一株解聚酸脂脂肪酶的分离鉴定及其结构分析。
A polylactic acid degrading lipase from Bacillus safensis: Characterization and structural analysis.
机构信息
College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang 110866, China.
College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang 110866, China; Liaoning Provincial Key Laboratory for Extreme-environmental Microbiology, Shenyang Agricultural University, Shenyang 110866, China.
出版信息
Int J Biol Macromol. 2024 May;268(Pt 2):131916. doi: 10.1016/j.ijbiomac.2024.131916. Epub 2024 Apr 26.
A polylactic acid degrading triacylglycerol lipase (TGL) was identified from Bacillus safensis based on genome annotation and validated by real-time quantitative PCR. TGL displayed optimal activity at pH 9.0 and 55 °C. It maintained stability at pH 9.0 and temperatures 45 °C. The activity of TGL was found to benefit from the presence of potassium sodium ions, and low concentrations of Triton X-100. The TGL could erode the surface of polylactic acid films and increase its hydrophilicity. The hydrolysis products of polylactic acid by TGL were lactate monomer and dimer. TGL contains a classical catalytic triad structure of lipase (Ser77, Asp133, and His156) and an Ala-X-Ser-X-Gly sequence. Compared with some lipases produced by the same genus Bacillus, TGL is highly conserved in its amino acid sequence, mainly reflected in the amino acid residues that exercise the enzyme activity, including the catalytic activity center and the substrate binding sites.
从解淀粉芽孢杆菌中基于基因组注释鉴定了一种聚乳酸降解三酰基甘油脂肪酶（TGL），并通过实时定量 PCR 进行了验证。TGL 在 pH 9.0 和 55°C 时显示出最佳活性。它在 pH 9.0 和 45°C 的温度下保持稳定。发现 TGL 的活性得益于钾钠离子和低浓度 Triton X-100 的存在。TGL 可以侵蚀聚乳酸薄膜的表面并增加其亲水性。TGL 水解聚乳酸的产物为乳酸单体和二聚体。TGL 含有脂肪酶的经典催化三联体结构（Ser77、Asp133 和 His156）和 Ala-X-Ser-X-Gly 序列。与同属的一些脂肪酶相比，TGL 在其氨基酸序列上高度保守，主要反映在行使酶活性的氨基酸残基上，包括催化活性中心和底物结合位点。
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