Molecular and Structural Characterizations of Lipases from Chlorella by Functional Genomics

Microalgae have been poorly investigated for new-lipolytic enzymes of biotechnological interest. In silico study combining analysis of sequences homologies and bioinformatic tools allowed the identification and preliminary characterization of 14 putative lipases expressed by Chlorella vulagaris. These proteins have different molecular weights, subcellular localizations, low instability index range and at least 40% of sequence identity with other microalgal lipases. Sequence comparison indicated that the catalytic triad corresponded to residues Ser, Asp and His, with the nucleophilic residue Ser positioned within the consensus GXSXG pentapeptide. 3D models were generated using different approaches and templates and demonstrated that these putative enzymes share a similar core with common alpha/beta hydrolases fold belonging to family 3 lipases and class GX. Six lipases were predicted to have a transmembrane domain and a lysosomal acid lipase was identified. A similar mammalian enzyme plays an important role in breaking down cholesteryl esters and triglycerides and its deficiency causes serious digestive problems in human. More structural insight would provide important information on the enzyme characteristics.

Automated summary

A study combining in silico analysis and bioinformatic tools identified and characterized 14 putative lipases expressed by Chlorella vulgaris, with diverse molecular weights, subcellular localizations, and sequence similarities. These lipases share a similar core with common alpha/beta hydrolases fold and belong to family 3 lipases and class GX, with some predicted to have transmembrane domains and a lysosomal acid lipase identified. Further structural insights are needed for understanding their enzymatic characteristics.