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Studies for lipase production ability of Aspergillus sp. strains from the Misiones rainforest of Paranaense.
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  • Laura Ester Ortellado ,
  • Laura Villalba,
  • Pedro Zapata,
  • Maria Fonseca
Laura Ester Ortellado
Universidad Nacional de Misiones Instituto de Biotecnologia Misiones Dra Maria Ebe Reca

Corresponding Author:[email protected]

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Laura Villalba
Universidad Nacional de Misiones Instituto de Biotecnologia Misiones Dra Maria Ebe Reca
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Pedro Zapata
Universidad Nacional de Misiones Instituto de Biotecnologia Misiones Dra Maria Ebe Reca
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Maria Fonseca
Universidad Nacional de Misiones Instituto de Biotecnologia Misiones Dra Maria Ebe Reca
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Abstract

The lipases produced by fungi of the genus Aspergillus are mostly extracellular enzymes that are secreted into the environment. These lipases have broad substrate specificity and are capable of hydrolyzing a variety of lipids, including triglycerides, phospholipids, cholesterol esters, and free fatty acids, making them the focus of many studies on their applications. The present work carried out an exploratory analysis of the production of lipases in fungi of the genus Aspergillus isolated in the Misiones rainforest of Paranaense. Using qualitative detection techniques with Tween 80 % and rhodamine B as substrates, and based on the quantitative analysis conducted, it was determined that the isolate Aspergillus sp. LBM 054 exhibited the highest lipase production capacity with a total of 133 U mL-1. A Plackett-Burman statistical test found that adding tributyrin to the culture medium increased lipase activity (P<0.05). Among the evaluated concentrations, the addition of 2% tributyrin demonstrated the highest increase in lipase activity, reaching a fivefold increase compared to the initial activity observed at the beginning of the trials. The optimal activity and high stability at neutral to alkaline pH values make these enzymes suitable for various biotechnological applications. The zymogram gel of the selected strain showed an enzymatic profile, where the protein’s molecular mass was 38 kDa.