Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B.

• Published in: PLOS ONE
• Main Authors: Nongluck Jaito, Nattha Kaewsawat, Suthathip Phetlum, Tanaporn Uengwetwanit
• Format: Article in Journal/Newspaper
• Language: English
• Published: Public Library of Science (PLoS) 2023
• Subjects: Medicine; R; Science; Q; Antarc*; Antarctica
• Online Access: https://doi.org/10.1371/journal.pone.0295397; https://doaj.org/article/68128c2beee0475a84a4f74136dc2316

Here we employed sequence-based and structure-based screening for prospecting lipases that have structural homolog to Candida antarctica lipase B (CalB). CalB, a widely used biocatalyst, was used as structural template reference because of its enzymatic properties. Structural homolog could aid in the discovery of novel wild-type enzymes with desirable features and serve as a scaffold for further biocatalyst design. The available metagenomic data isolated from various environments was leveraged as a source for bioprospecting. We identified two bacteria lipases that showed high structural similarity to CalB with <40% sequence identity. Partial purification was conducted. In comparison to CalB, the enzymatic characteristics of two potential lipases were examined. A candidate exhibited optimal pH of 8 and temperature of 50°C similar to CalB. The second lipase candidate demonstrated an optimal pH of 8 and a higher optimal temperature of 55°C. Notably, this candidate sustained considerable activity at extreme conditions, maintaining high activity at 70°C or pH 9, contrasting with the diminished activity of CalB under similar conditions. Further comprehensive experimentation is warranted to uncover and exploit these novel enzymatic properties for practical biotechnological purposes.