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    -Identification of a novel intestinal phospholipase A(2) from annular seabream: Insights into its catalytic mechanism and its role in biological processes

    Year: 2020

    Journal: Process Biochem., Volume 91, APR, page 197–207

    Authors: Smichi, N; Othman, H; Zarai, Z; Fendri, A; Abousalham, A

    Organizations: Ministry of higher education and scientific research of Tunisia

    Keywords: Annular seabream; Intestinal sPLA(2); Thermostability; Substrate specificity; Structural properties; Cytotoxic activity

    Phospholipase A(2) (PLA(2)) is responsible for the lipid hydrolysis process. Fish PLA(2) have warranted renewed interest due to their excellent properties in phospholipid digestion. We report for the first time the catalytic properties of a PLA(2) secreted from the intestine of the annular seabream Diplodus annularis (IDaPLA(2)). The refolded IDaPLA(2) was purified to homogeneity and showed a molecular mass of around 15 kDa attested by SDSPAGE and MALDI-TOF analyses. Interestingly, IDaPLA(2) revealed higher thermostability compared to mammal pancreatic sPLA(2) as it was active and stable at 55 degrees C with specific activity of 290 U mg(-1) on phosphatidylcholine (PC) as a substrate. Using the lipid monolayer technique, the activity of IDaPLA(2) was found to be 21.68, 6.88 and 5.66 mol cm(-2) min(-1) mM(-1) using phosphatidylglycerol (PG), PC and phosphatidylethanolamine (PE) monolayers, respectively, at surface pressures from 20 - 30 mN m(-1). Interestingly, the interfacial activity of IDaPLA(2) measured at higher surface pressures may highlight its ability to penetrate into phospholipid monolayers suggesting its involvement in cell lipid membrane degradation which can explain the cytotoxicity potential towards macrophage. The docking simulation data provided insights into the involvement of some key amino-acids in substrate binding and selectivity. The dynamic simulation proved the high stability of IDaPLA(2). Overall, these results provide original evidence on the involvement of IDaPLA(2) into the lipid hydrolysis suggesting it as a potential target in biotechnological applications.
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