[en] Lipases are serine hydrolases that catalyze in nature the hydrolysis of ester bonds of long chain triacylglycerol into fatty acid and glycerol. However, in favorable thermodynamic conditions, they are also able to catalyze reactions of synthesis such as esterification or amidation. The non-conventional yeast Yarrowia lipolytica possesses 16 paralogs of genes coding for lipase. However, little information on all those paralogs has been yet obtained and only three isoenzymes, namely Lip2p, Lip7p and Lip8p have been partly characterized so far. Microarray data suggest that only a few of them could be expressed and that lipase synthesis seems to be dependent on the fatty acid or oil used as carbon source confirming the high adaptation of Y. lipolytica to hydrophobic substrate utilization. This review focuses on the biochemical characterization of those enzymes with special emphasis on the Lip2p lipase which is the isoenzyme mainly synthesized by Y. lipolytica. Crystallographic data highlight that this latter is a lipase sensu stricto with a lid covering the active site of the enzyme in its closed conformation. Recent findings on enzyme conditioning in dehydrated or liquid formulation, in enzyme immobilization by entrapment in natural polymers from either organic or mineral origins are also discussed together with long-term storage strategies. The development of various biotechnological applications in different fields such as cheese ripening, waste treatment, drug synthesis or human therapeutics is also presented.
Disciplines :
Microbiology
Author, co-author :
Fickers, Patrick ; Université de Liège - ULiège > Chimie et bio-industries > Bio-industries
Marty, Alain
Nicaud, Jean Marc
Language :
English
Title :
The lipases from Yarrowia lipolytica: genetics, production, regulation, biochemical characterization and biotechnological applications.
Publication date :
2011
Journal title :
Biotechnology Advances
ISSN :
0734-9750
eISSN :
1873-1899
Publisher :
Elsevier, Netherlands
Volume :
29
Issue :
6
Pages :
632-44
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
Copyright (c) 2011 Elsevier Inc. All rights reserved.
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