It is known that phospholipase A₂ (PLA₂) hydrolyzes phosphatidylcholines (PC) producing lysophosphatidylcholine and fatty acids. The substrate of the enzymatic action is the sn₂ acyl chain being Ca²⁺ ion an essential cofactor for the activation. Many data are available showing the influence of hydration and defects of the interphase on the hydrolysis mechanism. In this regard, it is well known that carbonyl groups (CO) is a hydration site promoting different organization of water and packing defects at the surface level.

In this paper, the adsorption and activity of PLA₂ on ester and ether PC was measured in order to evaluate the influence of CO as hydration site. This was accomplished evaluating the zeta potential changes and the concomitant hydrolytic products in the presence of Ca²⁺. A model based on FTIR-ATR analysis and docking studies, considers the formation of an enzyme complex with CO and PO groups and Ca²⁺.

已知磷脂酶A ₂（PLA ₂）水解磷脂酰胆碱（PC），产生溶血磷脂酰胆碱和脂肪酸。酶促作用的底物是sn ₂酰基链，Ca ²⁺离子是激活的必要辅助因子。现有许多数据表明水合和中间相缺陷对水解机理的影响。在这方面，众所周知羰基（CO）是促进水的不同组织和表面水平堆积缺陷的水合位点。

本文通过测定PLA ₂在酯和醚PC上的吸附和活性，以评估CO对水合部位的影响。这是在存在Ca ²⁺的情况下评估zeta电位变化和伴随的水解产物而完成的。基于FTIR-ATR分析和对接研究的模型考虑了具有CO和PO基团以及Ca ²⁺的酶复合物的形成。