Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Arabidopsis Proteins / chemistry
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Arabidopsis Proteins / metabolism
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Biotechnology / methods*
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Emulsions
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Genetic Engineering / methods
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Hydrophobic and Hydrophilic Interactions
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Membrane Proteins
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Plant Proteins / chemistry*
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Plant Proteins / genetics
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Plant Proteins / metabolism*
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Plants, Genetically Modified
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Protein Conformation
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Protein Engineering / methods
Substances
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Arabidopsis Proteins
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Carrier Proteins
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Emulsions
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Membrane Proteins
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Plant Proteins
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oleosin Bn-III protein, Brassica napus
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oleosin protein, Arabidopsis