Diglyceride lipase: a pathway for arachidonate release from human platelets.
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Arachidonic Acids↗
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Biosynthesis of galactolipids by enzyme preparations from spinach leaves.
The pH optimum for galactolipid synthesis from UDP-galactose by spinach chloroplasts is 7.2 in Tris-HCl or phosphate buffer. The products include sterol glycosides, trigalactosyl diglyceride (tentatively identified), digalactosyl diglyceride, and monogalactosyl diglyceride in increasing order of quantity. The proportion of monogalactosyl diglyceride decreases and that of digalactosyl diglyceride increases as the pH is lowered. The galactolipid synthesis is quite resistant to elevated temperature; maximal incorporation of galactose from UDP-galactose was observed at 45 degrees C. The proportion of monogalactosyl diglyceride was greater at the higher temperatures. As much as 40% of the galactolipid-synthesizing capability of a spinach leaf homogenate is not sedimented by centrifugation for 60 min at 100,000 g. An acetone powder of spinach chloroplasts contains enzymes which catalyze galactolipid synthesis. This preparation is dependent on added diglycerides in order to make galactolipid, whereas the chloroplast preparation is not dependent on added diglycerides. Molecular species of diglycerides were compared as requirements for galactolipid synthesis. The requirement was satisfied best by the diglycerides of highest unsaturation. Methylation of the free hydroxyl of the diglyceride eliminated the effectiveness.
Chloroplasts↗
The reaction of phosphoglycolipids and other lipids with hydrofluoric acid.
1. The use of HF as a dephosphorylating reagent for phospholipids was examined. 2. Hydrolysis of phosphatidylethanolamine at 0 degrees C for 24h with 60% HF gives a good yield of diglyceride. Under similar conditions phosphatidyldiglucosyl diglyceride gives diglyceride and diglucosyl diglyceride. 3. The glycolipid is also obtained from hydrolysis of glycerylphosphoryldiglucosyl diglyceride. No lyso derivative of the glycolipid could be detected and the glycosidic linkage was also stable. 4. Triglycerides, unsaturated and cyclopropane fatty acids were unaffected by the reagent. 5. 1,2-Diglycerides and 1,3-diglycerides were partially isomerized and also gave small amounts of free fatty acid and monoglyceride. 6. Monoglycerides underwent extensive rearrangement to form 1,2- and 1,3-diglycerides. 7. Lysophosphatidylethanolamine also gave 1,2- and 1,3-diglycerides as well as monoglycerides. 8. The application of this procedure to the structure determination of various phosphoglycolipids is discussed.
Acids↗
Partial purification and properties of CTP:phosphatidic acid cytidylyltransferase from membranes of Escherichia coli.
The cytosine liponucleotides CDP-diglyceride and dCDP-diglyceride are key intermediates in phospholipid biosynthesis in Escherichia coli (C. R. H. Raetz and E. P. Kennedy, J. Biol. Chem. 248:1098--1105, 1973). The enzyme responsible for their synthesis, CTP:phosphatidic acid cytidylytransferase, was solubilized from the cell envelope by a differential extraction procedure involving the detergent digitonin and was purified about 70-fold (relative to cell-free extracts) in the presence of detergent. In studies of the heat stability of the enzyme, activity decayed slowly at 63 degrees C. Initial velocity kinetic experiments suggested a sequential, rather than ping-pong, reaction mechanism; isotopic exchange reaction studies supported this conclusion and indicated that inorganic pyrophosphate is released before CDP-diglyceride in the reaction sequence. The enzyme utilized both CTP and dCTP as nucleotide substrate for the synthesis of CDP-diglyceride and dCDP-diglyceride, respectively. No distinction was observed between CTP and dCTP utilization in any of the purification, heat stability, and reaction mechanism studies. In addition, CTP and dCTP were competitive substrates for the partially purified enzyme. It therefore appears that a single enzyme catalyzes synthesis of both CDP-diglyceride and dCDP-diglyceride in E. coli. The enzyme also catalyzes a pyrophosphorolysis of CDP-diglyceride, i.e., the reverse of its physiologically important catalysis.
Cell Membrane↗
Reversed cubic phase with membrane glucolipids from Acholeplasma laidlawii. 1H, 2H, and diffusion nuclear magnetic resonance measurements.
Monoglucosyl diglyceride and diglucosyl diglyceride are the dominant lipids of the Acholeplasma laidlawii membrane. Diglucosyl diglyceride forms a lamellar liquid crystalline phase with water while monoglucosyl diglyceride forms a reversed hexagonal phase. Depending on the amounts of unsaturated acyl chains of the lipids, a mixture of monoglucosyl diglyceride and diglucosyl diglyceride forms lamellar or reversed cubic phases at physiological temperatures. A high degree of cis unsaturation favors formation of the cubic phase with increasing monoglucosyl diglyceride content. The structure of the cubic phase is composed of aggregates, where the lipids can diffuse over macroscopical distances. A structure containing close-packed spherical micelles is therefore ruled out, and the NMR diffusion data are compatible with other previously proposed cubic bicontinuous structures [Luzzati, V., & Spegt, P. A. (1967) Nature (London) 215, 701; Scriven, L. E. (1976) Nature (London) 263, 123; Lindblom, G., Larsson, K., Johansson, L. B.-A., Fontell, K., & Forsén, S. (1979) J. Am. Chem. Soc. 101, 5465]. Monoglucosyl diglyceride/diglucosyl diglyceride ratios forming cubic phases have not been observed in vivo. It is concluded that formation of the cubic phase is strongly dependent on the molecular shape of the lipids. The results are significant for the physiological regulation of the lipid composition in A. laidlawii membranes as well as for the function and organization of biological membranes in general.
Acholeplasma laidlawii↗
Regulation of protein kinase C activity by lipids.
Protein kinase C is activated by the simultaneous presence of phospholipid, a diglyceride, and Ca2+. Under physiological conditions the activity of the enzyme is regulated by the availability of diglycerides, which are the products of phosphoinositide hydrolysis. The phospholipid-kinase interactions appear not to be of a highly specific nature. Phosphatidylserine (PS) is presumed to be the endogenous lipid that interacts with the kinase, but other acidic lipids can substitute. On the other hand, the kinase-diglyceride interactions are highly specific in nature, as would be expected of a physiological regulator. These interactions are stereo-specific and stoichiometric with respect to diglyceride. The specificity is directed toward the glycerol backbone and hydrophilic oxygen moieties of the diglyceride. The removal of one or more of the oxygen atoms or the addition of a single methyl group to the glycerol backbone virtually abolishes the activity of a putative diglyceride activator. The extreme specificity of the kinase toward the diglycerides, however, must be contrasted with the abilities of structurally diverse tumor promotors and irritants to activate the kinase. Specific small-molecule antagonists of protein kinase C have yet to be developed. The small-molecule antagonists that have been developed so far have been relatively nonspecific cationic lipids that appear to function by interfering with the interaction between the acidic phospholipids and Ca2+.
Binding Sites↗
Glyceroglucolipids of the human saliva.
Seven individual glycolipids (I--VII) have been isolated from the lipid extract of human saliva. All glycolipids contained glucose, glyceryl ethers and fatty acids, and differed from each other primarily with respect to the number of glucose residues. In addition, glycolipid V contained also the sulfate ester group. The structures of these glycolipids were identified by partial acid and alkaline hydrolysis, oxidation with periodate and chromium trioxide and methylation studies, as: Glc(alpha1 leads to 3)-diglyceride (glycolipid I), Glc(alpha1 leads to 6)Glc(alpha1 leads to 3)-diglyceride (glycolipids II and III), Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 3)-diglyceride (glycolipid IV), SO3H-6Glc(alpha1 leads to 6)Glc(alpha1 leads to 3)-diglyceride (glycolipid V), Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 3)-diglyceride (glycolipid VI) and Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 6)Glc(alpha1 lead to 6)Glc(alpha1 leads to 6)Glc(alpha1 leads to 3)-diglyceride (glycolipid VII). Diglyceride portion of these compounds consists of 1-O-alkyl-2-O-acyl-glycerol with the docosanoate and glyceryl-monodocosyl being the predominant acyl and alkyl components.
Diglycerides↗
Immunological properties of glycolipids from membranes of Acholeplasma laidlawii.
Glycolipids, the predominant class of lipids in the membranes of Acholeplasma laidlawii, are the haptenic determinants that react with anti-A. Laidlawii serum to fix complement. The predominant complement-fixing activity of the membrane glycolipids was associated with the monoglucoysyl diglyceride, diglucosyl diglyceride, glycerlphosphoryl diglucosyl diglyceride (GPDD), and an unknown lipid B, which did not react with ninhydrin but release glucose and glycerol and traces of phosphorus upon hydrolysis. The glycolipids monoglucosyl diglyceride and diglucosyl diglyceride or GPDD and unknown lipid B were paired as a result of their cross-reactions with selective antisera prepared with the aid of reconstituted membrane complexes containing membrane lipids. Reconstituted membrane complexes assembled from [14C]monoglucosyl diglyceride and delipidated membrane proteins gave optimal complement fixation titers before saturation of the complexes with the ]14C]monoglucosyl diglyceride. The phosphoglycolipid of the membrane, GPDD, was anticomplementary as a pure lipid, a cholesterol liposome, and a reconstituted membrane complex. This anticomplementary activity, which was caused by 3 mug of pure GPDD, affected both human and guinea pig complement. Although human C1, C4, C3, and C5 were not inhibited by GPDD, C2 was inhibited 10-fold by reconstituted membrane complexes containing 150 mug of GPDD. A role for this phosphoglycolipid is discussed in the hypothetical mechanism of inhibition of C2 attachment to SAC1, 4 sites.
Acholeplasma laidlawii↗
Sustained diacylglycerol formation from inositol phospholipids in angiotensin II-stimulated vascular smooth muscle cells.
Angiotensin II acts on cultured rat aortic vascular smooth muscle cells to stimulate phospholipase C-mediated hydrolysis of membrane phosphoinositides and subsequent formation of diacylglycerol and inositol phosphates. In intact cells, angiotensin II induces a dose-dependent increase in diglyceride which is detectable after 5 s and sustained for at least 20 min. Angiotensin II (100 nM)-stimulated diglyceride formation is biphasic, peaking at 15 s (227 +/- 19% control) and at 5 min (303 +/- 23% control). Simultaneous analysis of labeled inositol phospholipids shows that at 15 s phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 4-phosphate (PIP) decline to 52 +/- 6% control and 63 +/- 5% control, respectively, while phosphatidylinositol (PI) remains unchanged. In contrast, at 5 min, PIP2 and PIP have returned toward control levels (92 +/- 2 and 82 +/- 4% control, respectively), while PI has decreased substantially (81 +/- 2% control). The calcium ionophore ionomycin (15 microM) stimulates diglyceride accumulation but does not cause PI hydrolysis. 4 beta-Phorbol 12-myristate 13-acetate, an activator of protein kinase C, inhibits early PIP and PIP2 breakdown and diglyceride formation, without inhibiting late-phase diglyceride accumulation. Thus, angiotensin II induces rapid transient breakdown of PIP and PIP2 and delayed hydrolysis of PI. The rapid attenuation of polyphosphoinositide breakdown is likely caused by a protein kinase C-mediated inhibition of PIP and PIP2 hydrolysis. While in vascular smooth muscle stimulated with angiotensin II inositol 1,4,5-trisphosphate formation is transient, diglyceride production is biphasic, suggesting that initial and sustained diglyceride formation from the phosphoinositides results from different biochemical and/or cellular processes.
Angiotensin II↗
Differential activation of platelet phospholipases by thrombin and ionophore A23187.
Although exposure of platelets to ionophore A23187 causes some activation of phospholipase C, ionophore is an inefficient stimulus for this enzyme. A23187 induces the formation of one-fourth to one-sixth as much diglyceride as does thrombin when comparable amounts of phosphatidylinositol are hydrolyzed. We have shown previously that in the presence of indomethacin thrombin-treated platelets accumulate significant quantitites of diglyceride via inhibition of diglyceride lipase. However, a similar accumulation of diglyceride does not occur when ionophore is used as a stimulus in the presence of indomethacin. Ionophore does not appear to be stimulating the catabolism of diglyceride, since the simultaneous addition of ionophore and thrombin does not impair the formation and metabolism of diglyceride which is promoted by thrombin alone. Further, whereas indomethacin exerts no inhibitory effects upon phospholipase C or the formation of diglyceride in platelets responding to either stimulus, indomethacin does inhibit 1) the loss of arachidonic acid from phosphatidylcholine in response to thrombin and 2) the loss of arachidonic acid from phosphatidylcholine and phosphatidylinositol in response to A23187. We conclude that in A23187-activated platelets, phosphatidylinositol is hydrolyzed primarily by an enzyme other than phospholipase C. This indomethacin-inhibitable enzyme is probably a phospholipase A. Therefore, the full expression of phospholipase C in platelets requires more than a general flux in intracellular calcium.
Anti-Bacterial Agents↗
Polygalactolipids in spinach chloroplasts.
Two polygalactolipids, designated as components A and B, were isolated from spinach chloroplasts and were also obtained from glycolipid products synthesized with chloroplast enzymes using uridine diphosphate galactose as a galactose donor. These lipids were purified by column and thin layer chromatography. Chemical analysis of component A indicates that the lipid is trigalactosyl diglyceride, whereas component B behaves like tetragalactosyl diglyceride on a thin layer plate. The major fatty acid in trigalactosyl diglyceride was alpha-linolenic acid. Relative amount (molar ratio) of galactolipids in spinach chloroplasts was monogalactosyl diglyceride:digalactosyl diglyceride:trigalactosyl diglyceride:(tetragalactosyl diglyceride) = 60:30:5:1.
Chloroplasts↗
Metabolism of oleic acid in differentiating BFC-1 preadipose cells.
Incorporation of [3H]oleate and [14C]glucose into cellular lipids was studied in the preadipose cell line BFC-1 to determine flux changes that accompany the adipose conversion process. Dilution of oleate by intracellular fatty acids (FA) was estimated from the 3H/14C incorporation ratios and from relating steady-state radioactivity in diglycerides to their measured cellular levels. The data indicated that exogenous FA mixed with less than 1% of endogenous FA on its pathway to esterification. Conversion of preadipocytes to adipocytes increased uptake of FA and glucose by approximately 3-fold and synthesis of diglycerides and triglycerides by 5- and 16-fold, respectively, with little if any increase of phospholipid synthesis. A 50% drop in 3H/14C incorporation ratio indicated a doubling of the rate at which endogenous FA mixed with the exogenous FA that had entered the cell. Adipocytes compared with preadipocytes exhibited a 50% greater cell diameter and a doubling of intracellular water volume and of protein and phospholipid levels, reflecting cellular enlargement consequent to the arrest of cell division that precedes adipose conversion. Diglyceride levels were also increased in adipocytes, however, since their turnover was fast, as indicated by rapid equilibration of diglyceride labeling; the increase reflected changes in their relative rates of synthesis and disposal. Diglyceride levels related to cell phospholipid, and other indexes of cell size remained constant. This indicated that the supply of diglycerides was tightly coupled to the synthesis of triglycerides and phospholipids, which suggested feedback regulation of diglyceride formation. The studies provide a methodological approach to measurement and interpretation of rates of lipid deposition in cultured cells.
Adipose Tissue↗
Alpha-thrombin-induced nuclear sn-1,2-diacylglycerols are derived from phosphatidylcholine hydrolysis in cultured fibroblasts.
Diglycerides play an important role in a number of agonist-induced signal transduction pathways. We have recently demonstrated that alpha-thrombin induces a rapid increase in the level of diglyceride mass in the nucleus and a selective increase in nuclear PKC-alpha [Leach, K.L., Ruff, V.A., Jarpe, M.B., Fabbro, D., Adams, L.D., & Raben, D.M. (1992) J. Biol. Chem. 267, 21816-21822]. In the present report, we examined the potential source of the induced nuclear diglycerides by examining the molecular species profiles of both the induced diglycerides and nuclear phospholipids by capillary gas chromatography. The molecular species profiles of the nuclear diglycerides generated resemble the species profiles of PC, and not PI species, at all times. In addition, while our previous data indicated that the molecular species of whole-cell phospholipids did not change in response to alpha-thrombin, nuclear PE was altered in a dramatic and selective manner in response to this agonist. These results demonstrate that PC hydrolysis is the predominant, if not exclusive, source of the alpha-thrombin-induced nuclear diglycerides in these fibroblasts.
Cell Fractionation↗
Synthesis of biologically active spin-labelled radioactive cytidine diphosphodiglyceride, a novel probe for biological membranes.
A versatile synthesis of spin-labelled radioactive cytidine diphospho-sn-1,2-diacylglycerol (CDP-diglyceride) has been developed based on the combination of the enzymatic acylation of radioactive sn-glycero-3-phosphate with 12-doxyl stearic acid and the chemical conversion of the thus obtained spin-labelled radioactive phosphatidic acid with cytidine monophosphomorpholi-date into spin-labelled radioactive CDP-diglyceride. The method for the isolation and purification of the latter compound was described. This obtained CDP-[2-3H]diglyceride contained 10% of fatty acids of paramagnetic nature, presumably present as a covalently bound 12-doxyl stearic acid esters. The biological activity was tested by using the synthesized compound as a substrate in the mitochondrial biosynthesis of phosphatidylglycerol. It was found that spin-labelled CDP-[2-3H]diglyceride prepared as described can be converted in the presence of sn-[2-14C]-glycero-3-phosphate into a spin-labelled [2-3H, 2'-14C]phosphatidylglycerol with isolated rat liver mitochondria, establishing therefore that the site of its utilization is identical with the site of phosphatidylglycerol synthesis in isolated mitochondria, i.e. inner mitochondrial membrane. Results described demonstrate that the synthesized spin-labelled CDP-diglyceride can be used as a specific probe for the spin- and radioactive covalent labelling of polyglycerophosphatides of mitochondrial membranes. Some implications and further possibilities in the study of biological membranes using the spin-labelled radioactive CDP-diglyceride are discussed.
Animals↗
Acyl specificity in triglyceride synthesis by lactating rat mammary gland.
We have studied the specificity of the acyl-CoA:diglyceride acyltransferase reaction in lactating rat mammary gland to provide a rational explanation at the enzyme level for the nonrandom distribution of fatty acids in milk fat triglycerides. Acyl-CoA:diglyceride acyltransferase activity was measured using various diglyceride and radioactive acyl-CoA substrates; products were identified as triglycerides by thin-layer and gas-liquid chromatography. Most of the enzymatic activity was located in the microsomal fraction and showed a broad specificity for the acyl donors tested C10, C12, C14, C16, C18, and C18:1 CoA esters). The acyltransferase activity was highly specific for sn-1,2-diglyceride enantiomers; rac-1,3- and sn-2,3-diglycerides were relatively inactive. The acyl-CoA specificity was not affected by the type of 1,2-diglyceride acceptor offered, although dilaurin was the best acceptor and sn-1,2-dilaurin greater than sn-1,2-dimyristin greater than sn-1,2-dipalmitin greater than sn-1,2-distearin. We have previously shown that in the microsomal fraction from lactating rat mammary gland, the acyltransferase activities concerned with the conversion of sn-glycero-3-phosphate to diacylglycerophosphate show a very marked specificity for long chain acyl-CoA's. Therefore, we conclude that the predominant localization of long chain fatty acids in the 1 and 2 positions, and of shorter chain fatty acids in the 3 position of the glycerol backbone, results at least in part from the specificities of the mammary gland acyltransferases.
Acyltransferases↗
On the biological occurrence and regulation of 1-acyl and 1-O-alkyl-diradylglycerols in human neutrophils. Selective destruction of diacyl species using Rhizopus lipase.
The occurrence and regulation of 1-ether-linked diradylglycerol in human neutrophils were investigated using a sensitive and practical analytical mass method which distinguishes 1-O-alkyl- (EAG) versus 1-acyl (DAG) diglycerides. After phosphorylation of diglycerides to the corresponding [32P]phosphatidic acids using [gamma-32P]ATP and diglyceride kinase (Preiss, J., Loomis, C. R., Bishop, W. R., Stein, R., Niedel, J. E., and Bell, R. M. (1986) J. Biol. Chem. 261, 8597-8600), lipase from Rhizopus arrhizus selectively degraded the 1-acyl-containing species (DAG), but the ether lipid (EAG) was resistant and was identified and quantified after thin layer chromatography separation. By using this method, unstimulated neutrophils were demonstrated to contain both DAG and EAG (100-180 and 40-95 pmol/10(7) cells, respectively). The chemoattractant formyl-methionyl-leucyl-phenylalanine (fMLP) caused a rapid (30 s) and transient increase (1.6-fold) in DAG, but no increase in EAG. Opsonized zymosan produced a 6-8-fold sustained increase in DAG peaking at 2 to 3 min, but only a small (1.7-fold) increase in EAG which was not seen until later times (10 min). Thus, under these stimulation conditions, the major diglyceride was DAG. However, in neutrophils "primed" with cytochalasin B or phorbol ester, formyl-methionyl-leucyl-phenylalanine caused a significant increase in EAG. Neutrophils pretreated with cytochalasin B and then stimulated by fMLP showed a rapid (15-60 s) increase (more than 3-fold) in total diglycerides which was sustained beyond 5 min. At the earliest time points (15-30 s), the increase was due almost entirely to DAG (3-fold), but at 1 min and beyond, EAG comprised as much as 40% of the total (up to a 5-fold increase in EAG). Neutrophils pretreated with phorbol ester prior to fMLP stimulation showed a rapid (around 30 s) more than 2-fold increase in both DAG and EAG. Thus, priming conditions (in particular cytochalasin B) may alter either the access of phospholipase(s) C and/or D to membrane phospholipids or may affect their activities, allowing hydrolysis of 1-O-alkyl-containing lipids to generate 1-O-alkyl-containing diglycerides.
Cytochalasin B↗
Phospholipase C and diacylglycerol lipase in human gallbladder and hepatic bile.
A phospholipase C in bile, free of bacterial infection, has recently been identified from cholesterol gallstone patients. Because of the importance of phosphatidylcholine in solubilizing cholesterol in bile, this study further investigates the metabolism of phosphatidylcholine in delipidated gallbladder and common bile duct biles. Phospholipase C activity, as measured by the release of phosphoryl[3H]choline from the substrate 1,2-dipalmitoyl-sn-glycero-3-phospho [N-methyl-3H]choline, was identified in both hepatic and gallbladder biles. Similar levels of activity (nmol.h-1.mg-1 of delipidated protein) were found in common bile duct (11.25 +/- 14.23) and gallbladder bile (19.07 +/- 22.24), although per milliliter of bile, the mean gallbaldder levels were 6.4 times greater than those found in common duct bile. With the tow substrates, 1-palmitoyl-2[9,10-3H] palmitoyl-sn-glycero-3-phosphocholine and 1,2(1-14C) dipalmitoyl-sn-glycero-3-phosphocholine, the majority of organically extracted label, after thin-layer chromatography, was recovered as radiolabeled diglyceride, confirming the presence of phospholipase C. Diglyceride levels were found to be closely correlated with [3H]choline (slope, 0.9820; r = 0.9844). In addition to diglyceride, both radiolabeled free fatty acid and monoglyceride were identified in common bile duct and gallbladder biles, although their levels were an order of magnitude less than measurable phospholipase C activity. To determine whether the free fatty acid release was due to either a diacylglycerol-lipase or a phospholipase A2, the effect of adding unlabeled diglyceride on free fatty acid formation from the substrate [14C]DPPC was examined. As the concentration of unlabeled diglyceride was increased, the amount of free fatty acid and monoglyceride released were both reduced in parallel. Direct measurement of diacylglycerol-lipase activity by incubating the diglyceride, sn-2[3H]dipalmitoyl, resulted in release of both products in a ratio similar to that found with sn-2[3H]DPPC. Finally, no radiolabeled lysolecithin was identified with [3H]choline-DPPC or [14C]DPPC as substrate indicating the free fatty acid was the product of a diacylglycerol-lipase rather than a phospholipase A2. Phospholipase C and diacyl-glycerol-lipase activities were significantly correlated (P less than 0.01).(ABSTRACT TRUNCATED AT 400 WORDS)
Adult↗
Classification of edible oils by employing 31P and 1H NMR spectroscopy in combination with multivariate statistical analysis. A proposal for the detection of seed oil adulteration in virgin olive oils.
A combination of (1)H NMR and (31)P NMR spectroscopy and multivariate statistical analysis was used to classify 192 samples from 13 types of vegetable oils, namely, hazelnut, sunflower, corn, soybean, sesame, walnut, rapeseed, almond, palm, groundnut, safflower, coconut, and virgin olive oils from various regions of Greece. 1,2-Diglycerides, 1,3-diglycerides, the ratio of 1,2-diglycerides to total diglycerides, acidity, iodine value, and fatty acid composition determined upon analysis of the respective (1)H NMR and (31)P NMR spectra were selected as variables to establish a classification/prediction model by employing discriminant analysis. This model, obtained from the training set of 128 samples, resulted in a significant discrimination among the different classes of oils, whereas 100% of correct validated assignments for 64 samples were obtained. Different artificial mixtures of olive-hazelnut, olive-corn, olive-sunflower, and olive-soybean oils were prepared and analyzed by (1)H NMR and (31)P NMR spectroscopy. Subsequent discriminant analysis of the data allowed detection of adulteration as low as 5% w/w, provided that fresh virgin olive oil samples were used, as reflected by their high 1,2-diglycerides to total diglycerides ratio (D > or = 0.90).
Analysis of Variance↗