Thermoascus aurantiacus harbors an esterase/lipase that is highly activated by anionic surfactant

• Published in: Biochemical and biophysical research communications Vol. 733; p. 150572
• Main Authors: de Melo, Vandierly Sampaio, de Melo, Ricardo Rodrigues, Rade, Letícia Leandro, Miyamoto, Renan Yuji, Milan, Natalia, de Souza, Claudia Maria, de Oliveira, Vinicius Martins, Simões, Isabelle Taira, de Lima, Evandro Antonio, Guilherme, Ederson Paulo Xavier, Pinheiro, Glaucia Melina Squizato, Inacio Ramos, Carlos Henrique, Persinoti, Gabriela Felix, Generoso, Wesley Cardoso, Zanphorlin, Leticia Maria
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 12-11-2024
• Subjects: Class 3 lipase; Fungal lipolytic enzymes; Sodium dodecyl sulfate; Surfactant; Thermoascus aurantiacus; Sodium dodecyl sulfate; Class 3 lipase; Thermoascus aurantiacus; Surfactant; Fungal lipolytic enzymes
• ISSN: 0006-291X; 1090-2104; 1090-2104
• DOI: 10.1016/j.bbrc.2024.150572

Fungal lipolytic enzymes play crucial roles in various lipid bio-industry processes. Here, we elucidated the biochemical and structural characteristics of an unexplored fungal lipolytic enzyme (TaLip) from Thermoascus aurantiacus var. levisporus, a strain renowned for its significant industrial relevance in carbohydrate-active enzyme production. TaLip belongs to a poorly understood phylogenetic branch within the class 3 lipase family and prefers to hydrolyze mainly short-chain esters. Nonetheless, it also displays activity against natural long-chain triacylglycerols. Furthermore, our analyses revealed that the surfactant sodium dodecyl sulfate (SDS) enhances the hydrolytic activity of TaLip on pNP butyrate by up to 5.0-fold. Biophysical studies suggest that interactions with SDS may prevent TaLip aggregation, thereby preserving the integrity and stability of its monomeric form and improving its performance. These findings highlight the resilience of TaLip as a lipolytic enzyme capable of functioning in tandem with surfactants, offering an intriguing enzymatic model for further exploration of surfactant tolerance and activation in biotechnological applications.
•TaLip belongs to a poorly explored phylogenetic branch within class 3 lipases.•TaLip acts as an esterase with lipase properties.•SDS increases TaLip activity by up to 5-fold.•SDS avoids the formation of TaLip aggregates.•TaLip functions as a monomer in solution.