Enzymatic conversions of polar lipids. Principles, problems and solutions

Adlercreutz, Patrick; Virto, Carmen; Persson, Mattias; Vaz, Silvia; Adlercreutz, Dietlind; Svensson, Ingvar L; Wehtje, Ernst

doi:10.1016/s1381-1177(00)00015-1

Cited by 9 publications

(9 citation statements)

References 9 publications

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“…We assume it is an acyl-MGDG, formed by the addition of one acyl chain to the primary hydroxyl group of MGDG galactosyl group (Figure 6). This type of acylation transfer reaction on galactolipids in the course of lipolysis was previously observed when using fungal and bacterial lipases in organic media [15,55,56] but not yet with rGPLRP2.…”

Section: Qualitative Analysis Of Mgdg Enzymatic Hydrolysissupporting

confidence: 68%

“…They also have several potential applications in pharmaceutical [7][8][9] and food industries [10][11][12][13]. For some applications such as in nutrition, galactolipids in their native form are sufficient, but for other applications like biofuels and surfactants, it would be necessary to transform them via acyl transfer reactions using chemical or lipasebased catalysis [14,15]. Here, we present a method for the qualitative and quantitative analysis of galactolipids and their galactosylated degradation products, using Thin-Layer-Chromatography (TLC) coupled to scanning densitometry.…”

Section: Introductionmentioning

confidence: 99%

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Quantitative monitoring of galactolipid hydrolysis by pancreatic lipase-related protein 2 using thin layer chromatography and thymol-sulfuric acid derivatization

Sahaka

Amara

Lecomte

et al. 2021

Journal of Chromatography B

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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), thymolsulfuric acid as derivatization reagent and scanning densitometry for detection. Thymolsulfuric 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 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.

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Section: Qualitative Analysis Of Mgdg Enzymatic Hydrolysissupporting

confidence: 68%

Section: Introductionmentioning

confidence: 99%

Quantitative monitoring of galactolipid hydrolysis by pancreatic lipase-related protein 2 using thin layer chromatography and thymol-sulfuric acid derivatization

Sahaka

Amara

Lecomte

et al. 2021

Journal of Chromatography B

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“…propane, glycerol and hexane), microemulsions and near-critical solvents were studied with PC/LPC in the synthesis of PUFA-containing PC [24][25][26]. In studies by Na et al (1900) [27], Adlercreutz et al Previous studies suggested that the native ppPLA2 was used as catalyst in the transesterification reaction and active catalytically at a water activity of at least about 0.2 in toluene [24].…”

Section: Quantitative Analysis Of Reaction Of Ps and Dha To Form 2-dhmentioning

confidence: 99%

“…2004)[25,26] andEgger et al (1997) [28], toluene as the organic solvent was shown to increase yields in PUFA-containing PC synthesis. Glycerol, a food-compatible solvent, was used in the transesterification in current study, because the synthesized 2-DHA-PS was intended for food use.In our one-step transesterification reaction, to maximize the yield of 2-DHA-PS, variables including16 PS, rPLA2M and DHA concentrations, buffer pH, reaction temperature and reaction time were systematically tested.…”

mentioning

confidence: 99%

Characterization of the recombinant porcine pancreas phospholipase A 2 expressed in Pichia pastoris GS115 and its application to synthesis of 2-DHA-PS

Liu¹,

Huang²,

Li³

et al. 2016

Process Biochemistry

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“…Lipases from R. arrhizus and Rhizomucor miehei (Lipozyme™) were found to catalyze fatty acid exchange at the sn ‐1 position of DGDG, as well as acylation of the digalactosyl moiety, whereas lipases from Geotrichum candidum , Alcaligenes sp., and Penicillium camembertii did not 30. Several lipases with 1,3‐regioselectivity for the hydrolysis of TAGs are able to hydrolyze the ester bond at the sn ‐1 position of both glycerophospholipids and galactolipids 31.…”

Section: Introductionmentioning

confidence: 97%

The galactolipase activity of some microbial lipases and pancreatic enzymes

Amara

Lafont

Parsiegla

et al. 2013

Euro J Lipid Sci & Tech

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Several well known microbial lipases were screened for their ability to hydrolyze synthetic medium chain monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG). Fusarium solani cutinase and Thermomyces lanuginosus lipase (TLL) were found to hydrolyze MGDG at high rates (984 AE 62 and 450 AE 41 U/mg, respectively). These activities remained however lower than those measured with pancreatic lipase-related protein 2 (PLRP2) on the same substrate. As previously observed with PLRP2, galactolipid-bile salt mixed micelles were found to be the best substrate form for microbial enzymes. The galactolipid to bile salt molar ratios for measuring maximum galactolipase activities were found to be similar to those previously established with PLRP2, suggesting that bile salts have mainly an effect on the substrate and not on the enzyme itself. The galactolipase activity of cutinase and TLL, as well as human and guinea pig PLRP2s were also measured using galactolipid monomolecular films. Enzymes having a lid (TLL and human PLRP2) were found to act at higher surface pressures than those with no lid (cutinase and guinea pig PLRP2). In silico docking of medium chain MGDG and DGDG in the active site of guinea pig PLRP2 and TLL reveals some structural analogies between these enzymes.Practical applications: Galactolipase activity already finds applications in baking process with the partial lipolysis of galactolipids present in wheat flour and the in situ production of emulsifier molecules. More generally, these enzymes could be used for the enzymatic modification of galactolipids, the main plant lipids. These lipids are considered to be the most abundant at the surface of the earth and thus constitute the largest resource of fatty acids. Fax: þ33 491 715 857Abbreviations: BCEH, bovine pancreatic carboxylester hydrolase; CEH, pancreatic carboxylester hydrolase; DGDG, digalactosyldiacylglycerol; GPLRP2, guinea pig pancreatic lipase-related protein 2; HCEH, human pancreatic carboxylester hydrolase; HPL, human pancreatic lipase; HPLRP2, human pancreatic lipase-related protein 2; MGDG, monogalactosyldiacylglycerol; NaTDC, sodium taurodeoxycholate; PLRP2, pancreatic lipase-related protein 2; TAG, triacylglycerol; TC4, tributyrin; TLL, Thermomyces lanuginosus lipase; YLLIP2, Yarrowia lipolytica lipase 442Eur.

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Enzymatic conversions of polar lipids. Principles, problems and solutions

Cited by 9 publications

References 9 publications

Quantitative monitoring of galactolipid hydrolysis by pancreatic lipase-related protein 2 using thin layer chromatography and thymol-sulfuric acid derivatization

Quantitative monitoring of galactolipid hydrolysis by pancreatic lipase-related protein 2 using thin layer chromatography and thymol-sulfuric acid derivatization

Characterization of the recombinant porcine pancreas phospholipase A 2 expressed in Pichia pastoris GS115 and its application to synthesis of 2-DHA-PS

The galactolipase activity of some microbial lipases and pancreatic enzymes

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