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    Intestinal phospholipase A(2) from Sparidae species: Functional properties and cytotoxic potential evaluation

    Year: 2020

    Journal: Int. J. Biol. Macromol., Volume 143, JAN 15, page 881–890

    Authors: Smichi, N; Parsiegla, G; Achouri, N; Zarai, Z; Abousalham, A; Fendri, A

    Organizations: Ministry of higher education and scientific research of Tunisia

    Keywords: Sparidae; Intestinal sPLA(2); Isolation and expression; Thermostability; Substrate specificity; Structural properties; Cytotoxicity activity

    Marine species have gained significant attention as potential source for a broad spectrum of bioactive proteins. Fish phospholipases A(2) (PLA(2)) have attracted renewed interest due to their excellent properties in lipid digestion. Herein, we report for the first time the catalytic properties of two intestinal secreted PLA(2) (sPLA(2)) identified from Diplodus sargus (IDsPLA(2)) and Sparus aurata (ISaPLA(2)). The highest sequence identity was obtained with recently isolated Sparidae digestive PLA(2) (45%) and Human pancreatic PLA(2) (42%). IDsPLA(2) and ISaPLA(2) were overexpressed in E. coli as inclusion bodies, refolded and purified. Both enzymes have improved thermostability compared to mammalian pancreatic sPLA(2) since they are active and stable at 55 degrees C, with specific activities of 320 and 190 U mg(-1) measured on phosphatidylcholine, respectively. Interestingly, IDsPLA(2), but not ISaPLA(2), revealed weak toxicity towards macrophages and suggests its involvement in cell membrane degradation. ISaPLA(2) was found to be more active than IDsPLA(2) when using the monolayer technique at 20 mN m(-1). Structural models of both enzymes revealed their differences. In silico docking of phospholipids with both models allowed proposing key amino-acids in substrate binding and selectivity. Overall, these results provide insight into the enzymatic and structural properties of two novel sPLA(2) with potential for future applications. (C) 2019 Elsevier B.V. All rights reserved.
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