Expression of a lipase on the cell-surface of Escherichia coli using the OmpW anchoring motif and its application to enantioselective reactions

Biotechnology Letters

Volumn 35, Issue 10, 2013, Pages 1677-1683

  Lee, Hyuk ^a   Park, Si Jae ^b   Han, Mee Jung ^c   Eom, Gyeong Tae ^d   Choi, Min Jung ^a   Kim, Seong Ho ^a   Oh, Young Hoon ^a   Song, Bong Keun ^a   Lee, Seung Hwan ^a  

^a Korea Research Institute of Chemical Technology   (South Korea)

^b Myong Ji University   (South Korea)

^c Dongyang University   (South Korea)

^d Samsung Advanced Institute of Technology (SAIT)   (South Korea)

Author keywords

Cell surface display; Enantioselective biocatalyst; Lipase; Outer membrane protein

Indexed keywords

CELL SURFACE DISPLAYS; ENANTIOMERIC EXCESS; ENANTIOSELECTIVE; ENANTIOSELECTIVE HYDROLYSIS; ENANTIOSELECTIVE REACTIONS; FUNCTIONAL EXPRESSION; OUTER MEMBRANE PROTEIN; PSEUDOMONAS FLUORESCENCE;

BIOLOGICAL MEMBRANES; BIOSYNTHESIS; CELLS; CYTOLOGY; ENANTIOSELECTIVITY; ESCHERICHIA COLI; LIPASES;

PROTEINS;

BUTYRIC ACID DERIVATIVE; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; OMPW PROTEIN, E COLI; OUTER MEMBRANE PROTEIN; PHENETHYL ALCOHOL; TRIACYLGLYCEROL LIPASE;

ARTICLE; BIOSYNTHESIS; CELL SURFACE DISPLAY; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; IMMUNOBLOTTING; METABOLISM; METHODOLOGY; MOLECULAR WEIGHT; PSEUDOMONAS;

BACTERIAL OUTER MEMBRANE PROTEINS; BUTYRATES; CELL SURFACE DISPLAY TECHNIQUES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION; IMMUNOBLOTTING; LIPASE; MOLECULAR WEIGHT; PHENYLETHYL ALCOHOL; PSEUDOMONAS; RECOMBINANT FUSION PROTEINS;

EID: 84884811154     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-013-1260-0     Document Type: Article

References (23)

1. Ahn JH, Pan JG, Rhee JS (1999) Identification of the tliDEF ABC transporter specific for lipase in Pseudomonas fluorescens SIK W1. J Bacteriol 181: 1847-1852.
2. Asakura H, Kawamoto K, Haishima Y, Igimi S, Yamamoto S, Makino S (2008) Differential expression of the outer membrane protein W (OmpW) stress response in enterohemorrhagic Escherichia coli O157: H7 corresponds to the viable but non-culturable state. Res Microbiol 159: 709-717.
3. Benhar I (2001) Biotechnological application of phage and cell display. Biotechnol Adv 19: 1-33.
4. Blattner FR, Plunkett G, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode K, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y (1997) The complete genome sequence of Escherichia coli K-12. Science 277: 1453-1462.
5. Chen CS, Fujimoto Y, Girdaukas G, Sih CJ (1982) Quantitative analyses of biochemical kinetic resolutions of enantiomers. J Am Chem Soc 104: 7294-7299.
6. Georgiou G, Stathopoulos C, Daugherty PS, Nayak AR, Iverson BL, Curtiss R 3rd (1997) Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat Biotechnol 15: 29-34.
7. Hong H, Patel DR, Tamm LK, van den Berg B (2006) The outer membrane protein ompW forms an eight-stranded beta-barrel with a hydrophobic channel. J Biol Chem 281: 7568-7577.
8. Jung HC, Lebeault JM, Pan JG (1998) Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae. Nat Biotechnol 16: 576-580.
9. Kazlauskas RJ, Weissfloch ANE, Rappaport AT, Cuccia LA (1991) A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa. J Org Chem 56: 2656-2665.
10. Kondo A, Ueda M (2004) Yeast cell-surface display-applications of molecular display. Appl Microbiol Biotechnol 64: 28-40.
11. Kuroda K, Ueda M (2011) Cell-surface engineering of yeast for applications in white biotechnology. Biotechnol Lett 33: 1-9.
12. Lee SY, Choi JH, Xu Z (2003) Microbial cell-surface display. Trends Biotechnol 21: 45-52.
13. Lee SH, Choi JI, Park SJ, Lee SY, Park BC (2004) Display of bacterial lipase on the Escherichia coli cell-surface by using FadL as an anchoring motif and its use in enantioselective biocatalysis. Appl Environ Microbiol 70: 5074-5080.
14. Lee SH, Lee SY, Park BC (2005) Cell-surface display of lipase in Pseudomonas putida KT2442 using OprF as an anchoring motif and its biocatalytic applications. Appl Environ Microbiol 71: 8581-8586.
15. Lee JY, Sung BH, Yu BJ, Lee JH, Lee SH, Kim MS, Koob MD, Kim SC (2008) Phenotypic engineering by reprogramming gene transcription using novel artificial transcription factors in Escherichia coli. Nucleic Acids Res 36: e102.
16. Matsumoto T, Ito M, Fukuda H, Kondo A (2004) Enantioselective transesterification using lipase-displaying yeast whole-cell biocatalyst. Appl Microbiol Biotechnol 64: 481-485.
17. Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656.
18. Park S, Kazlauskas RJ (2001) Improved preparation and use of room-temperature ionic liquids in lipase-catalyzed enantio- and regioselective acylations. J Org Chem 66: 8395-8401.
19. Pilsl H, Smajs D, Braun V (1999) Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane. J Bacteriol 181: 3578-3581.
20. Shimazu M, Nuyen A, Mulchandani A, Chen W (2003) Cell-surface display of organophosphorus hydrolase in Pseudomonas putida using ice nucleation protein anchor. Biotechnol Prog 19: 1612-1614.
21. Tanaka T, Yamada R, Ogino C, Kondo A (2012) Recent developments in yeast cell-surface display toward extended applications in biotechnology. Appl Microbiol Biotechnol 95: 577-591.
22. van Bloois E, Winter RT, Kolmar H, Fraaije MW (2011) Decorating microbes: surface display of proteins on Escherichia coli. Trends Biotechnol 29: 79-86.
23. Wu L, Lin X, Peng X (2009) From proteome to genome for functional characterization of pH-dependent outer membrane proteins in Escherichia coli. J Proteome Res 8: 1059-1070.