Abstract
Avocado represents one of the most nutritious and consumed foods in Mexico, and its export generates significant profits; because of its fatty acids content, the avocado oil was used as an inducer for the synthesis of extracellular lipases from the non-conventional yeast Kluyveromyces marxianus L-2029. Lipases are able to catalyze acyl glycerides, hydrolyzing them into fatty acids and glycerol; they have several applications in various industries. In order to determine the ideal initial avocado oil concentration in the culture medium for the yeast, the induction was carried out at different concentrations in incubation for 24 h. The yeast presented the greater extracellular lipase productivity at a 3.5% v/v avocado oil concentration, with a 3.47 μmol PNF/mg prot * min (U/mL) maximum activity. The enzymatic extract obtained at this condition had an optimum lipase activity temperature of 36 °C and pH 6. The pYJR10W lipase was detected in the enzymatic extract from avocado oil induction, and is therefore responsible for the extracellular lipase activity of K. marxianus.
Highlights
Lipases are enzymes that catalyze a wide variety of reactions, such as the partial or total hydrolysis of triacylglycerides, and synthesis reactions, which are classified into two main types of reactions: esterification and transesterification (Colla et al, 2010)
The main objective of this work was to determine the best concentration of avocado oil for the induction of the synthesis of the extracellular lipase from K. marxianus L-2029, as well as their subsequent identification and partial characterization
The K. marxianus strain was previously isolated from spontaneous fermentations in the production of Mezcal (González-Hernández et al, 2012) and it was deposited in the National Collection of Microbial Strains and Cultures (CDBB) from CINVESTAV with registration number L-2029
Summary
Lipases are enzymes that catalyze a wide variety of reactions, such as the partial or total hydrolysis of triacylglycerides, and synthesis reactions, which are classified into two main types of reactions: esterification and transesterification (Colla et al, 2010). The lipases are serine enzymes defined as triacylglycerol acyl hydrolases (EC 3.1.1.3), capable of hydrolyzing long chain acylglycerol carboxylic esters, with chains greater than 10 carbon atoms, which distinguishes them from esterases (Casas-Godoy et al, 2009). This type of enzymes has a high importance in the industry thanks to its multiple applications in the degradation of substrates with high fat content, as well as in esterification reactions carried out in the food, paper, pharmaceutical, energy and cosmetic industries (Diez & Sandoval, 2012; Sharma et al, 2001). Lipase production alternatives have been continuously searched, in order to identify enzymes with potential characteristics for various biotechnological applications
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