Lipase from Yarrowia lipolytica: Production, characterization and application as an industrial biocatalyst

• Published in: Journal of molecular catalysis. B, Enzymatic Vol. 101; pp. 148 - 158
• Main Authors: Brígida, Ana I.S., Amaral, Priscilla F.F., Coelho, Maria A.Z., Gonçalves, Luciana R.B.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01-03-2014; Elsevier
• Subjects: Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnological applications; Biotechnology; Enzyme production; Fundamental and applied biological sciences. Psychology; Immobilization; Methods. Procedures. Technologies; Separation and purification; Yarrowia lipolytica lipase; Immobilization; Biotechnological applications; Yarrowia lipolytica lipase; Enzyme production; Separation and purification; Ascomycota; Biotechnology; Purification; Separation; Enzyme; Triacylglycerol lipase; Esterases; Carboxylic ester hydrolases; Biocatalyst; Fungi; Characterization; Production; Hydrolases; Application; Yarrowia lipolytica
• ISSN: 1381-1177; 1873-3158
• DOI: 10.1016/j.molcatb.2013.11.016

•The review deals with current state of art in Yarrowia lipolytica lipase (YLL).•The immobilization of YLL in different supports is discussed.•Stability of YLL and potential in biotechnological applications is also outlined.
Yarrowia lipolytica (YL) is a “non-conventional” yeast that is capable of producing important metabolites. One of the most important products 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. This review discusses the efforts that have been made to use YL lipase as an industrial biocatalyst, including enzyme production and recovery. Special attention is given to a compilation of relevant information on enzyme separation and purification, since it is a key step for LYL application, that is not detailed in other reviews in the field. Because immobilized enzymes are preferentially used as commercial lipases, the methods of immobilization are also discussed and important biotechnological applications are addressed.