The adsorption of substrates/products on immobilized enzymes was a common bad phenomenon. A novel method was proposed to turn this “drawback” into treasure. Immobilized phospholipase D (PLD) acted as not only the catalyst, but also an “anchor molecule” facilitating the adsorption of hydrophobic substrate phosphatidylcholine (PC) in purely aqueous solutions. The PC loading even reached 96.7 %. The adsorption region and relevant driving forces were confirmed by the molecular docking and dynamics. The highest yield of phosphatidylserine (PS) reached 95.4 %. An “artificial interphase” was created, allowing a hydrophobic microenvironment for minimal hydrolysis. Simulation results indicated that adsorbed PC molecules would diffuse into the active center by rapid adsorption-desorption equilibrium or the parallel movement on the surface of PLD or combination diffusion. It explained why these “fixed” substrates could interact with the active center. Moreover, obtained PS was manufactured into microcapsules and toxic solvents were completely avoided in the whole process.

底物/产物在固定化酶上的吸附是常见的不良现象。提出了一种新颖的方法来将这种“缺点”变成珍宝。固定化磷脂酶D（PLD）不仅充当催化剂，而且还充当“锚分子”，促进疏水性底物磷脂酰胆碱（PC）在纯水溶液中的吸附。PC加载量甚至达到了96.7％。通过分子对接和动力学确定了吸附区域和相关的驱动力。磷脂酰丝氨酸（PS）的最高产率达到95.4％。创建了“人工界面”，从而使疏水性微环境的水解减至最少。模拟结果表明，被吸附的PC分子将通过快速的吸附-解吸平衡或PLD表面上的平行运动或组合扩散而扩散到活性中心。它解释了为什么这些“固定的”基材可以与活性中心相互作用。而且，将获得的PS制成微囊，并且在整个过程中完全避免了有毒溶剂。