Abstract
BackgroundSterol esterases and lipases are enzymes able to efficiently catalyze synthesis and hydrolysis reactions of both sterol esters and triglycerides and due to their versatility could be widely used in different industrial applications. Lipases with this ability have been reported in the yeast Candida rugosa that secretes several extracellular enzymes with a high level of sequence identity, although different substrate specificity. This versatility has also been found in the sterol esterases from the ascomycetes Ophiostoma piceae and Melanocarpus albomyces.ResultsIn this work we present an in silico search of new sterol esterase and lipase sequences from the genomes of environmental fungi. The strategy followed included identification and search of conserved domains from these versatile enzymes, phylogenetic studies, sequence analysis and 3D modeling of the selected candidates.ConclusionsSix potential putative enzymes were selected and their kinetic properties and substrate selectivity are discussed on the basis of their similarity with previously characterized sterol esterases/lipases with known structures.
Highlights
Sterol esterases and lipases are enzymes able to efficiently catalyze synthesis and hydrolysis reactions of both sterol esters and triglycerides and due to their versatility could be widely used in different industrial applications
Identification of conserved motifs in lipase/sterol esterase enzymes and search in public microbial genomes After the analysis of the protein sequences described as lipase/sterol-esterase with versatile activity against triglycerides and sterol esters, two conserved motifs described for α/β hydrolases of the C. rugosa-like family were identified: GGGF and GESAG
The search of putative proteins automatically annotated as sterol esterase or lipase in the 128 public genomes deposited in the Joint Genome Institute (JGI) returned only 56 sequences from 26 different genomes
Summary
Sterol esterases and lipases are enzymes able to efficiently catalyze synthesis and hydrolysis reactions of both sterol esters and triglycerides and due to their versatility could be widely used in different industrial applications. Lipases with this ability have been reported in the yeast Candida rugosa that secretes several extracellular enzymes with a high level of sequence identity, different substrate specificity. 3.1.1.3), act on ester bonds of several compounds, with acylglycerols as their natural substrates These enzymes are able to catalyze under aqueous conditions the hydrolysis of triglycerides to free fatty acids, diglycerides and monoglycerides and to carry out synthesis and trans- and interesterification reactions in the presence of organic solvents. The mammalian cholesterol esterases are the best known for their role in lipid metabolism and cholesterol absorption [3,4] but these proteins have been reported in filamentous fungi, yeast and bacteria [5,6]
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