Characterization of the recombinant porcine pancreas phospholipase A2 expressed in Pichia pastoris GS115 and its application to synthesis of 2-DHA-PS

•A novel strategy for synthesis of 1-acyl-2-docosahexaenoyl-phosphatidylserine (2-DHA-PS) using recombinant porcine pancreas phospholipase A2 (rPLA2M) is studied.•rPLA2M is successfully expressed in Pichia pastoris GS115.•rPLA2M displays the same activity as the native porcine pancreas phospholipase A2.•rPLA2M is successfully applied in the synthesis of 2-DHA-PS.•The yield of 2-DHA-PS using the rPLA2M is 23% in a safe method.

1-Acyl-2-docosahexaenoyl-phosphatidylserine (2-DHA-PS) is a species of phosphatidylserine (PS) with a docosahexaenoic acid (DHA) esterified sn-2 position. 2-DHA-PS has been suggested to enhance cognitive performance. Enzyme-catalyzed synthesis of 2-DHA-PS is proceeded by using phospholipase A2. The codon-optimized gene pla2m, encoding porcine pancreas phospholipase A2 (ppPLA2), was expressed in Pichia pastoris GS115 for functional characterization of recombinant PLA2M (rPLA2M). The rPLA2M showed maximum enzymatic activity at 40 °C and pH 8.0 and was stable within a broad range of temperatures (30-55 °C) and pHs (pH 6.0-9.0). Moreover, rPLA2M was successfully applied in the synthesis of 2-DHA-PS using PS and DHA as substrates with a yield of 23%. Thus, rPLA2M displays the same hydrolysis and transesterification activities as native ppPLA2, providing a novel strategy for the production of 2-DHA-PS.

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