Properties and exploitation of oleosins.
Oleosins stabilize oil bodies in seeds and other tissues and contain a unique hydrophobic domain which appears to be inserted into the oil matrix as an alpha-helical hairpin. The oleosin proteins may be exploited to stabilize emulsions while the ease of oil body preparation has led to the expression of bioactive proteins as oleosin fusions in molecular farming.
Capuano
Floriana
F
Rothamsted Research, Harpenden, Herts AL5 2JQ, UK.
Beaudoin
Frédéric
F
Napier
Johnathan A
JA
Shewry
Peter R
PR
D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism; D001709:Biotechnology / Q000379:methods*; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D004655:Emulsions; D005818:Genetic Engineering / Q000379:methods; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D030821:Plants, Genetically Modified; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods
D029681:Arabidopsis Proteins; D002352:Carrier Proteins; D004655:Emulsions; D008565:Membrane Proteins; D010940:Plant Proteins; C448199:oleosin Bn-III protein, Brassica napus; C079353:oleosin protein, Arabidopsis