Homologous yeast lipases/acyltransferases exhibit remarkable cold-active properties.

• Published in: Applied Microbiology and Biotechnology
• Main Authors: Neang, Pisey M, Subileau, Maeva, Perrier, Véronique, Dubreucq, Eric
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2014
• Subjects: Chimie organique; Organic chemistry; Sciences agricoles; Agricultural sciences; Biotechnologies; Antarc*; Antarctica
• Online Access: http://prodinra.inra.fr/ft/C0A61A78-A455-4600-918A-A545B33FBF53; http://prodinra.inra.fr/record/259044; https://doi.org/10.1007/s00253-014-5776-6

Lipases/acyltransferases catalyse acyltransfer to various nucleophiles preferentially to hydrolysis even in aqueous media with high thermodynamic activity of water (a w >0.9). Characterization of hydrolysis and acyltransfer activities in a large range of temperature (5 to 80 °C) of secreted recombinant homologous lipases of the Pseudozyma antarctica lipase A superfamily (CaLA) expressed in Pichia pastoris, enlighten the exceptional cold-activity of two remarkable lipases/acyltransferases: CpLIP2 from Candida parapsilosis and CtroL4 from Candida tropicalis. The activation energy of the reactions catalysed by CpLIP2 and CtroL4 was 18-23 kJ mol(-1) for hydrolysis and less than 15 kJ mol(-1) for transesterification between 5 and 35 °C, while it was respectively 43 and 47 kJ mol(-1) with the thermostable CaLA. A remarkable consequence is the high rate of the reactions catalysed by CpLIP2 and CtroL4 at very low temperatures, with CpLIP2 displaying at 5 °C 65 % of its alcoholysis activity and 45 % of its hydrolysis activity at 30 °C. These results suggest that, within the CaLA superfamily and its homologous subgroups, common structural determinants might allow both acyltransfer and cold-active properties. Such biocatalysts are of great interest for the efficient synthesis or functionalization of temperature-sensitive lipid derivatives, or more generally to lessen the environmental impact of biocatalytic processes.