This is the first time secretory Phosphalipase A₂ (sPLA₂) enzymes from soybean seeds (Glycine max), denoted as GmsPLA₂-XIA-1 and GmsPLA₂-XIB-2, were produced by heterologous expression in E.coli, renatured from inclusion bodies by guanidine treatment and purified by ion exchange chromatography. Mixed micelles of phospholipid/Triton X-100 were used in a Colorimetric assay in order to obtain the optimum conditions for catalysis. Both sPLA₂s showed a maximum enzyme activity at pH 7, a requirement of Ca²⁺ essentially in micromolar concentrations and optimum temperature for catalysis of 60ºC, similar parameters to those found in animals and plants. These enzymes showed subtle differences in the preference for phospholipids with different head groups in the presence and absence of NaCl. The apparent kinetic parameters (V_max app and K_{m app}) demonstrate that both enzymes have more preference for phosphatidilcholine than for phosphatidylglycerol in contrast with the results observed for pancreatic sPLA₂. Furthermore, the mode of catalysis was studied. The effect of auxins as indole 3-acetic acid and indole 3-propionic acid were studied and shows to rapidly stimulate the conversion of phosphatidylcholine to LPC and free fatty acid.