Abstract
Yarrowia lipolytica (YL) is a “non-conventional” yeast that is capable of producing important metabolites. One of the most important products that is secreted by this microorganism is lipase, a ubiquitous enzyme that has considerable industrial potential and can be used as a biocatalyst in the pharmaceutical, food, and environmental industries. In this work, Yarrowia lipolytica lipase (YLL) was immobilized on Lewatit and Amberlite beads and is used in the enzymatic ring-opening polymerization (ROP) of cyclic esters in the presence of different organic solvents. YLL immobilized on Amberlite XAD7HP had the higher protein adsorption (96%) and a lipolytic activity of 35 U/g. Lewatit VPOC K2629 has the higher lipolytic activity (805 U/g) and 92% of protein adsorption. The highest molecular weight (Mn 10,685 Da) was achieved at 90 °C using YLL that was immobilized on Lewatit 1026 with decane as solvent after 60 h and 100% of monomer conversion.
Highlights
The non-conventional yeast Yarrowia lipolytica is of interest for fundamental research and biotechnological applications
Y. lipolytica secretes a set of valuable proteins, such as alkaline or acid proteases, RNases, phosphatases, lipases and inulinase into the medium, which are interesting for biotechnological applications
The adsorption rates of styrenic resins are attributed to stronger hydrophobic interactions between styrenic surfaces, functional groups of the resins and Yarrowia lipolytica lipase (YLL)
Summary
The non-conventional yeast Yarrowia lipolytica is of interest for fundamental research and biotechnological applications. Yarrowia lipolytica is a good model organism for protein secretion studies. Y. lipolytica secretes a set of valuable proteins, such as alkaline or acid proteases, RNases, phosphatases, lipases and inulinase into the medium, which are interesting for biotechnological applications. Lipases (E.C. 3.1.1.3) are serine hydrolases defined as triacylglycerol acylhydrolases They catalyze the hydrolysis of the ester bond of tri-, di-, and monoglycerides of long-chain fatty acids into fatty acids and glycerol. They differ from esterase (EC 3.1.1.1) due to their ability to hydrolyze triglyceride at the lipid-water interface [4]. Yarrowia lipolytica has been considered as an industrial workhorse because of its ability to produce important metabolites and intense secretory activity. The effects of lipase concentration (6–72 mg), monomer concentration (0.6–6 mmol), and temperature (70, 90 and 120 ◦ C) were evaluated
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