A comparative study on kinetics and substrate specificities of Phospholipase A₁ with Thermomyces lanuginosus lipase

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• 作者：Ruipu Xin^a ; Faez Iqbal Khan^b ; Zexin Zhao^c ; Zedong Zhang^a ; Bo Yang^c ; Yonghua Wang^a ; ^{yonghw@scut.edu.cn}
• 关键词：Lipase ; Phospholipase A1 ; Chain-length specificity ; Regiospecificity ; Monolayer ; Interfacial binding ; Substrate specificity
• 刊名：Journal of Colloid and Interface Science
• 出版年：2017
• 出版时间：15 February 2017
• 年：2017
• 卷：488
• 期：Complete
• 页码：149-154
• 全文大小：1676 K
• 卷排序：488

文摘

The mechanism of lipase binding to the lipid-water interface is crucial for substrate specificity and kinetic properties. In this study, the chain-length specificity, regiospecificity and substrate specificity of Phospholipase A1 (PLA1) and its parent enzyme Thermomyces lanuginosus lipase (TLL) have been investigated using a classical emulsion system. The results show that both PLA1 and TLL are 1,3-regioselective lipases. Additionally, the hydrolytic activity of PLA1 is comparatively lower on short-chain triacylglyceride (TAG) and higher on phosphatidylcholine (PC) than the hydrolytic activity of TLL. Further, the results obtained with monolayer film techniques demonstrate that the C-terminal region regulates the binding of PLA1 to PC. A hypothesis is presented according to which the α9 helix of C-terminal region in PLA1 not only controls the opening of lid but also serves as a membrane anchor that assists in binding to PC. These findings bring new insight into rational design of novel lipases with intriguing functionalities.