Streptomyces chromofuscus phospholipase D interaction with lipidic activators at the air–water interface

摘要: The phospholipase D from Streptomyces chromofuscus (PLDSc) is a soluble enzyme that interacts with membranes to catalyse phosphatidylcholine (PC) transformation. In this work, we focused on the interaction between PLDSc and two lipid activators: neutral lipid, diacylglycerol (DAG), an anionic one, phosphatidic acid (PA). DAG naturally occurring alcohol, so it potent nucleophile for transphosphatidylation reaction catalysed by PLD. Concerning PA, widely described activator of PLDSc-catalysed hydrolysis PC. monolayer technique allowed us define PA. case DAG, results suggest insertion within acyl chains exclusion pressure approximately 45 mN/m. PLDSc-DAG seemed occur preferentially in liquid-expanded (LE) phase. PA was found be more effective at high surface pressures. overall obtained show preferential protein condensed domains. No could PLDSc-PA indicating only superficial polar head lipid. Brewster angle microscopy (BAM) images were acquired order confirm these visualise patterns induced adsorption.