Molecular Cloning and Functional Analysis of a Δ-fatty Acid Desaturase from the Antarctic Microalga Sp. ICE-L
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sp. ICE-L, which can thrive in extreme environments of the Antarctic, could represent a promising alternative for polyunsaturated fatty acid (PUFA) production. A new Δ-fatty acid desaturase (FAD)-encoding gene ( ), 1269 bp in size, was cloned from sp. ICE-L. Bioinformatics analysis showed that -encoded protein was homologous to known FADs with conserved histidine motifs, and localized to the chloroplast. Functional analysis of indicated that recombinant 6803 expressing ΔCiFAD could accumulate C18:2, whereas recombinant expressing this enzyme could not accumulate C18:2 or any other new fatty acids. These results indicate that ΔCiFAD is a functional enzyme in the chloroplast that can adjust sp. ICE-L cell membrane fluidity to adapt to Antarctic extreme low-temperature environments, which give us insights into the frigostable and cold-resistant mechanisms of hypothermic organisms.
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