Biochemical characterization of Yarrowia lipolytica LIP8, a secreted lipase with a cleavable C-terminal region

A Temporal Evolution Perspective of Lipase Production by Yarrowia lipolytica in Solid-State Fermentation

“…Aloulou et al [50] verified lip2p aggregation to lipids after performing gel-filtration on the supernatant from production with oleic acid as lipase inducer. Kamoun et al [64] also reported aggregate formation due to the presence of lipids in samples of Lip8p. After purification with gel filtration and anion exchange chromatography, the authors have immunodetected Lip8 in supernatants as 2 species, one of 39-40 kDa and another of 37 kDa (majority), and speculated that this difference could be related to the production of a pro-enzyme that undergoes further processing outside the cell or a membrane-anchored enzyme (most likely) that suffers some cleavage to be released into the extracellular media.…”

“…All these data are summarized in Table 2. A critical aspect of produced lipases Lip2 and Lip8 is that they seem to be irreversibly inactivated by extreme pH changes and also by the lack of an emulsifying agent in the reaction media, as was shown by Aloulou et al [50] and Kamoun et al [64] using the lipolytic method.…”

Integrative computational approach for genome-based study of microbial lipid-degrading enzymes

“…Based on computational approaches, the 3D structural model of the Pseudomonas aeruginosa lipase was built using a crystal structure of acetylcholine esterase as a template, which suggested the role of the inner disulfide bond in stabilizing the enzymatically active conformation of this bacterial lipase (Jaeger et al 1993). Structural characterization of a 3D homology model of Y. lipilytica LIP8 lipase revealed post-translational modification of its C-terminus, which is a striking difference between LIP8 and its homologue, LIP2 (Kamoun et al 2015). The structural models of two bacterial esterase enzymes, belonging to the hormone-sensitive lipase-like group of the esterase/lipase family, were also constructed (Manco et al 1999(Manco et al , 2000.…”

Cleaner degreasing of sheepskins by the Yarrowia lipolytica LIP2 lipase as a chemical-free alternative in the leather industry

“…The LIP2 lipase from the yeast Yarrowia lipolytica (YLLIP2, NCBI accession number CAB91111) is an attractive enzyme that can be overproduced at industrial scale up to a level of 3 g of lipase/L of culture medium [7]. YLLIP2 is the main secreted lipase by Y. lipolytica by exhibiting more than 97% of the extracellular lipase activity [8,9]. It displays a 1,3regioselectivity that allows the hydrolysis of ester bonds at external positions of the glycerol backbone of TAG [7,10].…”