Polymorphism in the lipase genes of <i>Geotrichum candidum</i> strains

Bertolini, Maria Célia; Laramée, Louise; Thomas, David Y.; Cygler, Mirosław; Schrag, Joseph D.; Vernet, Thierry

doi:10.1111/j.1432-1033.1994.tb19921.x

Cited by 50 publications

(24 citation statements)

References 24 publications

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“…Our PCR and DNA hybridization results show that unlike some yeasts, including C. rugosa (4,25) and G. candidum (5), in which several highly homologous genes are present, Y. lipolytica probably contains a single gene encoding extracellular lipase. This is supported by the low residual extracellular lipase activity (less than 0.5 U/ml, the lower limit of detection of our assay) in strain JMY277, in which LIP2 was deleted.…”

Section: Discussionmentioning

confidence: 77%

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Characterization of an Extracellular Lipase Encoded by LIP2 in Yarrowia lipolytica

et al. 2000

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We isolated the LIP2 gene from the lipolytic yeast Yarrowia lipolytica. It was found to encode a 334-amino-acid precursor protein. The secreted lipase is a 301-amino-acid glycosylated polypeptide which is a member of the triacylglycerol hydrolase family (EC 3.1.1.3). The Lip2p precursor protein is processed by the KEX2-like endoprotease encoded by XPR6. Deletion of the XPR6 gene resulted in the secretion of an active but less stable proenzyme. Thus, the pro region does not inhibit lipase secretion and activity. However, it does play an essential role in the production of a stable enzyme. Processing was found to be correct in LIP2A (multiple LIP2 copy integrant)-overexpressing strains, which secreted 100 times more activity than the wild type, demonstrating that XPR6 maturation was not limiting. No extracellular lipase activity was detected with the lip2 knockout (KO) strain, strongly suggesting that extracellular lipase activity results from expression of the LIP2 gene. Nevertheless, the lip2 KO strain is still able to grow on triglycerides, suggesting an alternative pathway for triglyceride utilization in Y. lipolytica. This yeast naturally secretes several proteins, depending on the growth conditions (21). For example, if the pH is higher than 6, it secretes an alkaline extracellular protease (AEP) (33,38). Under optimal conditions, up to 1 g of AEP is secreted per liter (37). AEP is encoded by XPR2 (11,27,33). This gene codes for a 454-amino-acid (aa) prepro enzyme precursor containing a 15-aa signal sequence and a stretch of nine X-Ala or X-Pro dipeptides, followed by a 124-aa pro region that includes a glycosylation site (Asn 123 ) and a Lys 156 -Arg 157 processing site, and finally the mature form itself. The AEP precursor undergoes complex processing (27). A diaminopeptidase processes the stretch of nine dipeptides (X-Ala or X-Pro) (28,29), and the endoprotease encoded by the XPR6 gene is required to cleave the pro region, releasing the mature form (14). The pro region is involved in both the inhibition of protease activity and the folding of the propeptide into a conformation compatible with secretion, and secretion at 28°C depends on the glycosylation of the pro region (15, 28).Several enzymes are secreted by Y. lipolytica, and lipase and esterase activities have been detected and analyzed in various studies. Lipase secretion was first reported in 1948 by Peters and Nelson (41, 42), who described a single type of glucoserepressible activity. An extracellular and two cell-bound types of activity corresponding to lipase I (39 kDa) and lipase II (44 kDa) were described by Ota and coworkers (39, 47). The extracellular lipase required oleic acid as a stabilizer-activator, whereas the cell-bound lipases did not and differed in several properties from the extracellular enzyme (40). The rates of production of the extracellular and cell-bound enzymes were reported to depend on the carbon and nitrogen composition of the medium. Extracellular lipase was only detected in cultures grown with an organic nitrogen so...

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Section: Discussionmentioning

confidence: 77%

“…Such multicomponent gene families have been observed in other yeasts. A lipase family of five genes, with 80% identity, has been isolated in Candida rugosa (4,25), and two genes have been isolated in Geotrichum candidum (5).…”

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confidence: 99%

Characterization of an Extracellular Lipase Encoded by LIP2 in Yarrowia lipolytica

et al. 2000

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“…Also, Yan et al 28 , by expressing a 64 kDa lipase from G. geotrichum Y05 in P. pastoris GS115 and pPIC9K, obtained 1.22-fold (ammonium sulphate precipitation), 2.8-fold (anion exchange chromatography), and 3.2-fold (gel filtration chromatography) purification. Additionally, Bertolini et al 96 expressed G. candidum lipases I and II in S. cerevisiae, and significant differences between them were observed as lipase I presented much more affinity to long fatty acyl chains substrates than lipase II.…”

Section: Purification and Characterization Of Geotrichum Spp Lipasesmentioning

confidence: 99%

A Review on Geotrichum Lipases: Production, Purification, Immobilization and Applications

Maldonado

Lopes

Aguiar‐Oliveira

et al. 2017

Chem.Biochem.Eng.Q.

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Lipases are enzymes produced from innumerous microorganisms, plants and animal cells. They catalyze reactions of different lipid sources. The Geotrichum fungi are good producers of lipases with high hydrolytic activity and specificity for unsaturated fatty acids. A great number of studies have reported the importance of lipase from this genus and described important fermentation parameters for the enzyme production, such as nutrients, temperature, pH, inoculum, time of fermentation and others. Furthermore, different strategies have been used to purify and immobilize lipases from Geotrichum and innumerous applications are cited in different processes as polyunsaturated fatty acids enrichment, hydrolysis and esterification of fat and oils, synthesis of aromas, biodiesel, and many others. This review highlights fundamental aspects of the production, purification, characterization, immobilization, and the applications of lipases produced by the genus Geotrichum.

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“…Besides, Bertollini et al described that lipases can have different mechanisms able to promote their adaptation in different reaction media [31].…”

Section: Specificity Of the Concentrated Lipase Extract In Terms Of Ementioning

confidence: 99%

Concentration, Partial Characterization, and Immobilization of Lipase Extract from P. brevicompactum by Solid-State Fermentation of Babassu Cake and Castor Bean Cake

Silva

Freire²,

Castro

et al. 2011

Appl Biochem Biotechnol

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One relevant limitation hindering the industrial application of microbial lipases has been attributed to their production cost, which is determined by the production yield, enzyme stability among other. The objective of this work was to evaluate the concentration and immobilization of lipase extracts from Penicillium brevicompactum obtained by solid-state fermentation of babassu cake and castor bean cake. The precipitation with ammonium sulfate 60% of saturation of crude extract obtained with babassu cake as raw material showed an enhancement in hydrolytic and esterification activities from 31.82 to 227.57 U/g and from 170.92 to 207.40 U/g, respectively. Concentrated lipase extracts showed preference to medium-chain triglycerides and fatty acids. It is shown that the enzyme activity is maintained during storage at low temperatures (4 and -10°C) for up to 30 days. Higher esterification activities were achieved when the lipase extract was immobilized in sodium alginate and activated coal.

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Polymorphism in the lipase genes of Geotrichum candidum strains

Cited by 50 publications

References 24 publications

Characterization of an Extracellular Lipase Encoded by LIP2 in Yarrowia lipolytica

Characterization of an Extracellular Lipase Encoded by LIP2 in Yarrowia lipolytica

A Review on Geotrichum Lipases: Production, Purification, Immobilization and Applications

Concentration, Partial Characterization, and Immobilization of Lipase Extract from P. brevicompactum by Solid-State Fermentation of Babassu Cake and Castor Bean Cake

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