Fatty acid desaturation enzymes perform dehydrogenation reactions leading to the insertion of double bonds in fatty acids. ω‑3 desaturase has an important role in converting ω‑6 fatty acids into ω‑3 fatty acids. Although genes for this desaturase have been identified, the enzymatic activity of Δ‑17 with or without transmembrane domain, and the function of the Δ‑17 desaturase is poorly understood. In the present study, a transgenic microorganism was used to clone the Δ‑17 full length (Δ‑17FL) and Δ‑17 without transmembrane domain (Δ‑17NT), the expression efficiency was improved and western blotting was used to detect the protein expression level. The purification of Δ‑17 was precipitated using saturated ammonium sulfate solution, dissolved in phosphate buffered saline buffer, and then filtered using a 10 kDa ultrafiltration cube. Gas chromatography analysis was used to measure the effect of Δ‑17NT or Δ‑17FL expression on Pichia pastoris fatty acid composition. Furthermore, the function of Δ‑17NT in HepG2 cells was measured and the mechanism was explored. It was demonstrated that Δ‑17NT decreased cell growth and increased apoptosis in hepatocellular carcinoma cell lines in vitro. In conclusion, successful expression of high levels of recombinant Δ‑17NT represents a critical step towards the elucidation of the function of membrane fatty acid desaturases.

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