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The interaction between protein and phospholipids is a widespread phenomenon involving several physiological events in postmortem muscle. We hereby report a method for one-step purification of a phosphatidylcholine-binding (PC-binding) protein from duck Biceps femoris muscle with relatively high purity and yield using ion-exchange chromatography. This PC-binding protein has an inhibitory effect on the activity of phospholipase A2 (PLA2). A decrease (~62.3%) in PLA2 activity was observed. It had a strong affinity to bind PC at pH range of 6.2–6.8 with a peak at pH 6.6 (13.36 ± 0.48 g PC/g protein); in addition, raising ATP content from 1 to 5 μmol/mL enhanced the binding capacity. The PC-binding protein plays a potential role in the integrity of membrane and meat quality.

Purification and characterisation of a phosphatidylcholine-binding protein from duck Biceps femoris muscle