A phytase gene (appA) from Escherichia coli was cloned into Streptomyces lividans and expressed as an extracellular protein which was then compared with the same enzyme expressed in Pichia pastoris. The phytase expressed in S. lividans was not glycosylated and had a molecular mass of 45 kDa. Compared with the glycosylated phytase expressed in P. pastoris, this non-glycosylated phytase was 25-50% less active (p < 0.05) at pH 2 to 3.5 or at 45 and 55&DEG;C, but 50% more active (p < 0.05) at 75degreesC. The thermo-tolerance of the non-glycosylated phytase was 26 and 48% higher (p < 0.05) than that of the glycosylated phytase at 45 and 55&DEG;C, but was 80 and 94% lower (p < 0.05) at 65degrees and 75degreesC, respectively.