A polylactic acid degrading lipase from Bacillus safensis: Characterization and structural analysis

Yujun Wang; Wanting Zhang; Zhanyong Wang; Shuxia Lyu

doi:10.1016/j.ijbiomac.2024.131916

A polylactic acid degrading lipase from Bacillus safensis: Characterization and structural analysis

Int J Biol Macromol. 2024 Apr 26;268(Pt 2):131916. doi: 10.1016/j.ijbiomac.2024.131916. Online ahead of print.

Authors

Yujun Wang¹, Wanting Zhang¹, Zhanyong Wang², Shuxia Lyu³

Affiliations

¹ College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang 110866, China.
² 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. Electronic address: wangzy125@syau.edu.cn.
³ College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang 110866, China. Electronic address: lushuxia@syau.edu.cn.

PMID: 38679264
DOI: 10.1016/j.ijbiomac.2024.131916

Abstract

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.

Keywords: Biodegradable plastics; Enzymatic hydrolysis; Polylactic acid (PLA); Triacylglycerol lipase.