In vivo enzyme immobilization by inclusion body display

Applied and Environmental Microbiology

Volumn 76, Issue 16, 2010, Pages 5563-5569

  Steinmann, Björn ^a   Christmann, Andreas ^a   Heiseler, Tim ^a   Fritz, Janine ^a   Kolmar, Harald ^a  

^a DARMSTADT UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINUS; BIOPROCESSING; CO-EXPRESSION; COILED COIL; EXPRESSION IN ESCHERICHIA COLI; FUSARIUM; GALACTOSE OXIDASE; HELICAL COIL; HIGH LEVEL EXPRESSION; IN-VIVO; INCLUSION BODIES; MICRO-PARTICLES; NOVEL STRATEGIES; POLYHYDROXYBUTYRATE; POSITIVELY CHARGED; SYNTHASES;

AMINO ACIDS; CATALYSTS; CENTRIFUGATION; ENZYMES; ESCHERICHIA COLI;

ENZYME IMMOBILIZATION;

ACYLTRANSFERASE; GALACTOSE OXIDASE; IMMOBILIZED ENZYME; POLY(3-HYDROXYALKANOIC ACID) SYNTHASE; POLYHYDROXYALKANOATE SYNTHASE; RECOMBINANT PROTEIN;

BIOTRANSFORMATION; COLIFORM BACTERIUM; ENZYME ACTIVITY; EXPERIMENTAL STUDY; GENE EXPRESSION; GENETIC ENGINEERING; IMMOBILIZATION;

ARTICLE; BIOSYNTHESIS; CELL INCLUSION; CUPRIAVIDUS NECATOR; ENZYMOLOGY; ESCHERICHIA COLI; FUSARIUM; GENETICS; ISOLATION AND PURIFICATION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

ACYLTRANSFERASES; CUPRIAVIDUS NECATOR; ENZYMES, IMMOBILIZED; ESCHERICHIA COLI; FUSARIUM; GALACTOSE OXIDASE; INCLUSION BODIES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

CUPRIAVIDUS NECATOR; ESCHERICHIA COLI; FUSARIUM;

EID: 77955949629     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00612-10     Document Type: Article

References (36)

1. Atwood, J. A., andB. H. Rehm. 2009. Protein engineering towards biotechnological production of bifunctional polyester beads. Biotechnol. Lett. 31: 131-137.
2. Barnard, G. C., J. D. McCool, D. W. Wood, andT. U. Gerngross. 2005. Integrated recombinant protein expression and purification platform based on Rabtonia eutropha. Appl. Environ. Microbiol. 71:5735-5742.
3. Betscheider, D., andJ. Jose. 2009. Nile blue A for staining Escherichia coli in flow cytometer experiments. Anal. Biochem. 384:194-196.
4. Bowden, G. A., A. M. Paredes, andG. Georgiou. 1991. Structure and morphology of protein inclusion bodies in Escherichia coli. Biotechnology (NY) 9:725-730.
5. Carrio, M., N. Gonzalez-Montalban, A. Vera, A. Villaverde, andS. Ventura. 2005. Amyloid-like properties of bacterial inclusion bodies. J. Mol. Biol. 347:1025-1037.
6. Chao, H., D. L. Bautista, J. Litowski, R. T. Irvin, andR. S. Hodges. 1998. Use of a heterodimeric coiled-coil system for biosensor application and affinity purification. J. Chromatogr. B Biomed. Sci. Appl. 715:307-329.
7. Chen, R. R. Z. 2007. Permeability issues in whole-cell bioprocesses and cellular membrane engineering. Appl. Microbiol. Biotechnol. 74:730-738.
8. de Almeida, A., P. I. Nikel, A. M. Giordano, andM. J. Pettinari. 2007. Effects of granule-associated protein PhaP on glycerol-dependent growth and polymer production in poly(3-hydroxybutyrate)-producing Escherichia coli. Appl. Environ. Microbiol. 73:7912-7916.
9. Escalettes, F., andN. J. Turner. 2008. Directed evolution of galactose oxidase: generation of enantioselective secondary alcohol oxidases. Chembiochem 9:857-860.
10. Gillies, A. R., R. B. Mahmoud, andD. W. Wood. 2009. PHB-intein-mediated protein purification strategy. Methods Mol. Biol. 498:173-183.
11. Grage, K., A. C. Jahns, N. Parlane, R. Palanisamy, I. A. Rasiah, J. A. Atwood, andB. H. Rehm. 2009. Bacterial polyhydroxyalkanoate granules: biogenesis, structure, and potential use as nano/micro-beads in biotechnological and biomedical applications. Biomacromolecules 10:660-669.
12. Huisman, G. W., J. Liang, andA. Krebber. 2010. Practical chiral alcohol manufacture using ketoreductases. Curr. Opin. Chem. Biol. 14:122-129.
13. Ishige, T., K. Honda, andS. Shimizu. 2005. Whole organism biocatalysis. Curr. Opin. Chem. Biol. 9:174-180.
14. Meyer, H. P., andN. J. Turner. 2009. Biotechnological manufacturing options for organic chemistry. Mini-Rev. Org. Chem. 6:300-306.
15. Mifune, J., K. Grage, andB. H. Rehm. 2009. Production of functionalized biopolyester granules by recombinant Lactococcus lactis. Appl. Environ. Microbiol. 75:4668-4675.
16. Moldes, C., P. Garcia, J. L. Garcia, andM. A. Prieto. 2004. In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF. Appl. Environ. Microbiol. 70:3205-3212.
17. Parlane, N. A., D. N. Wedlock, B. M. Buddle, andB. H. Rehm. 2009. Bacterial polyester inclusions engineered to display vaccine candidate antigens for use as a novel class of safe and efficient vaccine delivery agents. Appl. Environ. Microbiol. 75:7739-7744.
18. Peters, V., D. Becher, andB. H. Rehm. 2007. The inherent property of polyhydroxyalkanoate synthase to form spherical PHA granules at the cell poles: the core region is required for polar localization. J. Biotechnol. 132: 238-245.
19. Peters, V., andB. H. Rehm. 2006. In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase. Appl. Environ. Microbiol. 72: 1777-1783.
20. Potter, M., H. Muller, F. Reinecke, R. Wieczorek, F. Fricke, B. Bowien, B. Friedrich, andA. Steinbuchel. 2004. The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha. Microbiology 150:2301-2311.
21. Rehm, B. H. 2007. Biogenesis of microbial polyhydroxyalkanoate granules: a platform technology for the production of tailor-made bioparticles. Curr. Issues Mol. Biol. 9:41-62.
22. Rehm, B. H., R. V. Antonio, P. Spiekermann, A. A. Amara, andA. Steinbuchel. 2002. Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: in vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model. Biochim. Biophys. Acta 1594:178-190.
23. Sheldon, R. A. 2007. Enzyme immobilization: the quest for optimum performance. Adv. Synth. Catal. 349:1289-1307.
24. Skerra, A. 1994. Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene 151: 131-135.
25. Spiekermann, P., B. H. A. Rehm, R. Kalscheuer, D. Baumeister, andA. Steinbuchel. 1999. A sensitive, viable-colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds. Arch. Microbiol. 171:73-80.
26. Studier, F. W., andB. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
27. Sun, L. H., T. Bulter, M. Alcalde, I. P. Petrounia, andF. H. Arnold. 2002. Modification of galactose oxidase to introduce glucose 6-oxidase activity. Chembiochem 3:781-783.
28. Sun, L. H., I. P. Petrounia, M. Yagasaki, G. Bandara, andF. H. Arnold. 2001. Expression and stabilization of galactose oxidase in Escherichia coli by directed evolution. Protein Eng. 14:699-704.
29. Tripet, B., L. Yu, D. L. Bautista, W. Y. Wong, R. T. Irvin, andR. S. Hodges. 1996. Engineering a de novo-designed coiled-coil heterodimerization domain off the rapid detection, purification and characterization of recombinantly expressed peptides and proteins. Protein Eng. 9:1029-1042.
30. Turner, N. J. 2009. Directed evolution drives the next generation of biocatalysts. Nat. Chem. Biol. 5:567-573.
31. Valentin, H. E., andA. Steinbuchel. 1994. Application of enzymatically synthesized short-chain-length hydroxy fatty acid coenzyme A thioesters for assay of polyhydroxyalkanoic acid synthases. Appl. Microbiol. Biotechnol. 40:699-709.
32. Wang, L., S. K. Maji, M. R. Sawaya, D. Eisenberg, andR. Riek. 2008. Bacterial inclusion bodies contain amyloid-like structure. PLoS Biol. 6:1791-1801.
33. Wasmer, C., L. Benkemoun, R. Sabate, M. O. Steinmetz, B. Coulary-Salin, L. Wang, R. Riek, S. J. Saupe, andB. H. Meier. 2009. Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids. Angew. Chem. Int. Ed. Engl. 48:4858-4860.
34. Wentzel, A., A. Christmann, T. Adams, andH. Kolmar. 2001. Display of passenger proteins on the surface oí Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA. J. Bacteriol. 183:7273-7284.
35. Wohlgemuth, R. 2009. The locks and keys to industrial biotechnology. New Biotechnol. 25:204-213.
36. Zhou, N. E., C. M. Kay, andR. S. Hodges. 1993. Disulfide bond contribution to protein stability: positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil. Biochemistry 32:3178-3187.