The phospholipase A(2) (PLA(2)) from Streptomyces violaceoruber was successfully expressed in the methylotrophic yeast Pichia pastoris GS115 under the control of AOX1 promoter for the first time. The maximum activity of the recombinant PLA(2) (rPLA(2)) reached 34.7 +/- 0.2 U/mL, and specific activity was 170 +/- 4 U/mg after purification. On the sodium dodecyl sulfate polyacrylamide gel electrophoresis of the culture supernatants, three bands of 21, 18, and 14.3 kDa were observed. The peptide mass fingerprinting analysis showed that all of these three bands were rPLA(2) from S. violaceoruber. By the treatment with Endo H and PNGase F, it indicated that the rPLA(2) occurred N-glycosylation. The enzymatic properties of this enzyme were determined. The rPLA(2) exhibited a lower optimum pH (pH = 6.0) compared to the wild-type enzyme, which was a desirable property in the application of oil degumming. In the enzymatic degumming process, the phosphorus content decreased from 261.77 +/- 3.51 mg/kg to 20.74 +/- 0.23 mg/kg, which is very promising for the industrial application.