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Background  Trefoil factor 1 (TFF1) mediates mucosal repair and belongs to a highly conserved trefoil factor family proteins which are secreted by epithelial cells in the stomach or colon mucous membrane. TFF1 forms a homodimer via a disulphide linkage that affects wound healing activity. Previous recombinant expressions of TFF1 were too low yield for industrial application. This study aims to improve the expression level of bioactive recombinant TFF1 (rTFF1) and facilitate application potency.    Methods  The rTFF1 gene  rtff 1 was synthesized, expressed by  Escherichia coli  and secreted by  Brevibacillus choshinensis . The rTFF1s were purified. The polymeric patterns and wound healing capacities of purified rTFF1s were checked.    Results  In  Escherichia coli , 21.08 mg/L rTFF1 was stably expressed as monomer, dimer and oligomer in soluble fraction. In  Brevebacillus choshinensis , the rTFF1 was secreted extracellularly at high level (35.73 mg/L) and formed monomer, dimer and oligomer forms. Both proteins from different sources were purified by Ni-NTA chromatography and exhibited the wound healing activities. The rTFF1 produced by  B. choshinensis  had better wound healing capability than the rTFF1 produced by  E. co li. After pH 2.4 buffer treatments, the purified rTFF1 formed more oligomeric forms as well as better wound healing capability. Glycosylation assay and LC-MS/MS spectrometry experiments showed that the rTFF1 produced by  B. choshinensis  was unexpectedly glycosylated at N-terminal Ser residue. The glycosylation may contribute to the better wound healing capacity.    Conclusions  This study provides a potent tool of rTFF1 production to be applied in gastric damage protection and wound healing. The protein sources from  B. choshinensis  were more efficient than rTFF1 produced by  E. coli .    Electronic supplementary material  The online version of this article (doi:10.1186/s12896-015-0149-5) contains supplementary material, which is available to authorized users.

Functional expression of recombinant human trefoil factor 1 by Escherichia coli and Brevibacillus choshinensis