Abstract
Lipases have been successfully produced under submerged cultivation conditions using olive oil as carbon source and complex culture media. The aims of this study were to evaluate lipase production by Candida viswanathii in submerged cultivation with different culture medium compositions, replace olive oil with plant oils from the Amazonian region, and assess the effect of nitrogen sources. By using olive oil as the sole carbon source, C. viswanathii produced high levels of biomass and lipase with minimal nutritional requirements (potassium, magnesium, and yeast extract). Plant oils from the Amazonian region supported cell growth, and pequi oil was the best inducer for lipase production (1.66 U mL -1 ). In comparison with inorganic sources, organic nitrogen sources induced the highest levels of lipase production. Typical microbial growth and lipase production were observed using pequi oil and peptone as a nitrogen source. The selected conditions resulted in good cell growth ( Y X/S = 1.25 g g -1 ) and lipase production ( Y P/S = 118.10 U g -1 ) after 60 hours of cultivation. In conclusion, the fermentation parameters indicated that Amazonian oils are promising for lipase production by C. viswanathii , and oils modified by this enzyme can be used in the food and cosmetic industries.
Highlights
Lipases (E.C. 3.1.1.3, triacylglycerol acyl hydrolase) hydrolyze carboxylic ester bonds, releasing carboxylic acids and alcohols
Various nutrient medium compositions supplemented with 2.0% olive oil were evaluated for C. viswanathii growth and lipase production (Figure 1)
C. viswanathii cultivation revealed that medium composition mainly influenced lipase production more than microbial growth
Summary
Lipases (E.C. 3.1.1.3, triacylglycerol acyl hydrolase) hydrolyze carboxylic ester bonds, releasing carboxylic acids and alcohols. Reactions known as esterification or transesterification reactions may occur Their capacity of catalyzing such reactions with high efficiency and stability, their chemo-, regio- and enantioselectivity, as well as not requiring cofactors and being active in organic solvents render lipases very attractive and versatile enzymes from the industrial point of view (Daiha, Angeli, Oliveira, & Almeida, 2015). Lipases are distinguished by a broad substrate scope and excellent stability in various media and have participated in a wide range of industrial applications in the oleochemical, polymer, textile, biodiesel, detergent industry and others. With their excellent enantioselectivity, they belong to the most important biocatalysts for the synthesis of fine chemicals (Kourist, Hollmann, & Nguyen, 2014). These enzymes are considered to have great potential as biocatalysts in various industrial processes including the synthesis of food ingredients, detergents, drugs, and other refined products (Adrio & Demain, 2014; Barriuso, Vaquero, Prieto, & Martínez, 2016)
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