Recognized as the biotechnol. workhorse, Escherichia coli has been commonly employed for mass production of recombinant proteins. Target proteins that are overexpressed in E. coli usually accumulate in cell cyctoplasm. This inherent limitation renders the downstream process for protein recovery complicated and costly. This issue was addressed by development of the programmed cell-lysis system. The cell-lysis system was constructed with a core element consisting of the cell lesion-incurred module and the regulatory circuit. The module comprises the gene E of bacteriophage ϕX174 (ϕXE) and the gene e of T4 bacteriophage (T4E). The toxin activity of ϕXE and T4E is responsible for disintegration of cell membrane and of cell wall, resp. The circuit encompasses the thermo-sensitive cI857 and hybrid promoters which are recognized by various sigma factors including σ70, σ32, and σ38. Consequently, the expression of ϕXE and T4E was induced by heat. The production of amidohydrolase (AHL) by the T7 expression system was investigated in E. coli BL21(DE3) strain equipped with the cell-lysis system. It resulted in 93% of and 76% of the expressed AHL being secreted after administration of thermal induction in the late log phase and the early stationery phase, resp. The result indicates that the cell-lysis system is programmed in response to heat, which shows a promise for efficient secretion of the recombinant protein.