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The Lipases from Y. lipolytica: Genetics, Production, Regulation, and Biochemical Characterization

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Yarrowia lipolytica

Part of the book series: Microbiology Monographs ((MICROMONO,volume 25))

Abstract

The yeast Yarrowia lipolytica possesses multiple paralogues of genes dedicated to hydrophobic substrates metabolization. Among them, 16 lipase encoding genes, involved in lipid or grease breakdown, were highlighted in the yeast genome. However, little information on all those paralogues has been yet obtained. Microarray data suggest that only a few of them could be expressed. Lipase synthesis seems to be dependent on the fatty acid or oil used as carbon source confirming the high adaptation of Y. lipolytica to different hydrophobic substrate. 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. The 3D structure of this lipase established by homology modeling confirms that Lip2p 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 and in enzyme immobilization by entrapment in natural polymers from either organic or mineral origins are also discussed together with long-term storage strategies.

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Correspondence to Patrick Fickers .

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Fickers, P., Sauveplane, V., Nicaud, JM. (2013). The Lipases from Y. lipolytica: Genetics, Production, Regulation, and Biochemical Characterization. In: Barth, G. (eds) Yarrowia lipolytica. Microbiology Monographs, vol 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-38583-4_3

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