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

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de Melo, Vandierly Sampaio ; de Melo, Ricardo Rodrigues ; Rade, Leticia Leandro ; Miyamoto, Renan Yuji ; Milan, Natalia ; de Souza, Claudia Maria ; de Oliveira, Vinicius Martins ; Simoes, Isabelle Taira ; Lima, Evandro Antonio de ; Guilherme, Ederson Paulo Xavier ; Pinheiro, Glaucia Melina Squizato ; Ramos, Carlos Henrique Inacio ; Persinoti, Gabriela Felix ; Generoso, Wesley Cardoso ; Zanphorlin, Leticia Maria

• Document type: Journal article
• Source: Biochemical and Biophysical Research Communications; v. 733, p. 9-pg., 2024-08-26.

Abstract

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. (AU)

• FAPESP's process: 20/01967-6 - Decarboxylation enzymatic mechanisms of fatty acids into terminal olefins to obtain drop-in biofuels
• Grantee: Natalia Milan
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• FAPESP's process: 17/14253-9 - Evaluation of the biotechnological potential of the cellulolytic system of Xanthomonas axonopodis pv. citri: a structural, functional and applied approach
• Grantee: Ricardo Rodrigues de Melo
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 18/04897-9 - Production of biodiesel and renewable hydrocarbons via enzymatic route: from the enzyme synthesis to the economic evaluation of the integrated process
• Grantee: Letícia Leandro Rade
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 21/14410-2 - Study of P450 enzymes of the CYP152 family able to promote the decarboxylation of fatty acids
• Grantee: Isabelle Taira Simões
• Support Opportunities: Scholarships in Brazil - Master
• FAPESP's process: 21/14726-0 - Discovery and development of oxidative enzymes for the in vivo biosynthesis of hydrocarbons
• Grantee: Vandierly Sampaio de Melo
• Support Opportunities: Scholarships in Brazil - Doctorate
• FAPESP's process: 18/02865-2 - Molecular investigation of new xylose isomerases for application to lignocellulosic materials fermentation
• Grantee: Renan Yuji Miyamoto
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• FAPESP's process: 19/08855-1 - New mechanisms of P450: an enzymatic strategy for renewable hydrocarbons
• Grantee: Leticia Maria Zanphorlin
• Support Opportunities: Regular Research Grants