A variant of Yarrowia lipolytica lipase with improved activity and enantioselectivity for resolution of 2-bromo-arylacetic acid esters

Cancino, Miguel; Bauchart, Philippe; Sandoval, Georgina; Nicaud, Jean‐Marc; André, Isabelle; Dossat, Valérie; Marty, Alain

doi:10.1016/j.tetasy.2008.06.009

Cited by 33 publications

(21 citation statements)

References 14 publications

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“…Lipases are among the most important class of industrial enzymes. In recent years, the growing demand of lipolytic enzymes has increased due to their potential use in various manufacturing processes for industrial goods such as detergent, food, cosmetics, flavour enhancers and also in pharmaceutical (Cancino et al, 2008). It is clearly known that lipases contained in latex in some plants have catalytic properties and numerous industrial applications (Paques and Macedo 2006;Mazou et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Catalytic properties of lipase from Ficus trichopoda and Euphorbia unispina latex: Study of their typoselectivity

Mazou¹,

Djossou²,

Tchobo³

et al. 2017

J. App. Bioscience.

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Objective: The search for lipase with distinct features, from plant latex is of great importance for industrial applications. The catalytic properties of lipases from Ficus trichopoda and Euphorbia unispina latex were characterized. Methodology and Results: Fresh latex from Ficus trichopoda and Euphorbia unispina were collected and dried through solar. Dried latex was taken for complete proximate analysis and their activity was analysed by thin layer chromatography. The two lipases were optimally active at pH=5 and temperature of 35°C and 50°C for Ficus trichopoda and Euphorbia unispina latex, respectively. The presence of metal ions enhances the activity of Ficus trichopoda latex, while no significant enhancement was observed in the case of Euphorbia unispina latex. Both lipases were able to hydrolyze saturated esters, and showed typo-selectivity for this group. However, the lipases are weak selective for the hydrolysis of unsaturated esters, especially for 18:2 fatty acids. Conclusions and application of finding: The enzyme from Ficus trichopoda latex was able to attack specific oil to generate free fatty acids or ester as the major product. This understanding may help in devising efficient methods to produce valuable modified oils.

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Section: Introductionmentioning

confidence: 99%

Catalytic properties of lipase from Ficus trichopoda and Euphorbia unispina latex: Study of their typoselectivity

Mazou¹,

Djossou²,

Tchobo³

et al. 2017

J. App. Bioscience.

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“…Enantiomerically pure drugs preparation through enzymatic resolution of enantiomers is an attractive subject (1). Extracellular lipase of the yeast Yarrowia lipolytica is frequently used as biocatalyst for the resolution of enantiomers in the racemic mixtures (2,3). In recent years, high-level production of extracellular lipase by Y. lipolytica has been a favorite subject for the researchers (4)(5)(6).…”

Section: Introductionmentioning

confidence: 99%

Cloning and Molecular Analysis of Extracellular Lipase Gene From Native and Mutant Yarrowia lipolytica Strains

Darvishi

2013

Jundishapur J Microbiol

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Background:The lipase enzyme of the Yarrowia lipolytica yeast is an important enzyme in pharmaceutical, food and environmental biotechnology. Objectives: The aims of the study were cloning and molecular analysis of extracellular lipase genes from DSM3286 native and U6 mutant strains of Y. lipolytica in Escherichia coli. Materials and Methods: LIP2 gene of Y. lipolytica DSM3286 and its mutant Y. lipolytica U6 were isolated and cloned in E. coli using the appropriate vector. The native and mutant extracellular lipase ORFs were sequenced for further analyses and finding the differences in the nucleotide sequences. Results: Two nucleotide substitutions were found in the extracellular lipase LIP2 ORFs of Y. lipolytica U6 mutant strain compared to the wild-type strain. In this study, the LIP2 ORF region genetic changes were found in the industrial and high-level extracellular lipase producer Y. lipolytica mutant strain. Conclusions: Results of this study could be used to find suitable targets for inverse metabolic engineering and site-directed mutagenesis to achieve stable and high-level extracellular lipase production in Y. lipolytica and other yeasts.

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“…In recent years the growing demand of lipolytic enzymes has been increased due to its potential use in the various manufacturing processes of industrial goods such as detergent industry, food industry, cosmetics, flavour enhancers and in pharmaceutical industry (Gandhi, 1997;Corzo and Revah, 1999;Cancino et al, 2008). Lipase may be used to produce fatty acids (Linder et al, 2002), aroma and flavor compounds (Athawale et al, 2003), lubricant and solvent esters (Hills, 2003), polyesters (Kumar and Gross, 2000), amides, thiol esters (Gandhi, 1997) and biomodified fats (Neklyudov et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Biochemical Studies of Lipase from Germinating Oil Seeds (Glycine max)

K.¹

2011

American Journal of Biochemistry and Biotechnology

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Problem statement:Lipase is one of the important enzymes in food, pharmaceutical, detergent and biofuels industries. Search for the lipase with distinct features, possibly from germinating seeds, is of interest for industrial applications. Approach: The lipase produced by soybean oil seeds was partially purified and characterized in terms of the optimal pH and temperature for activity as well as substrate specificity. Results: The lipase was extracted and partially purified from germinating soybean seeds using chilled acetone and ammonium sulfate precipitation. Partially purified and dialyzed enzyme profile was observed on native-Polyacrylamide Gel Electrophoresis (PAGE). The lipase was optimally active at pH 8 and temperature of 24°C. In the presence of Ca 2+ and Mg 2+ enhance the activity at low concentration, while the Hg 2+ and Ethylene Diaminotetracetic Acid (EDTA) showed inhibitory effect. The enzyme was found to be metalloenzyme. Enzyme kinetics with olive oil emulsion substrate showed k m and v max of 7.67 mg and 0.0125 µm mL min −1 , respectively. Conclusion:The mettaloenzyme enzyme was able to attack specifically on oil in seeds to generate free fatty acids as the major end product. This understanding may help in devising efficient methods to overcome the problem of soybean seed oil in stability.

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A variant of Yarrowia lipolytica lipase with improved activity and enantioselectivity for resolution of 2-bromo-arylacetic acid esters

Cited by 33 publications

References 14 publications

Catalytic properties of lipase from <i>Ficus trichopoda</i> and <i>Euphorbia unispina</i> latex: Study of their typoselectivity

Catalytic properties of lipase from <i>Ficus trichopoda</i> and <i>Euphorbia unispina</i> latex: Study of their typoselectivity

Cloning and Molecular Analysis of Extracellular Lipase Gene From Native and Mutant Yarrowia lipolytica Strains

Biochemical Studies of Lipase from Germinating Oil Seeds (<i>Glycine max</i>)

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