Lecomte J

References (7)

Title : Quantitative monitoring of galactolipid hydrolysis by pancreatic lipase-related protein 2 using thin layer chromatography and thymol-sulfuric acid derivatization - Sahaka_2021_J.Chromatogr.B.Analyt.Technol.Biomed.Life.Sci_1173_122674
Author(s) : Sahaka M , Amara S , Lecomte J , Rodier JD , Lafont D , Villeneuve P , Gontero B , Carriere F
Ref : Journal of Chromatography B Analyt Technol Biomed Life Sciences , 1173 :122674 , 2021
Abstract : Galactolipids are the most abundant lipids on earth where they are mainly found in photosynthetic membranes of plant, algae, and cyanobacteria. Pancreatic lipase-related protein 2 (PLRP2) is an enzyme with galactolipase activity allowing mammals, especially herbivores, to digest this important source of fatty acids. We present a method for the quantitative analysis of galactolipids and galactosylated products resulting from their digestion by guinea pig PLRP2 (GPLRP2), using thin-layer-chromatography (TLC), thymol-sulfuric acid as derivatization reagent and scanning densitometry for detection. Thymol-sulfuric acid reagent has been used for the colorimetric detection of carbohydrates. It is shown here that the derivatization of galactosyl group from galactolipids by this reagent is not affected by the bound acyl glycerol, acyl chains length and number of galactose residues in the polar head. This allowed quantifying simultaneously the initial substrate and all galactosylated products generated upon the hydrolysis of monogalactosyl di-octanoylglycerol (C8-MGDG) by GPLRP2 using a single calibration with C8-MGDG as reference standard. The reaction products, monogalactosyl monooctanoyl glycerol (C8-MGMG) and monogalactosyl glycerol (MGG), were identified and quantified, MGG being recovered from the aqueous phase and analyzed by a separate TLC analysis. This method is therefore suitable to quantify the products resulting from the release of both fatty acids present in MGDG and thereby shows that PLRP2 can contribute to the complete digestion of galactolipids and further intestinal absorption of their fatty acids.
ESTHER : Sahaka_2021_J.Chromatogr.B.Analyt.Technol.Biomed.Life.Sci_1173_122674
PubMedSearch : Sahaka_2021_J.Chromatogr.B.Analyt.Technol.Biomed.Life.Sci_1173_122674
PubMedID: 33827017

Title : The digestion of galactolipids and its ubiquitous function in Nature for the uptake of the essential alpha-linolenic acid - Sahaka_2020_Food.Funct_11_6710
Author(s) : Sahaka M , Amara S , Wattanakul J , Gedi MA , Aldai N , Parsiegla G , Lecomte J , Christeller JT , Gray D , Gontero B , Villeneuve P , Carriere F
Ref : Food Funct , 11 :6710-6744 , 2020
Abstract : Galactolipids, mainly monogalactosyl diglycerides and digalactosyl diglycerides are the main lipids found in the membranes of plants, algae and photosynthetic microorganisms like microalgae and cyanobacteria. As such, they are the main lipids present at the surface of earth. They may represent up to 80% of the fatty acid stocks, including a large proportion of polyunsaturated fatty acids mainly alpha-linolenic acid (ALA). Nevertheless, the interest in these lipids for nutrition and other applications remains overlooked, probably because they are dispersed in the biomass and are not as easy to extract as vegetable oils from oleaginous fruit and oil seeds. Another reason is that galactolipids only represent a small fraction of the acylglycerolipids present in modern human diet. In herbivores such as horses, fish and folivorous insects, galactolipids may however represent the main source of dietary fatty acids due to their dietary habits and digestion physiology. The development of galactolipase assays has led to the identification and characterization of the enzymes involved in the digestion of galactolipids in the gastrointestinal tract, as well as by microorganisms. Pancreatic lipase-related protein 2 (PLRP2) has been identified as an important factor of galactolipid digestion in humans, together with pancreatic carboxyl ester hydrolase (CEH). The levels of PLRP2 are particularly high in monogastric herbivores thus highlighting the peculiar role of PLRP2 in the digestion of plant lipids. Similarly, pancreatic lipase homologs are found to be expressed in the midgut of folivorous insects, in which a high galactolipase activity can be measured. In fish, however, CEH is the main galactolipase involved. This review discusses the origins and fatty acid composition of galactolipids and the physiological contribution of galactolipid digestion in various species. This overlooked aspect of lipid digestion ensures not only the intake of ALA from its main natural source, but also the main lipid source of energy for growth of some herbivorous species.
ESTHER : Sahaka_2020_Food.Funct_11_6710
PubMedSearch : Sahaka_2020_Food.Funct_11_6710
PubMedID: 32687132
Gene_locus related to this paper: helam-a0a2w1b5z2 , cavpo-2plrp

Title : A Two-Step Bioconversion Process for Canolol Production from Rapeseed Meal Combining an Aspergillus niger Feruloyl Esterase and the Fungus Neolentinus lepideus - Odinot_2017_Microorganisms_5_67
Author(s) : Odinot E , Fine F , Sigoillot JC , Navarro D , Laguna O , Bisotto A , Peyronnet C , Ginies C , Lecomte J , Faulds CB , Lomascolo A
Ref : Microorganisms , 5 : , 2017
Abstract : Rapeseed meal is a cheap and abundant raw material, particularly rich in phenolic compounds of biotechnological interest. In this study, we developed a two-step bioconversion process of naturally occurring sinapic acid (4-hydroxy-3,5-dimethoxycinnamic acid) from rapeseed meal into canolol by combining the complementary potentialities of two filamentous fungi, the micromycete Aspergillus niger and the basidiomycete Neolentinus lepideus. Canolol could display numerous industrial applications because of its high antioxidant, antimutagenic and anticarcinogenic properties. In the first step of the process, the use of the enzyme feruloyl esterase type-A (named AnFaeA) produced with the recombinant strain A. niger BRFM451 made it possible to release free sinapic acid from the raw meal by hydrolysing the conjugated forms of sinapic acid in the meal (mainly sinapine and glucopyranosyl sinapate). An amount of 39 nkat AnFaeA per gram of raw meal, at 55 degreesC and pH 5, led to the recovery of 6.6 to 7.4 mg of free sinapic acid per gram raw meal, which corresponded to a global hydrolysis yield of 68 to 76% and a 100% hydrolysis of sinapine. Then, the XAD2 adsorbent (a styrene and divinylbenzene copolymer resin), used at pH 4, enabled the efficient recovery of the released sinapic acid, and its concentration after elution with ethanol. In the second step, 3-day-old submerged cultures of the strain N. lepideus BRFM15 were supplied with the recovered sinapic acid as the substrate of bioconversion into canolol by a non-oxidative decarboxylation pathway. Canolol production reached 1.3 g/L with a molar yield of bioconversion of 80% and a productivity of 100 mg/L day. The same XAD2 resin, when used at pH 7, allowed the recovery and purification of canolol from the culture broth of N. lepideus. The two-step process used mild conditions compatible with green chemistry.
ESTHER : Odinot_2017_Microorganisms_5_67
PubMedSearch : Odinot_2017_Microorganisms_5_67
PubMedID: 29036919
Gene_locus related to this paper: aspni-FAEA

Title : Biodiesel production from crude jatropha oil catalyzed by immobilized lipase\/acyltransferase from Candida parapsilosis in aqueous medium - Rodrigues_2016_Bioresour.Technol_218_1224
Author(s) : Rodrigues J , Perrier V , Lecomte J , Dubreucq E , Ferreira-Dias S
Ref : Bioresour Technol , 218 :1224 , 2016
Abstract : The lipase/acyltransferase from Candida parapsilosis (CpLIP2) immobilized on two synthetic resins (Accurel MP 1000 and Lewatit VP OC 1600) was used as catalyst for the production of biodiesel (fatty acid methyl esters, FAME) by transesterification of jatropha oil with methanol, in a lipid/aqueous system. The oil was dispersed in a buffer solution (pH 6.5) containing methanol in excess (2M in the biphasic system; molar ratio methanol/acyl chains 2:1). Transesterification was carried out at 30 degrees C, under magnetic stirring, using 10% (w/w) of immobilized enzyme in relation to oil. The maximum FAME yields were attained after 8h reaction time: 80.5% and 93.8%, when CpLIP2 immobilized on Accurel MP 1000 or on Lewatit VP OC 1600 were used, respectively. CpLIP2 on both Accurel MP 1000 and Lewatit VP OC 1600 showed high operational stability along 5 consecutive 8h batches.
ESTHER : Rodrigues_2016_Bioresour.Technol_218_1224
PubMedSearch : Rodrigues_2016_Bioresour.Technol_218_1224
PubMedID: 27474957
Gene_locus related to this paper: canpa-LIP2

Title : The use of lipases as biocatalysts for the epoxidation of fatty acids and phenolic compounds - Aouf_2014_Green.Chem_16_1740
Author(s) : Aouf C , Durand E , Lecomte J , Figueroa-Espinoza MC , Dubreucq E , Fulcrand H , Villeneuve P
Ref : Green Chem , 16 :1740 , 2014
Abstract : Lipases are versatile enzymes that can be used for various kinds of biocatalyzed reactions. Owing to their selectivity and their mild reaction conditions, they can be often considered as more interesting than classical chemical catalysts. Besides their application in oil and fat processes, these enzymes have proved to be very attractive for other lipase-catalyzed reactions. This review discusses the latest results where lipases are used for the epoxidation of lipid substrates (namely fatty acids and their derivatives) and phenolic compounds. This chemo-enzymatic process involves a two step synthesis where the biocatalyst acts as a perhydrolase to produce peracids, which then act as catalysts to epoxidize double bonds. Various factors govern the efficiency of the reaction in terms of kinetics, yields and enzyme stability. These parameters are evaluated and discussed herein.
ESTHER : Aouf_2014_Green.Chem_16_1740
PubMedSearch : Aouf_2014_Green.Chem_16_1740
PubMedID:

Title : Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2 - Amara_2010_Biochim.Biophys.Acta_1801_508
Author(s) : Amara S , Barouh N , Lecomte J , Lafont D , Robert S , Villeneuve P , de Caro A , Carriere F
Ref : Biochimica & Biophysica Acta , 1801 :508 , 2010
Abstract : Monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG) are the most abundant lipids in nature, mainly as important components of plant leaves and chloroplast membranes. Pancreatic lipase-related protein 2 (PLRP2) was previously found to express galactolipase activity, and it is assumed to be the main enzyme involved in the digestion of these common vegetable lipids in the gastrointestinal tract. Most of the previous in vitro studies were however performed with medium chain synthetic galactolipids as substrates. It was shown here that recombinant guinea pig (Cavia porcellus) as well as human PLRP2 hydrolyzed at high rates natural DGDG and MGDG extracted from spinach leaves. Their specific activities were estimated by combining the pH-stat technique, thin layer chromatography coupled to scanning densitometry and gas chromatography. The optimum assay conditions for hydrolysis of these natural long chain galactolipids were investigated and the optimum bile salt to substrate ratio was found to be different from that established with synthetic medium chains MGDG and DGDG. Nevertheless the length of acyl chains and the nature of the galactosyl polar head of the galactolipid did not have major effects on the specific activities of PLRP2, which were found to be very high on both medium chain [1786+/-100 to 5420+/-85U/mg] and long chain [1756+/-208 to 4167+/-167U/mg] galactolipids. Fatty acid composition analysis of natural MGDG, DGDG and their lipolysis products revealed that PLRP2 only hydrolyzed one ester bond at the sn-1 position of galactolipids. PLRP2 might be used to produce lipid and free fatty acid fractions enriched in either 16:3 n-3 or 18:3 n-3 fatty acids, both found at high levels in galactolipids.
ESTHER : Amara_2010_Biochim.Biophys.Acta_1801_508
PubMedSearch : Amara_2010_Biochim.Biophys.Acta_1801_508
PubMedID: 20083229
Gene_locus related to this paper: human-PNLIPRP2

Title : A spectrophotometric transesterification-based assay for lipases in organic solvent - Goujard_2009_Anal.Biochem_385_161
Author(s) : Goujard L , Villeneuve P , Barea B , Lecomte J , Pina M , Claude S , Le Petit J , Ferre E
Ref : Analytical Biochemistry , 385 :161 , 2009
Abstract : A new method to evaluate lipase activities in nonaqueous conditions using vinyl ester absorbance at ultraviolet (UV) wavelengths is described. The model reaction is the transesterification between vinyl stearate and pentanol in hexane at 30 degrees C or in decane at 50 degrees C. The conversion of vinyl stearate into pentyl stearate is monitored through decreasing UV absorbance at 200 nm. Six commercial lipases were tested with this method, and results were compared with gas chromatography (GC) quantification and a classical spectrophotometric method using p-nitrophenyl palmitate. Results from the new spectrophotometric assay are similar both to results from GC quantification (R(2)=0.999) and to results from p-nitrophenyl palmitate (R(2)=0.989). The proposed method is able to evaluate both high activity from immobilized lipases such as immobilized Candida antarctica B lipase (3060 +/- 350 U g(-1)) and low activity from crude enzymatic extracts such as Carica papaya dried latex (0.1 +/- 0.04 U g(-1)). The method has also been used to measure kinetic parameters of C. antarctica B lipase for vinyl stearate and the correlation between its synthesis activity and its concentration. The method has also proved to be effective in studying the acyl selectivity of a lipase by comparing its activities with increasing chain lengths of vinyl esters.
ESTHER : Goujard_2009_Anal.Biochem_385_161
PubMedSearch : Goujard_2009_Anal.Biochem_385_161
PubMedID: 19013125