Objective:To gain insight of biological characteristics and application feasibility for GFP homolog hmGFP from Heteractis magnifica.Methods:Two different prokaryotic expression systems(pET21b and pETTRX) of hmGFP were constructed and recombinant hmGFP can be both functionally expressed under low temperature.The expression difference between pET21b-hmGFP and pETTRX-hmGFP were further investigated.Results:The expression level and the solubility of the recombinant hmGFP protein in pETTRX were better than that in pET21b.Conclusion:The optimal pETTRX-hmGFP expression condition was established for next step of purifying mature recombinant hmGFP protein to characterize its fluorescent spectrum.