Functional Characterization of Fatty Acyl-Reductase CG17560 in Drosophila Melanogaster
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Authors
Yi, Bo R.
Issue Date
2014
Type
Thesis
Language
en_US
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Abstract
Over the past few decades, there has been growing interest in biofuel
development to supplement current energy sources, with different approaches being
explored. Use of enzymes from insects, such as fatty-acyl reductases (FARs), has been
one such approach. FARs convert fatty acids to equivalent aldehydes and/or alcohols.
Aldehydes may serve as precursors for decarbonylation, resulting in hydrocarbon
production which could then be purified as biofuel. The FAR 17560 protein from
Drosophila melanogaster was analyzed for its substrate specificity and resulting product.
The experiment involved baculoviral expression of the FAR 17560 gene in SF9 cells and
functional assays with various free fatty acid substrates, using whole cell incubations.
Initial reactions with infected cells producing recombinant FAR 17560 showed uptake of
substrate when given a free fatty acid cocktail (24:0, 26:0, 28:0) with only 24:0 being
taken up in preferentially, however aldehyde or alcohol products from these substrates
were not detected . The free fatty acid 18:0 was also tested for substrate specificity. These
data suggest that FAR 17560 may have specificity for 24:0 FFA and smaller chain length
FFAs. This suggests that FARs work together with other enzymes not present in the SF9
cells, which would explain why only FFA uptake without substrate modification was
observed. As such, conducting additional research can help to further identify the
specificity of FAR 17560 protein.
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