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  • Title: A comparative study on kinetics and substrate specificities of Phospholipase A1 with Thermomyces lanuginosus lipase.
    Author: Xin R, Khan FI, Zhao Z, Zhang Z, Yang B, Wang Y.
    Journal: J Colloid Interface Sci; 2017 Feb 15; 488():149-154. PubMed ID: 27821336.
    Abstract:
    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.
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