| Title : Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B - Jaito_2023_PLoS.One_18_e0295397 |
| Author(s) : Jaito N , Kaewsawat N , Phetlum S , Uengwetwanit T |
| Ref : PLoS ONE , 18 :e0295397 , 2023 |
| Abstract : 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 degreesC similar to CalB. The second lipase candidate demonstrated an optimal pH of 8 and a higher optimal temperature of 55 degreesC. Notably, this candidate sustained considerable activity at extreme conditions, maintaining high activity at 70 degreesC 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. |
| ESTHER : Jaito_2023_PLoS.One_18_e0295397 |
| PubMedSearch : Jaito_2023_PLoS.One_18_e0295397 |
| PubMedID: 38055755 |
| Gene_locus related to this paper: 9actn-a0a930yca5 , 9gamm-a0a2e0ixe3 |