti, F
    Taddei, N
    Baroni, F
    Capanni, C
    Stefani, M
    Ramponi, G
    Dobson, CM
    [J]. NATURE STRUCTURAL BIOLOGY, 2002, 9 (02) : 137 - 143
  • [10] CRYSTAL-STRUCTURES OF RECOMBINANT HUMAN DIHYDROFOLATE-REDUCTASE COMPLEXED WITH FOLATE AND 5-DEAZAFOLATE
    DAVIES, JF
    DELCAMP, TJ
    PRENDERGAST, NJ
    ASHFORD, VA
    FREISHEIM, JH
    KRAUT, J
    [J]. BIOCHEMISTRY, 1990, 29 (40) : 9467 - 9479