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ISRN Botany
Volume 2012 (2012), Article ID 173954, 16 pages
http://dx.doi.org/10.5402/2012/173954
Review Article

Integral Proteins in Plant Oil Bodies

Graduate Institute of Biotechnology, National Chung Hsing University, Taichung 402, Taiwan

Received 11 September 2012; Accepted 3 October 2012

Academic Editors: G. T. Maatooq and Y. Yamauchi

Copyright © 2012 Jason T. C. Tzen. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. V. Ibl and E. Stoger, “The formation, function and fate of protein storage compartments in seeds,” Protoplasma, vol. 249, no. 2, pp. 379–392, 2012. View at Publisher · View at Google Scholar
  2. M. R. Tandang-Silvas, E. M. Tecson-Mendoza, B. Mikami, S. Utsumi, and N. Maruyama, “Molecular design of seed storage proteins for enhanced food physicochemical properties,” Annual Review of Food Science and Technology, vol. 2, pp. 59–73, 2011. View at Publisher · View at Google Scholar
  3. T. Kawakatsu and F. Takaiwa, “Cereal seed storage protein synthesis: fundamental processes for recombinant protein production in cereal grains,” Plant Biotechnology Journal, vol. 8, no. 9, pp. 939–953, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. S. Pérez and E. Bertoft, “The molecular structures of starch components and their contribution to the architecture of starch granules: a comprehensive review,” Starch/Staerke, vol. 62, no. 8, pp. 389–420, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. S. G. Ball and M. K. Morell, “From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule,” Annual Review of Plant Biology, vol. 54, pp. 207–233, 2003. View at Publisher · View at Google Scholar · View at Scopus
  6. A. M. Smith, “The biosynthesis of starch granules,” Biomacromolecules, vol. 2, no. 2, pp. 335–341, 2001. View at Publisher · View at Google Scholar · View at Scopus
  7. K. D. Chapman, J. M. Dyer, and R. T. Mullen, “Biogenesis and functions of lipid droplets in plants: Thematic Review Series: Lipid Droplet Synthesis and Metabolism: from Yeast to Man,” Journal of Lipid Research, vol. 53, no. 2, pp. 215–226, 2012. View at Publisher · View at Google Scholar
  8. D. J. Murphy, “The dynamic roles of intracellular lipid droplets: from archaea to mammals,” Protoplasma, vol. 249, no. 3, pp. 541–585, 2011.
  9. J. T. C. Tzen, “Seed oil bodies of sesame and their surface proteins, oleosin, caleosin, and steroleosin,” in Sesame, the Genus Sesamum, D. Bedigian, Ed., vol. 48, chapter 10, pp. 187–200, CRC Press, London, UK, 1st edition, 2011.
  10. A. H. C. Huang, “Oleosins and oil bodies in seeds and other organs,” Plant Physiology, vol. 110, no. 4, pp. 1055–1061, 1996. View at Scopus
  11. D. L. Brasaemle and N. E. Wolins, “Packaging of fat: an evolving model of lipid droplet assembly and expansion,” Journal of Biological Chemistry, vol. 287, no. 4, pp. 2273–2279, 2012. View at Publisher · View at Google Scholar
  12. D. Zweytick, K. Athenstaedt, and G. Daum, “Intracellular lipid particles of eukaryotic cells,” Biochimica et Biophysica Acta, vol. 1469, no. 2, pp. 101–120, 2000. View at Publisher · View at Google Scholar · View at Scopus
  13. J. A. Napier, A. K. Stobart, and P. R. Shewry, “The structure and biogenesis of plant oil bodies: the role of the ER membrane and the oleosin class of proteins,” Plant Molecular Biology, vol. 31, no. 5, pp. 945–956, 1996. View at Scopus
  14. C. C. Peng and J. T. C. Tzen, “Analysis of the three essential constituents of oil bodies in developing sesame seeds,” Plant and Cell Physiology, vol. 39, no. 1, pp. 35–42, 1998. View at Scopus
  15. J. T. C. Tzen, Y. Z. Cao, P. Laurent, C. Ratnayake, and A. H. C. Huang, “Lipids, proteins, and structure of seed oil bodies from diverse species,” Plant Physiology, vol. 101, no. 1, pp. 267–276, 1993. View at Scopus
  16. C. R. Slack, W. S. Bertaud, B. D. Shaw, R. Holland, J. Browse, and H. Wright, “Some studies on the composition and surface properties of oil bodies from the seed cotyledons of safflower (Carthamus tinctorius) and linseed (Linum ustatissimum),” Biochemical Journal, vol. 190, no. 3, pp. 551–561, 1980. View at Scopus
  17. R. Qu, S. M. Wang, Y. H. Lin, V. B. Vance, and A. H. Huang, “Characteristics and biosynthesis of membrane proteins of lipid bodies in the scutella of maize (Zea mays L.),” The Biochemical Journal, vol. 235, no. 1, pp. 57–65, 1986. View at Scopus
  18. E. M. Herman, “Immunogold-localization and synthesis of an oil-body membrane protein in developing soybean seeds,” Planta, vol. 172, no. 3, pp. 336–345, 1987. View at Publisher · View at Google Scholar · View at Scopus
  19. D. J. Murphy, “Storage lipid bodies in plants and other organisms,” Progress in Lipid Research, vol. 29, no. 4, pp. 299–324, 1990. View at Scopus
  20. L. Y. Yatsu and T. J. Jacks, “Spherosome membranes: half unit-membranes,” Plant Physiology, vol. 49, no. 6, pp. 937–943, 1972. View at Publisher · View at Google Scholar
  21. A. H. C. Huang, “Oil bodies and oleosins in seeds,” Annual Review of Plant Physiology and Plant Molecular Biology, vol. 43, no. 1, pp. 177–200, 1992. View at Scopus
  22. D. J. Murphy, “Structure, function and biogenesis of storage lipid bodies and oleosins in plants,” Progress in Lipid Research, vol. 32, no. 3, pp. 247–280, 1993. View at Publisher · View at Google Scholar · View at Scopus
  23. G. I. Frandsen, J. Mundy, and J. T. C. Tzen, “Oil bodies and their associated proteins, oleosin and caleosin,” Physiologia Plantarum, vol. 112, no. 3, pp. 301–307, 2001. View at Publisher · View at Google Scholar · View at Scopus
  24. Z. Purkrtova, P. Jolivet, M. Miquel, and T. Chardot, “Structure and function of seed lipid body-associated proteins,” Comptes Rendus Biologies, vol. 331, no. 10, pp. 746–754, 2008. View at Publisher · View at Google Scholar · View at Scopus
  25. V. B. Vance and A. H. Huang, “The major protein from lipid bodies of maize. Characterization and structure based on cDNA cloning,” Journal of Biological Chemistry, vol. 262, no. 23, pp. 11275–11279, 1987. View at Scopus
  26. R. Qu and A. H. C. Huang, “Oleosin KD 18 on the surface of oil bodies in maize. Genomic and cDNA sequences and the deduced protein structure,” Journal of Biological Chemistry, vol. 265, no. 4, pp. 2238–2243, 1990. View at Scopus
  27. D. J. Murphy and D. M. Y. Au, “A new class of highly abundant apolipoproteins involved in lipid storage in oilseeds,” Biochemical Society Transactions, vol. 117, no. 4, pp. 682–683, 1989.
  28. D. J. Murphy, J. N. Keen, J. N. O'Sullivan et al., “A class of amphipathic proteins associated with lipid storage bodies in plants. Possible similarities with animal serum apolipoproteins,” Biochimica et Biophysica Acta, vol. 1088, no. 1, pp. 86–94, 1991. View at Publisher · View at Google Scholar · View at Scopus
  29. J. S. Keddie, G. Hübner, S. P. Slocombe et al., “Cloning and characterisation of an oleosin gene from Brassica napus,” Plant Molecular Biology, vol. 19, no. 3, pp. 443–453, 1992. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Kalinski, D. S. Loer, J. M. Weisemann, B. F. Matthews, and E. M. Herman, “Isoforms of soybean seed oil body membrane protein 24 kDa oleosin are encoded by closely related cDNAs,” Plant Molecular Biology, vol. 17, no. 5, pp. 1095–1098, 1991. View at Publisher · View at Google Scholar · View at Scopus
  31. P. Hatzopoulos, G. Franz, L. Choy, and R. Z. Sung, “Interaction of nuclear factors with upstream sequences of a lipid body membrane protein gene from carrot,” Plant Cell, vol. 2, no. 5, pp. 457–467, 1990. View at Scopus
  32. I. Cummins and D. J. Murphy, “cDNA sequence of a sunflower oleosin and transcript tissue specificity,” Plant Molecular Biology, vol. 19, no. 5, pp. 873–876, 1992. View at Publisher · View at Google Scholar · View at Scopus
  33. G. J. H. van Rooijen, L. I. Terning, and M. M. Moloney, “Nucleotide sequence of an Arabidopsis thaliana oleosin gene,” Plant Molecular Biology, vol. 18, no. 6, pp. 1177–1179, 1992. View at Publisher · View at Google Scholar · View at Scopus
  34. D. W. Hughes, H. Y. Wang, and G. A. Galau, “Cotton (Gossypium hirsutum) MatP6 and MatP7 oleosin genes,” Plant Physiology, vol. 101, no. 2, pp. 697–698, 1993. View at Scopus
  35. Q. Liu, Y. Sun, W. Su, et al., “Species-specific size expansion and molecular evolution of the oleosins in angiosperms,” Gene, vol. 509, no. 2, pp. 247–257, 2012. View at Publisher · View at Google Scholar
  36. R. B. Aalen, “The transcripts encoding two oleosin isoforms are both present in the aleurone and in the embryo of barley (Hordeum vulgare L.) seeds,” Plant Molecular Biology, vol. 28, no. 3, pp. 583–588, 1995. View at Scopus
  37. R. L. C. Chuang, J. C. F. Chen, J. Chu, and J. T. C. Tzen, “Characterization of seed oil bodies and their surface oleosin isoforms from rice embryos,” Journal of Biochemistry, vol. 120, no. 1, pp. 74–81, 1996. View at Scopus
  38. J. C. F. Chen, R. H. Lin, H. C. Huang, and J. T. C. Tzen, “Cloning, expression and isoform classification of a minor oleosin in sesame oil bodies,” Journal of Biochemistry, vol. 122, no. 4, pp. 819–824, 1997. View at Scopus
  39. L. S. H. Wu, L. D. Wang, P. W. Chen, L. J. Chen, and J. T. C. Tzen, “Genomic cloning of 18 kDa oleosin and detection of triacylglycerols and oleosin isoforms in maturing rice and postgerminative seedlings,” Journal of Biochemistry, vol. 123, no. 3, pp. 386–391, 1998. View at Scopus
  40. J. T. C. Tzen and A. H. C. Huang, “Surface structure and properties of plant seed oil bodies,” Journal of Cell Biology, vol. 117, no. 2, pp. 327–335, 1992. View at Publisher · View at Google Scholar · View at Scopus
  41. J. T. C. Tzen, G. C. Lie, and A. H. C. Huang, “Characterization of the charged components and their topology on the surface of plant seed oil bodies,” Journal of Biological Chemistry, vol. 267, no. 22, pp. 15626–15634, 1992. View at Scopus
  42. J. T. C. Tzen, C. C. Peng, D. J. Cheng, E. C. F. Chen, and J. M. H. Chiu, “A new method for seed oil body purification and examination of oil body integrity following germination,” Journal of Biochemistry, vol. 121, no. 4, pp. 762–768, 1997. View at Scopus
  43. E. C. F. Chen, S. S. K. Tai, C. C. Peng, and J. T. C. Tzen, “Identification of three novel unique proteins in seed oil bodies of sesame,” Plant and Cell Physiology, vol. 39, no. 9, pp. 935–941, 1998. View at Scopus
  44. L. J. Lin and J. T. C. Tzen, “Two distinct steroleosins are present in seed oil bodies,” Plant Physiology and Biochemistry, vol. 42, no. 7-8, pp. 601–608, 2004. View at Publisher · View at Google Scholar · View at Scopus
  45. J. T. C. Tzen, M. M. Wang, J. C. F. Chen, L. J. Lin, and M. C. M. Chen, “Seed oil body proteins: oleosin, caleosin, and steroleosin,” Current Topic in Biochemical Reseaech, vol. 5, pp. 133–139, 2003.
  46. J. C. F. Chen, C. C. Y. Tsai, and J. T. C. Tzen, “Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds,” Plant and Cell Physiology, vol. 40, no. 10, pp. 1079–1086, 1999. View at Scopus
  47. L. J. Lin, S. S. K. Tai, C. C. Peng, and J. T. C. Tzen, “Steroleosin, a sterol-binding dehydrogenase in seed oil bodies,” Plant Physiology, vol. 128, no. 4, pp. 1200–1211, 2002. View at Publisher · View at Google Scholar · View at Scopus
  48. H. Tnani, I. López, T. Jouenne, and C. M. Vicient, “Quantitative subproteomic analysis of germinating related changes in the scutellum oil bodies of Zea mays,” Plant Science, vol. 191-192, pp. 1–7, 2012. View at Publisher · View at Google Scholar
  49. H. Tnani, I. López, T. Jouenne, and C. M. Vicient, “Protein composition analysis of oil bodies from maize embryos during germination,” Journal of Plant Physiology, vol. 168, no. 5, pp. 510–513, 2011. View at Publisher · View at Google Scholar · View at Scopus
  50. S. Popluechai, M. Froissard, P. Jolivet et al., “Jatropha curcas oil body proteome and oleosins: L-form JcOle3 as a potential phylogenetic marker,” Plant Physiology and Biochemistry, vol. 49, no. 3, pp. 352–356, 2011. View at Publisher · View at Google Scholar · View at Scopus
  51. F. Capuano, N. J. Bond, L. Gatto, et al., “LC-MS/MS methods for absolute quantification and identification of proteins associated with chimeric plant oil bodies,” Analytical Chemistry, vol. 83, no. 24, pp. 9267–9272, 2011. View at Publisher · View at Google Scholar
  52. P. Jolivet, C. Boulard, A. Bellamy et al., “Protein composition of oil bodies from mature Brassica napus seeds,” Proteomics, vol. 9, no. 12, pp. 3268–3284, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. V. Katavic, G. K. Agrawal, M. Hajduch, S. L. Harris, and J. J. Thelen, “Protein and lipid composition analysis of oil bodies from two Brassica napus cultivars,” Proteomics, vol. 6, no. 16, pp. 4586–4598, 2006. View at Publisher · View at Google Scholar · View at Scopus
  54. P. Jolivet, E. Roux, S. D'Andrea et al., “Protein composition of oil bodies in Arabidopsis thaliana ecotype WS,” Plant Physiology and Biochemistry, vol. 42, no. 6, pp. 501–509, 2004. View at Publisher · View at Google Scholar · View at Scopus
  55. J. T. C. Tzen, M. M. C. Wang, S. S. K. Tai, T. T. T. Lee, and C. C. Peng, “The abundant proteins in sesame seed: storage proteins in protein bodies and oleosins in oil bodies,” Advances in Plant Physiolology, vol. 6, pp. 93–105, 2003.
  56. L. J. Lin, P. C. Liao, H. H. Yang, and J. T. C. Tzen, “Determination and analyses of the N-termini of oil-body proteins, steroleosin, caleosin and oleosin,” Plant Physiology and Biochemistry, vol. 43, no. 8, pp. 770–776, 2005. View at Publisher · View at Google Scholar · View at Scopus
  57. D. J. Murphy, “The biogenesis and functions of lipid bodies in animals, plants and microorganisms,” Progress in Lipid Research, vol. 40, no. 5, pp. 325–438, 2001. View at Publisher · View at Google Scholar · View at Scopus
  58. F. Capuano, F. Beaudoin, J. A. Napier, and P. R. Shewry, “Properties and exploitation of oleosins,” Biotechnology Advances, vol. 25, no. 2, pp. 203–206, 2007. View at Publisher · View at Google Scholar · View at Scopus
  59. T. L. Shimada and I. Hara-Nishimura, “Oil-body-membrane proteins and their physiological functions in plants,” Biological and Pharmaceutical Bulletin, vol. 33, no. 3, pp. 360–363, 2010. View at Publisher · View at Google Scholar · View at Scopus
  60. C. C. Peng, V. S. Y. Lee, M. Y. Lin, H. Y. Huang, and J. T. C. Tzen, “Minimizing the central hydrophobic domain in oleosin for the constitution of artificial oil bodies,” Journal of Agricultural and Food Chemistry, vol. 55, no. 14, pp. 5604–5610, 2007. View at Publisher · View at Google Scholar · View at Scopus
  61. B. M. Abell, M. Hahn, L. A. Holbrook, and M. M. Moloney, “Membrane topology and sequence requirements for oil body targeting of oleosin,” Plant Journal, vol. 37, no. 4, pp. 461–470, 2004. View at Publisher · View at Google Scholar · View at Scopus
  62. K. Giannoulia, G. Banilas, and P. Hatzopoulos, “Oleosin gene expression in olive,” Journal of Plant Physiology, vol. 164, no. 1, pp. 104–107, 2007. View at Publisher · View at Google Scholar · View at Scopus
  63. B. M. Abell, L. A. Holbrook, M. Abenes, D. J. Murphy, M. J. Hills, and M. M. Moloney, “Role of the proline knot motif in oleosin endoplasmic reticulum topology and oil body targeting,” Plant Cell, vol. 9, no. 8, pp. 1481–1493, 1997. View at Publisher · View at Google Scholar · View at Scopus
  64. K. B. Vargo, R. Parthasarathy, and D. A. Hammer, “Self-assembly of tunable protein suprastructures from recombinant oleosin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 29, pp. 11657–11662, 2012. View at Publisher · View at Google Scholar
  65. Y. Gohon, J. D. Vindigni, A. Pallier et al., “High water solubility and fold in amphipols of proteins with large hydrophobic regions: oleosins and caleosin from seed lipid bodies,” Biochimica et Biophysica Acta, vol. 1808, no. 3, pp. 706–716, 2011. View at Publisher · View at Google Scholar · View at Scopus
  66. L. G. Alexander, R. B. Sessions, A. R. Clarke, A. S. Tatham, P. R. Shewry, and J. A. Napier, “Characterization and modelling of the hydrophobic domain of a sunflower oleosin,” Planta, vol. 214, no. 4, pp. 546–551, 2002. View at Publisher · View at Google Scholar · View at Scopus
  67. M. Li, D. J. Murphy, K. H. K. Lee et al., “Purification and structural characterization of the central hydrophobic domain of oleosin,” Journal of Biological Chemistry, vol. 277, no. 40, pp. 37888–37895, 2002. View at Publisher · View at Google Scholar · View at Scopus
  68. B. M. Abell, S. High, and M. M. Moloney, “Membrane protein topology of oleosin is constrained by its long hydrophobic domain,” Journal of Biological Chemistry, vol. 277, no. 10, pp. 8602–8610, 2002. View at Publisher · View at Google Scholar · View at Scopus
  69. D. J. Lacey, N. Wellner, F. Beaudoin, J. A. Napier, and P. R. Shewry, “Secondary structure of oleosins in oil bodies isolated from seeds of safflower (Carthamus tinctorius L.) and sunflower (Helianthus annuus L.),” Biochemical Journal, vol. 334, no. 2, pp. 469–477, 1998. View at Scopus
  70. M. Millichip, A. S. Tatham, F. Jackson, G. Griffiths, P. R. Shewry, and A. K. Stobart, “Purification and characterization of oil-bodies (oleosomes) and oil-body boundary proteins (oleosins) from the developing cotyledons of sunflower (Helianthus annuus L.),” Biochemical Journal, vol. 314, no. 1, pp. 333–337, 1996. View at Scopus
  71. M. Li, J. S. Keddie, L. J. Smith, D. C. Clark, and D. J. Murphy, “Expression and characterization of the N-terminal domain of an oleosin protein from sunflower,” Journal of Biological Chemistry, vol. 268, no. 23, pp. 17504–17512, 1993. View at Scopus
  72. M. Li, L. J. Smith, D. C. Clark, R. Wilson, and D. J. Murphy, “Secondary structures of a new class of lipid body proteins from oilseeds,” Journal of Biological Chemistry, vol. 267, no. 12, pp. 8245–8253, 1992. View at Scopus
  73. S. Takahashi, T. Katagiri, K. Yamaguchi-Shinozaki, and K. Shinozaki, “An Arabidopsis gene encoding a Ca2+ -binding protein is induced by abscisic acid during dehydration,” Plant and Cell Physiology, vol. 41, no. 7, pp. 898–903, 2000. View at Scopus
  74. Z. Purkrtova, C. Le Bon, B. Kralova, M. H. Ropers, M. Anton, and T. Chardot, “Caleosin of Arabidopsis thaliana: effect of calcium on functional and structural properties,” Journal of Agricultural and Food Chemistry, vol. 56, no. 23, pp. 11217–11224, 2008. View at Publisher · View at Google Scholar · View at Scopus
  75. M. B. Busch, K. H. Kortje, H. Rahmann, and A. Sievers, “Characteristic and differential calcium signals from cell structures of the root cap detected by energy-filtering electron microscopy (EELS/ESI),” European Journal of Cell Biology, vol. 60, no. 1, pp. 88–100, 1993. View at Scopus
  76. P. L. Jiang and J. T. C. Tzen, “Caleosin serves as the major structural protein as efficient as oleosin on the surface of seed oil bodies,” Plant Signaling and Behavior, vol. 5, no. 4, pp. 447–449, 2010. View at Scopus
  77. T. H. Liu, C. L. Chyan, F. Y. Li, and J. T. C. Tzen, “Stability of artificial oil bodies constituted with recombinant caleosins,” Journal of Agricultural and Food Chemistry, vol. 57, no. 6, pp. 2308–2313, 2009. View at Publisher · View at Google Scholar · View at Scopus
  78. J. C. F. Chen and J. T. C. Tzen, “An in vitro system to examine the effective phospholipids and structural domain for protein targeting to seed oil bodies,” Plant and Cell Physiology, vol. 42, no. 11, pp. 1245–1252, 2001. View at Scopus
  79. Z. Purkrtova, S. d'Andrea, P. Jolivet et al., “Structural properties of caleosin: a MS and CD study,” Archives of Biochemistry and Biophysics, vol. 464, no. 2, pp. 335–343, 2007. View at Publisher · View at Google Scholar · View at Scopus
  80. C. I. Brändeén, “Relation between structure and function of alpha/beta-proteins,” Quarterly Reviews of Biophysics, vol. 13, no. 3, pp. 317–338, 1980. View at Scopus
  81. C. van der Schoot, L. K. Paul, S. B. Paul, and P. L. Rinne, “Plant lipid bodies and cell-cell signaling: a new role for an old organelle?” Plant Signaling and Behavior, vol. 6, no. 11, pp. 1732–1738, 2011. View at Publisher · View at Google Scholar
  82. T. L. Shimada, T. Shimada, H. Takahashi, Y. Fukao, and I. Hara-Nishimura, “A novel role for oleosins in freezing tolerance of oilseeds in Arabidopsis thaliana,” Plant Journal, vol. 55, no. 5, pp. 798–809, 2008. View at Publisher · View at Google Scholar · View at Scopus
  83. Y. Y. Wu, Y. R. Chou, C. S. Wang, T. H. Tseng, L. J. Chen, and J. T. C. Tzen, “Different effects on triacylglycerol packaging to oil bodies in transgenic rice seeds by specifically eliminating one of their two oleosin isoforms,” Plant Physiology and Biochemistry, vol. 48, no. 2-3, pp. 81–89, 2010. View at Publisher · View at Google Scholar · View at Scopus
  84. M. A. Schmidt and E. M. Herman, “Suppression of soybean oleosin produces micro-oil bodies that aggregate into oil body/ER complexes,” Molecular Plant, vol. 1, no. 6, pp. 910–924, 2008. View at Publisher · View at Google Scholar · View at Scopus
  85. R. M. P. Siloto, K. Findlay, A. Lopez-Villalobos, E. C. Yeung, C. L. Nykiforuk, and M. M. Moloney, “The accumulation of oleosins determines the size of seed oilbodies in Arabidopsis,” Plant Cell, vol. 18, no. 8, pp. 1961–1974, 2006. View at Publisher · View at Google Scholar · View at Scopus
  86. E. Roux, S. Baumberger, M. A. V. Axelos, and T. Chardot, “Oleosins of Arabidopsis thaliana: expression in Escherichia coli, purification, and functional properties,” Journal of Agricultural and Food Chemistry, vol. 52, no. 16, pp. 5245–5249, 2004. View at Publisher · View at Google Scholar · View at Scopus
  87. C. C. Peng, I. P. Lin, C. K. Lin, and J. T. C. Tzen, “Size and stability of reconstituted sesame oil bodies,” Biotechnology Progress, vol. 19, no. 5, pp. 1623–1626, 2003. View at Publisher · View at Google Scholar · View at Scopus
  88. J. T. L. Ting, K. Lee, C. Ratnayake, K. A. Platt, R. A. Balsamo, and A. H. C. Huang, “Oleosin genes in maize kernels having diverse oil contents are constitutively expressed independent of oil contents: size and shape of intracellular oil bodies are determined by the oleosins/oils ratio,” Planta, vol. 199, no. 1, pp. 158–165, 1996. View at Scopus
  89. N. Babazadeh, M. Poursaadat, H. R. Sadeghipour, and A. Hossein Zadeh Colagar, “Oil body mobilization in sunflower seedlings is potentially regulated by thioredoxin h,” Plant Physiology and Biochemistry, vol. 57, pp. 134–142, 2012. View at Publisher · View at Google Scholar
  90. M. Rudolph, A. Schlereth, M. Körner et al., “The lipoxygenase-dependent oxygenation of lipid body membranes is promoted by a patatin-type phospholipase in cucumber cotyledons,” Journal of Experimental Botany, vol. 62, no. 2, pp. 749–760, 2011. View at Publisher · View at Google Scholar · View at Scopus
  91. E. S. L. Hsiao and J. T. C. Tzen, “Ubiquitination of oleosin-H and caleosin in sesame oil bodies after seed germination,” Plant Physiology and Biochemistry, vol. 49, no. 1, pp. 77–81, 2011. View at Publisher · View at Google Scholar · View at Scopus
  92. S. Vandana and S. C. Bhatla, “Evidence for the probable oil body association of a thiol-protease, leading to oleosin degradation in sunflower seedling cotyledons,” Plant Physiology and Biochemistry, vol. 44, no. 11-12, pp. 714–723, 2006. View at Publisher · View at Google Scholar · View at Scopus
  93. V. Parthibane, S. Rajakumari, V. Venkateshwari, R. Iyappan, and R. Rajasekharan, “Oleosin is bifunctional enzyme that has both monoacylglycerol acyltransferase and phospholipase activities,” The Journal of Biological Chemistry, vol. 287, no. 3, pp. 1946–1954, 2012.
  94. V. Parthibane, R. Iyappan, A. Vijayakumar, V. Venkateshwari, and R. Rajasekharan, “Serine/threonine/tyrosine protein kinase phosphorylates oleosin, a regulator of lipid metabolic functions,” Plant Physiology, vol. 159, no. 1, pp. 95–104, 2012. View at Publisher · View at Google Scholar
  95. P. L. Jiang, J. C. F. Chen, S. T. Chiu, and J. T. C. Tzen, “Stable oil bodies sheltered by a unique caleosin in cycad megagametophytes,” Plant Physiology and Biochemistry, vol. 47, no. 11-12, pp. 1009–1016, 2009. View at Publisher · View at Google Scholar · View at Scopus
  96. M. Poxleitner, S. W. Rogers, A. Lacey Samuels, J. Browse, and J. C. Rogers, “A role for caleosin in degradation of oil-body storage lipid during seed germination,” Plant Journal, vol. 47, no. 6, pp. 917–933, 2006. View at Publisher · View at Google Scholar · View at Scopus
  97. P. L. Jiang, C. S. Wang, C. M. Hsu, G. Y. Jauh, and J. T. C. Tzen, “Stable oil bodies sheltered by a unique oleosin in lily pollen,” Plant and Cell Physiology, vol. 48, no. 6, pp. 812–821, 2007. View at Publisher · View at Google Scholar · View at Scopus
  98. P. L. Jiang, G. Y. Jauh, C. S. Wang, and J. T. C. Tzen, “A unique caleosin in oil bodies of lily pollen,” Plant and Cell Physiology, vol. 49, no. 9, pp. 1390–1395, 2008. View at Publisher · View at Google Scholar · View at Scopus
  99. K. Zienkiewicz, A. J. Castro, J. D. D. Alché, A. Zienkiewicz, C. Suárez, and M. I. Rodríguez-García, “Identification and localization of a caleosin in olive (Olea europaea L.) pollen during in vitro germination,” Journal of Experimental Botany, vol. 61, no. 5, pp. 1537–1546, 2010. View at Publisher · View at Google Scholar · View at Scopus
  100. A. Hanano, M. Burcklen, M. Flenet et al., “Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif,” Journal of Biological Chemistry, vol. 281, no. 44, pp. 33140–33151, 2006. View at Publisher · View at Google Scholar · View at Scopus
  101. M. Partridge and D. J. Murphy, “Roles of a membrane-bound caleosin and putative peroxygenase in biotic and abiotic stress responses in Arabidopsis,” Plant Physiology and Biochemistry, vol. 47, no. 9, pp. 796–806, 2009. View at Publisher · View at Google Scholar · View at Scopus
  102. H. Feng, X. Wang, Y. Sun et al., “Cloning and characterization of a calcium binding EF-hand protein gene TaCab1 from wheat and its expression in response to Puccinia striiformis f. sp. tritici and abiotic stresses,” Molecular Biology Reports, vol. 38, no. 6, pp. 3857–3866, 2011. View at Publisher · View at Google Scholar · View at Scopus
  103. Y. Y. Kim, K. W. Jung, K. S. Yoo, J. U. Jeung, and J. S. Shin, “A stress-responsive caleosin-like protein, AtCLO4, Acts as a Negative Regulator of ABA Responses in Arabidopsis,” Plant and Cell Physiology, vol. 52, no. 5, pp. 874–884, 2011. View at Publisher · View at Google Scholar · View at Scopus
  104. Y. Aubert, L. Leba, C. Cheval et al., “Involvement of RD20, a member of caleosin family, in ABA-mediated regulation of germination in Arabidopsis thaliana,” Plant Signaling and Behavior, vol. 6, no. 4, pp. 538–540, 2011. View at Publisher · View at Google Scholar · View at Scopus
  105. H. B. Khalil, Z. Wang, J. A. Wright, et al., “Heterotrimeric Gα subunit from wheat (Triticum aestivum), GA3, interacts with the calcium-binding protein, Clo3, and the phosphoinositide-specific phospholipase C, PI-PLC1,” Plant Molecular Biology, vol. 77, pp. 145–158, 2011. View at Publisher · View at Google Scholar
  106. E. Blée, M. Flenet, B. Boachon, and M. L. Fauconnier, “A non-canonical caleosin from Arabidopsis efficiently epoxidizes physiological unsaturated fatty acids with complete stereoselectivity,” The FEBS Journal, vol. 279, no. 20, pp. 3981–3995, 2012. View at Publisher · View at Google Scholar
  107. S. De Domenico, S. Bonsegna, M. S. Lenucci, et al., “Localization of seed oil body proteins in tobacco protoplasts reveals specific mechanisms of protein targeting to leaf lipid droplets,” Journal of Integrative Plant Biology, vol. 53, no. 11, pp. 858–868, 2011. View at Publisher · View at Google Scholar
  108. J. Hänisch, M. Wältermann, H. Robenek, and A. Steinbüchel, “Eukaryotic lipid body proteins in oleogenous actinomycetes and their targeting to intracellular triacylglycerol inclusions: impact on models of lipid body biogenesis,” Applied and Environmental Microbiology, vol. 72, no. 10, pp. 6743–6750, 2006. View at Publisher · View at Google Scholar · View at Scopus
  109. W. Li, L. G. Li, X. F. Sun, and K. X. Tang, “An oleosin-fusion protein driven by the CaMV35S promoter is accumulated in Arabidopsis (Brassicaceae) seeds and correctly targeted to oil bodies,” Genetics and Molecular Research, vol. 11, no. 3, pp. 2138–2146, 2012. View at Publisher · View at Google Scholar
  110. G. J. Van Rooijen and M. M. Moloney, “Structural requirements of oleosin domains for subcellular targeting to the oil body,” Plant Physiology, vol. 109, no. 4, pp. 1353–1361, 1995. View at Scopus
  111. I. Cummins, M. J. Hills, J. H. E. Ross, D. H. Hobbs, M. D. Watson, and D. J. Murphy, “Differential, temporal and spatial expression of genes involved in storage oil and oleosin accumulation in developing rapeseed embryos: implications for the role of oleosins and the mechanisms of oil-body formation,” Plant Molecular Biology, vol. 23, no. 5, pp. 1015–1027, 1993. View at Scopus
  112. W. S. Lee, J. T. C. Tzen, J. C. Kridl, S. E. Radke, and A. H. C. Huang, “Maize oleosin is correctly targeted to seed oil bodies in Brassica napus transformed with the maize oleosin gene,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 14, pp. 6181–6185, 1991. View at Scopus
  113. T. Wahlroos, J. Soukka, A. Denesyuk, R. Wahlroos, T. Korpela, and N. J. Kilby, “Oleosin expression and trafficking during oil body biogenesis in tobacco leaf cells,” Genesis, vol. 35, no. 2, pp. 125–132, 2003. View at Publisher · View at Google Scholar · View at Scopus
  114. J. T. L. Ting, R. A. Balsamo, C. Ratnayake, and A. H. C. Huang, “Oleosin of plant seed oil bodies is correctly targeted to the lipid bodies in transformed yeast,” Journal of Biological Chemistry, vol. 272, no. 6, pp. 3699–3706, 1997. View at Publisher · View at Google Scholar · View at Scopus
  115. F. Beaudoin, B. M. Wilkinson, C. J. Stirling, and J. A. Napier, “In vivo targeting of a sunflower oil body protein in yeast secretory (sec) mutants,” Plant Journal, vol. 23, no. 2, pp. 159–170, 2000. View at Publisher · View at Google Scholar · View at Scopus
  116. F. Beaudoin and J. A. Napier, “The targeting and accumulation of ectopically expressed oleosin in non-seed tissues of Arabidopsis thaliana,” Planta, vol. 210, no. 3, pp. 439–445, 2000. View at Scopus
  117. C. Sarmiento, J. H. E. Ross, E. Herman, and D. J. Murphy, “Expression and subcellular targeting of a soybean oleosin in transgenic rapeseed. Implications for the mechanism of oil-body formation in seeds,” Plant Journal, vol. 11, no. 4, pp. 783–796, 1997. View at Publisher · View at Google Scholar · View at Scopus
  118. P. J. Thoyts, M. I. Millichip, A. K. Stobart, W. T. Griffiths, P. R. Shewry, and J. A. Napier, “Expression and in vitro targeting of a sunflower oleosin,” Plant Molecular Biology, vol. 29, no. 2, pp. 403–410, 1995. View at Scopus
  119. D. S. Loer and E. M. Herman, “Cotranslational integration of soybean (Glycine max) oil body membrane protein oleosin into microsomal membranes,” Plant Physiology, vol. 101, no. 3, pp. 993–998, 1993. View at Scopus
  120. M. J. Hills, M. D. Watson, and D. J. Murphy, “Targeting of oleosins to the oil bodies of oilseed rape (Brassica napus L.),” Planta, vol. 189, no. 1, pp. 24–29, 1993. View at Publisher · View at Google Scholar · View at Scopus
  121. M. Froissard, S. D'Andréa, C. Boulard, and T. Chardot, “Heterologous expression of AtClo1, a plant oil body protein, induces lipid accumulation in yeast,” FEMS Yeast Research, vol. 9, no. 3, pp. 428–438, 2009. View at Publisher · View at Google Scholar · View at Scopus
  122. F. Beaudoin and J. A. Napier, “Targeting and membrane-insertion of a sunflower oleosin in vitro and in Saccharomyces cerevisiae: the central hydrophobic domain contains more than one signal sequence, and directs oleosin insertion into the endoplasmic reticulum membrane using a signal anchor sequence mechanism,” Planta, vol. 215, no. 2, pp. 293–303, 2002. View at Publisher · View at Google Scholar · View at Scopus
  123. J. T. C. Tzen, Y. K. Lai, K. L. Chan, and A. H. C. Huang, “Oleosin isoforms of high and low molecular weights are present in the oil bodies of diverse seed species,” Plant Physiology, vol. 94, no. 3, pp. 1282–1289, 1990. View at Scopus
  124. J. T. C. Tzen, R. L. C. Chuang, J. C. F. Chen, and L. S. H. Wu, “Coexistence of both oleosin isoforms on the surface of seed oil bodies and their individual stabilization to the organelles,” Journal of Biochemistry, vol. 123, no. 2, pp. 318–323, 1998. View at Scopus
  125. S. S. K. Tai, M. C. M. Chen, C. C. Peng, and J. T. C. Tzen, “Gene family of oleosin isoforms and their structural stabilization in sesame seed oil bodies,” Bioscience, Biotechnology and Biochemistry, vol. 66, no. 10, pp. 2146–2153, 2002. View at Scopus
  126. A. C. N. Chua, P. L. Jiang, L. S. Shi, W. M. Chou, and J. T. C. Tzen, “Characterization of oil bodies in jelly fig achenes,” Plant Physiology and Biochemistry, vol. 46, no. 5-6, pp. 525–532, 2008. View at Publisher · View at Google Scholar · View at Scopus
  127. A. J. Simkin, T. Qian, V. Caillet et al., “Oleosin gene family of Coffea canephora: quantitative expression analysis of five oleosin genes in developing and germinating coffee grain,” Journal of Plant Physiology, vol. 163, no. 7, pp. 691–708, 2006. View at Publisher · View at Google Scholar · View at Scopus
  128. L. S. H. Wu, G. H. H. Hong, R. F. Hou, and J. T. C. Tzen, “Classification of the single oleosin isoform and characterization of seed oil bodies in gymnosperms,” Plant and Cell Physiology, vol. 40, no. 3, pp. 326–334, 1999. View at Scopus
  129. M. R. Roberts, R. Hodge, and R. Scott, “Brassica napus pollen oleosins possess a characteristic C-terminal domain,” Planta, vol. 195, no. 3, pp. 469–470, 1995. View at Scopus
  130. D. J. Murphy and J. H. E. Ross, “Biosynthesis, targeting and processing of oleosin-like proteins, which are major pollen coat components in Brassica napus,” Plant Journal, vol. 13, no. 1, pp. 1–16, 1998. View at Scopus
  131. C. Y. Huang, C. I. Chung, Y. C. Lin, Y. I. C. Hsing, and A. H. C. Huang, “Oil bodies and oleosins in Physcomitrella possess characteristics representative of early trends in evolution,” Plant Physiology, vol. 150, no. 3, pp. 1192–1203, 2009. View at Publisher · View at Google Scholar · View at Scopus
  132. L. S. Robert, J. Gerster, S. Allard, L. Cass, and J. Simmonds, “Molecular characterization of two Brassica napus genes related to oleosins which are highly expressed in the tapetum,” Plant Journal, vol. 6, no. 6, pp. 927–933, 1994. View at Scopus
  133. J. H. E. Ross and D. J. Murphy, “Characterization of anther-expressed genes encoding a major class of extracellular oleosin-like proteins in the pollen coat of Brassicaceae,” Plant Journal, vol. 9, no. 5, pp. 625–637, 1996. View at Scopus
  134. L. O. Franco, C. L. De, S. Hamdi, G. Sachetto-Martins, and D. E. De Oliveira, “Distal regulatory regions restrict the expression of cis-linked genes to the tapetal cells,” The FEBS Letters, vol. 517, no. 1–3, pp. 13–18, 2002. View at Publisher · View at Google Scholar · View at Scopus
  135. D. H. Chen, C. L. Chyan, P. L. Jiang, C. S. Chen, and J. T. C. Tzen, “The same oleosin isoforms are present in oil bodies of rice embryo and aleurone layer while caleosin exists only in those of the embryo,” Plant Physiology and Biochemistry, vol. 60, pp. 18–24, 2012. View at Publisher · View at Google Scholar
  136. H. C. Lu, P. L. Jiang, L. R. C. Hsu, C. L. Chyan, and J. T. C. Tzen, “Characterization of Oil bodies in adlay (Coix lachryma-jobi L),” Bioscience, Biotechnology and Biochemistry, vol. 74, no. 9, pp. 1841–1847, 2010. View at Publisher · View at Google Scholar · View at Scopus
  137. H. Liu, P. Hedley, L. Cardle et al., “Characterisation and functional analysis of two barley caleosins expressed during barley caryopsis development,” Planta, vol. 221, no. 4, pp. 513–522, 2005. View at Publisher · View at Google Scholar · View at Scopus
  138. K. Zienkiewicz, A. Zienkiewicz, M. I. Rodríguez-García, and A. J. Castro, “Characterization of a caleosin expressed during olive (Olea europaea L.) pollen ontogeny,” BMC Plant Biology, vol. 11, article 122, 2011.
  139. I. P. Lin, P. L. Jiang, C. S. Chen, and J. T. C. Tzen, “A unique caleosin serving as the major integral protein in oil bodies isolated from Chlorella sp. cells cultured with limited nitrogen,” Plant Physiology and Biochemistry, vol. 44, no. 61, pp. 80–87, 2012. View at Publisher · View at Google Scholar
  140. H. Næsted, G. I. Frandsen, G. Y. Jauh et al., “Caleosins: Ca2+-binding proteins associated with lipid bodies,” Plant Molecular Biology, vol. 44, no. 4, pp. 463–476, 2000. View at Publisher · View at Google Scholar · View at Scopus
  141. C. C. Peng, J. C. F. Chen, D. J. H. Shyu, M. J. Chen, and J. T. C. Tzen, “A system for purification of recombinant proteins in Escherichia coli via artificial oil bodies constituted with their oleosin-fused polypeptides,” Journal of Biotechnology, vol. 111, no. 1, pp. 51–57, 2004. View at Publisher · View at Google Scholar · View at Scopus
  142. C. C. Peng, D. J. H. Shyu, W. M. Chou, M. J. Chen, and J. T. C. Tzen, “Method for bacterial expression and purification of sesame cystatin via artificial oil bodies,” Journal of Agricultural and Food Chemistry, vol. 52, no. 10, pp. 3115–3119, 2004. View at Publisher · View at Google Scholar · View at Scopus
  143. M. C. M. Chen, C. L. Chyan, T. T. T. Lee, S. H. Huang, and J. T. C. Tzen, “Constitution of stable artificial oil bodies with triacylglycerol, phospholipid, and caleosin,” Journal of Agricultural and Food Chemistry, vol. 52, no. 12, pp. 3982–3987, 2004. View at Publisher · View at Google Scholar · View at Scopus
  144. G. J. H. Van Rooijen and M. M. Moloney, “Plant seed oil-bodies as carriers for foreign proteins,” Bio/Technology, vol. 13, no. 1, pp. 72–77, 1995. View at Scopus
  145. J. G. Boothe, J. A. Saponja, and D. L. Parmenter, “Molecular farming in plants: oilseeds as vehicles for the production of pharmaceutical proteins,” Drug Development Research, vol. 42, no. 3-4, pp. 172–181, 1997.
  146. N. Markley, C. Nykiforuk, J. Boothe, and M. Moloney, “Producing proteins using transgenic oilbody-oleosin technology,” BioPharm International, vol. 19, no. 6, pp. 34–57, 2006. View at Scopus
  147. S. C. Bhatla, V. Kaushik, and M. K. Yadav, “Use of oil bodies and oleosins in recombinant protein production and other biotechnological applications,” Biotechnology Advances, vol. 28, no. 3, pp. 293–300, 2010. View at Publisher · View at Google Scholar · View at Scopus
  148. M. D. McLean, R. Chen, D. Yu, et al., “Purification of the therapeutic antibody trastuzumab from genetically modified plants using safflower Protein A-oleosin oilbody technology,” Transgenic Research. In press.
  149. G. Banilas, G. Daras, S. Rigas, M. M. Moloney, and P. Hatzopoulos, “Oleosin di-or tri-meric fusions with GFP undergo correct targeting and provide advantages for recombinant protein production,” Plant Physiology and Biochemistry, vol. 49, no. 2, pp. 216–222, 2011. View at Publisher · View at Google Scholar · View at Scopus
  150. C. Y. Yang, S. Y. Chen, and G. C. Duan, “Transgenic peanut (Arachis hypogaea L.) expressing the urease subunit B gene of Helicobacter pylori,” Current Microbiology, vol. 63, no. 4, pp. 387–391, 2011. View at Publisher · View at Google Scholar
  151. W. Li, L. Li, K. Li, J. Lin, X. Sun, and K. Tang, “Expression of biologically active human insulin-like growth factor 1 in Arabidopsis thaliana seeds via oleosin fusion technology,” Biotechnology and Applied Biochemistry, vol. 58, no. 3, pp. 139–146, 2011. View at Publisher · View at Google Scholar · View at Scopus
  152. A. Ahmad, E. O. Pereira, A. J. Conley, A. S. Richman, and R. Menassa, “Green biofactories: recombinant protein production in plants,” Recent Patents on Biotechnology, vol. 4, no. 3, pp. 242–259, 2010. View at Publisher · View at Google Scholar · View at Scopus
  153. C. E. Orozco-Barrios, S. F. Battaglia-Hsu, M. L. Arango-Rodriguez et al., “Vitamin B12-impaired metabolism produces apoptosis and Parkinson phenotype in rats expressing the transcobalamin-oleosin chimera in substantia nigra,” PLoS ONE, vol. 4, no. 12, Article ID e8268, 2009. View at Publisher · View at Google Scholar · View at Scopus
  154. L. Pons, S. F. Battaglia-Hsu, C. E. Orozco-Barrios et al., “Anchoring secreted proteins in endoplasmic reticulum by plant oleosin: the example of vitamin B12 cellular sequestration by transcobalamin,” PLoS ONE, vol. 4, no. 7, Article ID e6325, 2009. View at Publisher · View at Google Scholar · View at Scopus
  155. M. M. Moloney, “Oil-body proteins as carriers of high-value peptides in plants,” Patent US, 659835, 1991.
  156. M. M. Moloney and G. van Rooijen Sembiosys, “Expression of epidermal growth factor in plant seeds,” Patent US, 7091401, 2006.
  157. M. M. Moloney, “Oil-body proteins as carriers of high-value peptides in plants,” Patent US, 5650554, 1997.
  158. M. M. Moloney, J. Boothe, and G. van Rooijen, “Oil bodies and associated proteins as affinity matrices,” Patent US, 6509453, 2003.
  159. S. Szarka, G. van Rooijen, and M. M. Moloney, “Methods for the production of multimeric immunoglobulins, and related compositions,” Patent US, 7098383, 2006.
  160. G. van Rooijen, S. Zaplachinski, P. B. Heifetz, et al., “Methods for the production of multimeric protein complexes, and related compositions,” Patent US, 2006/0179514, 2006.
  161. J. McCarthy and S. A. Nestec, “Recombinant oleosins from cacao and their use as flavoring or emulsifying agents,” Patent US, 7126042, 2006.
  162. T. Harada, K. Kashihara, and N. Nio, “Oleosin/phospholipid complex and process for producing the same,” Patent WO, 2002/026788, 2002.
  163. H. M. Deckers, G. van Rooijen, J. Boothe, et al., “Uses of oil bodies,” Patent US, 6210742, 2001.
  164. C. J. Chiang, H. C. Chen, Y. P. Chad, and J. T. C. Tzen, “Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli,” Journal of Agricultural and Food Chemistry, vol. 53, no. 12, pp. 4799–4804, 2005. View at Publisher · View at Google Scholar · View at Scopus
  165. J. R. Liu, C. H. Duan, X. Zhao, J. T. C. Tzen, K. J. Cheng, and C. K. Pai, “Cloning of a rumen fungal xylanase gene and purification of the recombinant enzyme via artificial oil bodies,” Applied Microbiology and Biotechnology, vol. 79, no. 2, pp. 225–233, 2008. View at Publisher · View at Google Scholar · View at Scopus
  166. Y. J. Hung, C. C. Peng, J. T. C. Tzen, M. J. Chen, and J. R. Liu, “Immobilization of Neocallimastix patriciarum xylanase on artificial oil bodies and statistical optimization of enzyme activity,” Bioresource Technology, vol. 99, no. 18, pp. 8662–8666, 2008. View at Publisher · View at Google Scholar · View at Scopus
  167. R. W. Scott, S. Winichayakul, M. Roldan et al., “Elevation of oil body integrity and emulsion stability by polyoleosins, multiple oleosin units joined in tandem head-to-tail fusions,” Plant Biotechnology Journal, vol. 8, no. 8, pp. 912–927, 2010. View at Publisher · View at Google Scholar · View at Scopus
  168. J. M. Tseng, J. R. Huang, H. C. Huang, J. T. C. Tzen, W. M. Chou, and C. C. Peng, “Facilitative production of an antimicrobial peptide royalisin and its antibody via an artificial oil-body system,” Biotechnology Progress, vol. 27, no. 1, pp. 153–161, 2011. View at Publisher · View at Google Scholar · View at Scopus
  169. S. Winichayakul, A. Pernthaner, S. Livingston, et al., “Production of active single-chain antibodies in seeds using trimeric polyoleosin fusion,” Journal of Biotechnology, vol. 161, no. 4, pp. 407–413, 2012. View at Publisher · View at Google Scholar
  170. C. J. Chiang, H. C. Chen, H. F. Kuo, Y. P. Chao, and J. T. C. Tzen, “A simple and effective method to prepare immobilized enzymes using artificial oil bodies,” Enzyme and Microbial Technology, vol. 39, no. 5, pp. 1152–1158, 2006. View at Publisher · View at Google Scholar · View at Scopus
  171. C. J. Chiang, H. C. Chen, Y. P. Chao, and J. T. C. Tzen, “One-step purification of insoluble hydantoinase overproduced in Escherichia coli,” Protein Expression and Purification, vol. 52, no. 1, pp. 14–18, 2007. View at Publisher · View at Google Scholar · View at Scopus
  172. R. C. W. Hou, M. Y. Lin, M. M. C. Wang, and J. T. C. Tzen, “Increase of viability of entrapped cells of Lactobacillus delbrueckii ssp. bulgaricus in artificial sesame oil emulsions,” Journal of Dairy Science, vol. 86, no. 2, pp. 424–428, 2003. View at Scopus
  173. M. C. M. Chen, J. L. Wang, and J. T. C. Tzen, “Elevating bioavailability of cyclosporine A via encapsulation in artificial oil bodies stabilized by caleosin,” Biotechnology Progress, vol. 21, no. 4, pp. 1297–1301, 2005. View at Publisher · View at Google Scholar · View at Scopus
  174. C. J. Chiang, C. C. Lin, T. L. Lu, and H. F. Wang, “Functionalized nanoscale oil bodies for targeted delivery of a hydrophobic drug,” Nanotechnology, vol. 22, no. 41, Article ID 415102, 2011. View at Publisher · View at Google Scholar
  175. C. J. Chiang, C. J. Chen, L. J. Lin, C. H. Chang, and Y. P. Chao, “Selective delivery of cargo entities to tumor cells by nanoscale artificial oil bodies,” Journal of Agricultural and Food Chemistry, vol. 58, no. 22, pp. 11695–11702, 2010. View at Publisher · View at Google Scholar · View at Scopus
  176. C. J. Chiang, L. J. Lin, C. C. Lin, C. H. Chang, and Y. P. Chao, “Selective internalization of self-assembled artificial oil bodies by HER2/neu-positive cells,” Nanotechnology, vol. 22, no. 1, Article ID 015102, 2011. View at Publisher · View at Google Scholar · View at Scopus
  177. M. T. Chang, C. R. Chen, T. H. Liu, C. P. Lee, and J. T. C. Tzen, “Development of a protocol to solidify native and artificial oil bodies for long-term storage at room temperature,” Journal of the Science of Food and Agriculture. In press. View at Publisher · View at Google Scholar
  178. T. H. Liu, C. L. Chyan, F. Y. Li, Y. J. Chen, and J. T. C. Tzen, “Engineering lysine-rich caleosins as carrier proteins torenderbiotin as a hapten on artificial oil bodies for antibody production,” Biotechnology Progress, vol. 27, no. 6, pp. 1760–1767, 2011. View at Publisher · View at Google Scholar