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
• Other Authors: Département de génie chimique et de génie biotechnologique, Faculté de génie, Université de Sherbrooke (UdeS), Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA)
• Format: Article in Journal/Newspaper
• Language: English
• Published: HAL CCSD 2014
• Subjects: [CHIM.ORGA]Chemical Sciences/Organic chemistry; [SDV.SA]Life Sciences [q-bio]/Agricultural sciences; [SDV.BIO]Life Sciences [q-bio]/Biotechnology; Antarc*; Antarctica
• Online Access: https://hal.archives-ouvertes.fr/hal-01189940; https://hal.archives-ouvertes.fr/hal-01189940/document; https://hal.archives-ouvertes.fr/hal-01189940/file/Publis014-iate-008_Neang_Appl%20Microbiol%20Biotechnol_Homologous%20yeast%20lipases%20cold-active%20properties_%7BC0A61A78-A455-4600-918A-A545B33FBF53%7D.pdf; 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.