{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang P"],"funding":["Fundamental Research Funds for the Central Universities","National Key Research and Development Program of China Stem Cell and Translational Research","National Natural Science Foundation of China","National Key Research and Development Program of China","Natural Science Foundation of Jiangsu Province"],"pagination":["273-280"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10073938"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(2)"],"pubmed_abstract":["Phospholipase D (PLD) is an essential biocatalyst for the biological production of phosphatidylserine and phospholipid modification. However, the efficient heterologous expression of PLD is limited by its cell toxicity. In this study, a PLD was secretory expressed efficiently in <i>Bacillus subtilis</i> with an activity around 100 U/mL. A secretory expression system containing the signal peptide SP<sub>EstA</sub> and the dual-promoter P<sub>HpaII-SrfA</sub> was established, and the extracellular PLD activity further reached 119.22 U/mL through scale-up fermentation, 191.30-fold higher than that of the control. Under optimum reaction conditions, a 61.61% conversion ratio and 21.07 g/L of phosphatidylserine production were achieved. Finally, the synthesis system of PL derivates was established, which could efficiently synthesis novel PL derivates. The results highlight that the secretory expression system constructed in this study provides a promising PLD producing strain in industrial application, and laid the foundation for the biosynthesis of phosphatidylserine and other PL derivates. As far as we know, this work reports the highest level of extracellular PLD expression to date and the enzymatic production of several PL derivates for the first time."],"journal":["Synthetic and systems biotechnology"],"pubmed_title":["Efficient secretory expression of phospholipase D for the high-yield production of phosphatidylserine and phospholipid derivates from soybean lecithin."],"pmcid":["PMC10073938"],"funding_grant_id":["2021YFC2100900","BK20221082","32171261","JUSRP21940"],"pubmed_authors":["Su C","Rao ZM","Gong JS","Shi JS","Xie ZH","Zhang XM","Xu ZH","Zhang P"],"additional_accession":[]},"is_claimable":false,"name":"Efficient secretory expression of phospholipase D for the high-yield production of phosphatidylserine and phospholipid derivates from soybean lecithin.","description":"Phospholipase D (PLD) is an essential biocatalyst for the biological production of phosphatidylserine and phospholipid modification. However, the efficient heterologous expression of PLD is limited by its cell toxicity. In this study, a PLD was secretory expressed efficiently in <i>Bacillus subtilis</i> with an activity around 100 U/mL. A secretory expression system containing the signal peptide SP<sub>EstA</sub> and the dual-promoter P<sub>HpaII-SrfA</sub> was established, and the extracellular PLD activity further reached 119.22 U/mL through scale-up fermentation, 191.30-fold higher than that of the control. Under optimum reaction conditions, a 61.61% conversion ratio and 21.07 g/L of phosphatidylserine production were achieved. Finally, the synthesis system of PL derivates was established, which could efficiently synthesis novel PL derivates. The results highlight that the secretory expression system constructed in this study provides a promising PLD producing strain in industrial application, and laid the foundation for the biosynthesis of phosphatidylserine and other PL derivates. As far as we know, this work reports the highest level of extracellular PLD expression to date and the enzymatic production of several PL derivates for the first time.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2025-04-26T20:54:36.17Z","creation":"2025-04-06T16:34:35.429Z"},"accession":"S-EPMC10073938","cross_references":{"pubmed":["37033293"],"doi":["10.1016/j.synbio.2023.03.006"]}}