Abstract
Abstract Human epidermal growth factor (hEGF) is a crucial factor in wound healing, and therefore has wide applications in the pharmaceutical and cosmetics industries. To improve the production of hEGF protein for the industrial scale, we established an hEGF gene construct for recombinant secretion by Bacillus subtilis. Examination of the secretion abilities of various signal peptides (SPs) revealed six SPs that could effectively guide hEGF secretion from B. subtilis into the culture medium. The highest production level was obtained when the hEGF gene was fused with the xynD SP (lipo type). Two copies of the hEGF expression cassette had the same effect on improving production yield as isopropyl-β- d -1-thiogalactopyranoside (IPTG) induction, and the highest yield of hEGF can reach 360 ± 9.41 mg/L. Moreover, high-purity hEGF was obtained using a His-tagged purification system. Overall, these results demonstrate that B. subtilis is a suitable cell factory for hEGF production with improved yield compared to previous systems.
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