In this study, we characterised a novel lysophospholipase (LysoPL) from the L. mucosae LM1 strain. The gene, LM-lysoPL, encoding LysoPL from L. mucosae LM1 was cloned, analyzed, and expressed. LM-lysoPL contained a conserved region and catalytic triad motif responsible for lysophospholipase activity. After purification, UHPLC-MS analysis showed that recombinant LM-LysoPL hydrolyzed phosphatidic acid, generating lysophosphatidic acid. The enzyme had greater hydrolytic activity against C16 and C18 fatty acids, indicating a preference for long-chain fatty acids. Enzymatic assays showed that the optimal pH and temperature of recombinant LM-LysoPL were 7 and 30 °C, respectively, and it was enzymatically active within a narrow pH range. To the best of our knowledge, this is the first study to identify and characterize a lysophospholipase from lactic acid bacteria. Our findings provide a basis for understanding the probiotic role of L. mucosae LM1 in the gut.

中文翻译：

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来自黏膜乳杆菌的溶血磷脂酶的表征

在这项研究中，我们表征了一种来自黏膜 L. LM1 菌株的新型溶血磷脂酶 (LysoPL)。基因 LM-lysoPL 编码来自黏膜乳杆菌 LM1 的 LysoPL 被克隆、分析和表达。LM-lysoPL 包含一个保守区域和负责溶血磷脂酶活性的催化三联体基序。纯化后UHPLC-MS分析表明重组LM-LysoPL水解磷脂酸，生成溶血磷脂酸。该酶对 C16 和 C18 脂肪酸具有更高的水解活性，表明偏爱长链脂肪酸。酶学分析表明，重组 LM-LysoPL 的最佳 pH 和温度分别为 7 和 30 °C，并且在狭窄的 pH 范围内具有酶活性。据我们所知，这是第一项从乳酸菌中鉴定和表征溶血磷脂酶的研究。我们的研究结果为了解黏膜 LM1 在肠道中的益生菌作用提供了基础。