ABSTRACT
The analysis of Pleurotus ostreatus genome reveals the presence of automatically annotated 53 lipase and 34 carboxylesterase putative coding-genes. Since no biochemical or physiological data are available so far, a functional approach was applied to identify lipases from P. ostreatus. In the tested growth conditions, four lipases were found expressed, with different patterns depending on the used C source. Two of the four identified proteins (PleoLip241 and PleoLip369), expressed in both analysed conditions, were chosen for further studies, such as an in silico analysis and their molecular characterization. To overcome limits linked to native production, a recombinant expression approach in the yeast Pichia pastoris was applied. Different expression levels were obtained: PleoLip241 reached a maximum activity of 4000 U/L, whereas PleoLip369 reached a maximum activity of 700 U/L. Despite their sequence similarity, these enzymes exhibited different substrate specificity and diverse stability at pH, temperature, and presence of metals, detergents and organic solvents. The obtained data allowed classifying PleoLip241 as belonging to the "true lipase" family. Indeed, by phylogenetic analysis the two proteins fall in different clusters. PleoLip241 was used to remove the hydrophobic layer from wool surface in order to improve its dyeability. The encouraging results obtained with lipase treated wool led to forecast PleoLip241 applicability in this field.
Subject(s)
Fungal Proteins/genetics , Genome, Fungal , Lipase/genetics , Pleurotus/enzymology , Pleurotus/genetics , Animals , Carboxylesterase/chemistry , Carboxylesterase/genetics , Carboxylesterase/metabolism , Catalytic Domain , Coloring Agents , Data Mining , Fungal Proteins/chemistry , Fungal Proteins/metabolism , Industrial Microbiology , Kinetics , Lipase/chemistry , Lipase/metabolism , Models, Molecular , Phylogeny , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Substrate Specificity , WoolABSTRACT
An analysis of the scientific literature published in the last 10 years reveals a constant growth of laccase applicative research in several industrial fields followed by the publication of a great number of patents. The Green Chemistry journal devoted the cover of its September 2014 issue to a laccase as greener alternative for chemical oxidation. This indicates that laccase "never-ending story" has found a new promising trend within the constant search for efficient (bio)catalysts able to meet the 12 green chemistry principles. A survey of ancient and cutting-edge uses of laccase in different industrial sectors is offered in this review with the aim both to underline their potential and to provide inspiration for new ones. Applications in textile and food fields have been deeply described, as well as examples concerning polymer synthesis and laccase-catalysed grafting. Recent applications in pharmaceutical and cosmetic industry have also been reviewed.
