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PubMed1996

Specific long-chain fatty acids promote optimal growth of Frankia: accumulation and intracellular distribution of palmitic and propionic acid

Frankia isolates from nodules of the genera Casuarina (BR, S21, Thr), Allocasuarina (Allo2), and Gymnostoma (G80) were found to grow exponentially with high biomass yield and minimal sporangia formation in stirred propionate mineral medium when supplemented either with 2.4 μM palmitic acid (C16:0), pentadecanoic (C15:0), heptadecanoic (C17:0), or linoleic (C18:2, cis 9, 12) fatty acids. Strains also grew with lauric (C12:0) or myristic (C14:0) acids, but gave lower biomass yield. Stearic acid (C18:0) produced a good biomass yield, but cultures slowly accumulated sporangia; oleic acid (C18:1, cis-9) was detrimental to growth. Caprylic (C8:0) or capric (C10:0) acids proved to be prejudicial for long-term storage of Frankia strains. In experiments using labeled 1,2-dipalmitoyl phosphatidylcholine and palmitic acid, radioactivity bound rapidly to the insoluble, but solvent-extractable fraction of Frankia cells. In contrast, label from propionic acid accumulated in the cytosolic fraction. Therefore, the beneficial effect of some specific phospatidylcholines or free fatty acids on Frankia growth appears to result from their utilization as building blocks for the membrane, suggesting that membrane biosynthesis may be the limiting step for Frankia growth in unamended propionate mineral medium.

Journal Article↗
PubMed2004

Hydrolysis of carbaryl by human serum albumin.

Human serum (HS) and human serum albumin (HSA) were able to hydrolyse the carbamate carbaryl. Carbarylase activity found in HSA was slightly activated by 1 mM Zn2+, Mn2+, Cd2+, Ni2+ and Na+ and by 0.01 mM Pb2+. The organophosphorus compounds paraoxon and O-hexyl O-2,5-dichlorophenyl phosphoramidate, caprylic acid, palmitic acid and the carboxyl ester p-nitrophenyl butyrate inhibited the hydrolysis of carbaryl by HSA, being in the last case a competitive inhibition. Using selective amino acid reagents, we concluded that Cys, Trp, Arg and Tyr seem to play important roles in the carbarylase activity of HSA. In addition, Tyr and Arg seem to be located in the active centre of the enzyme since carbaryl protected the activity from the inhibition. It was concluded that HSA hydrolyses carbaryl by a mechanism similar to that described for rabbit serum albumin based in transient carbamylation of a Tyr residue. The extrapolation of the hydrolysis rate to physiological albumin concentrations suggests that albumin might be playing a critical role in the detoxication of carbaryl.

Carbaryl↗
PubMed1999

Independent production of two molecular forms of a recombinant Rhizopus oryzae lipase by KEX2-engineered strains of Saccharomyces cerevisiae.

A mixture of rProROL having the full-length prosequence (97 amino acids) for a recombinant lipase of Rhizopus oryzae (rROL) and r28ROL having 28 amino acids of the same prosequence has been produced as active forms by Saccharomyces cerevisiae [Takahashi et al. (1998) J Ferment Bioeng 86: 164-168]. However, the separation of rProROL and r28ROL has not been successful due to their identical behavior on column chromatographs, presumably because of the similarity of their surface properties. The independent production of two different molecular forms of rROL was carried out using KEX2-engineered strains of S. cerevisiae, since r28ROL was predicted to be a product from rProROL by a Kex2-like protease. rProROL was successfully obtained by expression of the ROL gene in the S. cerevisiae kex2 strain in which the KEX2 gene encoding Kex2p was disrupted, while r28ROL was obtained by co-expression of the gene (KEX2 delta 613) encoding the soluble form of the C-terminal truncated Kex2 protease (sKex2p). The specific lipase activities of rProROL and r28ROL were 92.9 U/mg and 140 U/mg, respectively. rProROL was stable at pH 2.2-8.0, and showed the optimal reaction temperature to be 30-35 degrees C with a T50 of 55 degrees C (T50 is the temperature resulting in 50% loss of activity). The values for r28ROL were pH 3.0-10.0, 25-30 degrees C, and 40 degrees C, respectively. rProROL was an N-linked glycosylated form, but r28ROL was not. The enhanced thermostability of rProROL did not seem to be due to the N-linked glycosylation, as judged by the results of the Endo H treatment. rProROL had the highest esterase activity toward p-nitrophenyl laurate (C12), whereas r28ROL had the highest esterase activity toward p-nitrophenyl caprylate (C8) and stearate (C18). These results suggest that the distinct properties of these two forms of lipase are caused by the different length of the ROL prosequence.

Bacterial Proteins↗
PubMed2006

Purification, characterization, and molecular cloning of organic-solvent-tolerant cholesterol esterase from cyclohexane-tolerant Burkholderia cepacia strain ST-200.

Extracellular cholesterol esterase of Burkholderia cepacia strain ST-200 was purified from the culture supernatant. Its molecular mass was 37 kDa. The enzyme was stable at pH 5.5-12 and active at pH 5.5-6, showing optimal activity at pH 7.0 at 45 degrees C. Relative to the commercially available cholesterol esterases, the purified enzyme was highly stable in the presence of various water-miscible organic solvents. The enzyme preferentially hydrolyzed long-chain fatty acid esters of cholesterol, except for that of cholesteryl palmitate. The enzyme exhibited lipolytic activity toward various p-nitrophenyl esters. The hydrolysis rate of p-nitrophenyl caprylate was enhanced 3.5- to 7.2-fold in the presence of 5-20% (vol/vol) water-miscible organic solvents relative to that in the absence of organic solvents. The structural gene encoding the cholesterol esterase was cloned and sequenced. The primary translation product was predicted to be 365 amino acid residues. The mature product is composed of 325 amino acid residues. The amino acid sequence of the product showed the highest similarity to the lipase LipA (87%) from B. cepacia DSM3959.

Amino Acid Sequence↗
PubMed2004

Oral absorption enhancement of cromolyn sodium through noncovalent complexation.

PURPOSE: To determine the effect of Sodium N-[8-(2-hydroxybenzoyl)amino]caprylate (SNAC) on the permeation of cromolyn across Caco-2 cell monolayers and explore the molecular basis for the enhanced absorption. METHODS: Transport studies of cromolyn across Caco-2 cell monolayers were conducted in the presence of various SNAC concentrations. Permeation of cellular transport markers and lactate dehydrogenase (LDH) release were measured to evaluate cell integrity. Molecular interactions betweent the two compounds were investigated using isothermal titration calorimetry (ITC), nuclear magnetic resonance (NMR), and Fourier-transfrom infrared (FTIR) spectroscopies and molecular dynamics simulations. RESULTS: The absorption of cromolyn across Caco-2 monolayers was enhanced markedly by SNAC. SNAC did not cause significant LDH leakage and changes in the permeation of transport markers. ITC, spectroscopies, and molecular dynamic simulations indicated the existence of intermolecular interactions between cromolyn and SNAC that involve the 2-hydroxybenzamide moiety on SNAC and weaken the hydrogen bonding between cromolyn and surrounding water molecules. CONCLUSIONS: SNAC increases the permeability of Caco-2 monolayers to cromolyn without measurable cell damage. SNAC interacts with cromolyn mainly via ring stacking. One major mode of interaction appears to involve the insertion of the aromatic ring of SNAC between cromolyn's rings. Such interaction appears to reduce the hydration of cromolyn and thus optimize its hydrophobicity for oral absorption.

Absorption↗
PubMed2003

Recoveries of rat lymph FA after administration of specific structured 13C-TAG.

The potential of the specific structured TAG MLM [where M = caprylic acid (8:0) and L = linoleic acid (18:2n-6)] is the simultaneous delivery of energy and EFA. Compared with long-chain TAG (LLL), they may be more rapidly hydrolyzed and absorbed. This study examined the lymphatic recoveries of intragastrically administered L*L*L*, M*M*M*, ML*M, and ML*L* (where * = 13C-labeled FA) in rats. Lymph lipids were separated into lipid classes and analyzed by GC combustion isotope ratio MS. The recoveries of lymph TAG 18:2n-6 8 h after administration of L*L*L*, ML*M, and ML*L* were 38.6, 48.4, and 49.1%, respectively, whereas after 24 h the recoveries were approximately 50% in all experimental groups. The exogenous contribution to lymph TAG 18:2n-6 was approximately 80 and 60% at maximum absorption of the specific structured TAG and L*L*L*, respectively, 3-6 h after administration. The tendency toward more rapid recovery of exogenous long-chain FA following administration of specific structured TAG compared with long-chain TAG was probably due to fast hydrolysis. The lymphatic recovery of 8:0 was 2.2% 24 h after administration of M*M*M*. This minor lymphatic recovery of exogenous 8:0 was probably due to low stimulation of chylomicron formation. These results demonstrate tendencies toward faster lymphatic recovery of long-chain FA after administration of specific structured TAG compared with long-chain TAG.

Animals↗
PubMed2006

Lymphatic recovery of exogenous oleic acid in rats on long chain or specific structured triacylglycerol diets.

Specific structured triacylglycerols, MLM (M = medium-chain fatty acid, L = long-chain fatty acid), rapidly deliver energy and long-chain fatty acids to the body and are used for longer periods in human enteral feeding. In the present study rats were fed diets of 10 wt% MLM or LLL (L = oleic acid [18:1 n-9], M = caprylic acid [8:01) for 2 wk. Then lymph was collected 24 h following administration of a single bolus of 13C-labeled MLM or LLL. The total lymphatic recovery of exogenous 18:1 n-9 24 h after administration of a single bolus of MLM or LLL was similar in rats on the LLL diet (43% and 45%, respectively). However, the recovery of exogenous 18:1 n-9 was higher after a single bolus of MLM compared with a bolus of LLL in rats on the MLM diet (40% and 24%, respectively, P = 0.009). The recovery of lymphatic 18:1 n-9 of the LLL bolus tended to depend on the diet triacylglycerol structure and composition (P= 0.07). This study demonstrated that with a diet containing specific structured triacylglycerol, the lymphatic recovery of 18:1 n-9 after a single bolus of fat was dependent on the triacylglycerol structure of the bolus. This indicates that the lymphatic recovery of long-chain fatty acids from a single meal depends on the overall long-chain fatty acid composition of the habitual diet. This could have implications for enteral feeding for longer periods.

Administration, Oral↗
PubMed1983

Fluorimetric assay of hydrolases at longwave excitation and emission wavelengths with new substrates possessing unique water solubility.

A direct and continuous kinetic method for the fluorimetric assay of various hydrolases by using new, highly water-soluble substrates is described. The latter consist of esters of strongly fluorescent 1-hydroxypyren-3,6,8-trisulfonic acid trisodium salt with acetic, butyric, caprylic, and oleic acid. Km and vmax values are given for the hydrolytic activity of porcine liver carboxylic ester hydrolase, wheat germ lipase, candida cylindracea lipase, hog kidney acylase I, and bovine pancreas alpha-chymotrypsin, while others (acetylesterase, trypsin, and cholinesterase) were studied qualitatively. By proper choice of the substrate, a fair selectivity may be achieved. Detection limits as low as 1 microgram enzyme/ml are found in some cases. Advantages of these new substrates over existing ones are briefly discussed.

Animals↗
PubMed1988

Isolation and characterization of a fatty acyl esterase from rat lung.

In an effort to facilitate studies of the reaction involved in the removal of fatty acids from acyl proteins, we have synthesized an octanoic acid ester of doubly blocked serine, specifically octanoyl N-carbobenzoxy-L-serine-benzyl ester (octanoyl boc-serine), and used it as a substrate to guide the purification of an esterase from rat lung. The esterase was purified 228-fold by column chromatography on DE-52 cellulose, hydroxylapatite, octyl-Sepharose, and concanavalin A-Sepharose and by HPLC gel filtration. The final enzyme preparation ran as a single 77,000-Da band when subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and exhibited a single symmetrical peak (sedimentation coefficient, 4.5 S) when centrifuged through a sucrose density gradient (empirical Mr, 63,000). The esterase is an acidic protein, pI 4.1, and is very active against p-nitrophenyl esters comprised of C4-C14 fatty acids; the highest specific activity (26.5 mumol/min/mg) was obtained using p-nitrophenyl caprylate as substrate. The pH optimum of the lung esterase is near 8.0 and the activity on octanoyl boc-serine is maximum when 0.3% (w/v) Myrj-52 is included in the assay medium. The activity of the esterase is not dependent on calcium ions. The enzyme does not remove acyl groups from the G-protein of vesicular stomatitis virus or the proteolipid of bovine brain. The possible role of the esterase in the metabolism of acylated proteins is considered.

Animals↗
PubMed1989

Capsaicin and its analogs inhibit the activity of NADH-coenzyme Q oxidoreductase of the mitochondrial respiratory chain.

Capsaicin and its analogs with different acyl moieties were found to inhibit the electron-transfer activity of NADH-coenzyme Q oxidoreductase isolated from beef heart mitochondria. The inhibitory potency of capsaicin was lower than those of dihydrocapsaicin and analogs with heptanoyl, capryl, undecanoyl, and lauroyl moieties, but was higher than those of analogs with palmitoyl and stearoyl moieties. The analog with the lauroyl moiety showed the strongest inhibition. These results suggest that hydrophobicity and the appropriate carbon chain length of the acyl moiety are important for the binding of compounds to the enzyme. On the other hand, capsaicin and its analogs did not interrupt rotenone-insensitive electron transfer from NADH to menadione. Furthermore, these compounds had almost no effect on the spectral properties and EPR signals arising from iron-sulfur clusters of the NADH-treated enzyme. Kinetic analyses with double-reciprocal plots showed that these compounds were competitive inhibitors with respect to coenzyme Q1, an electron acceptor. These results strongly suggest that capsaicin and its analogs bind to the coenzyme Q1 binding site of the enzyme.

Animals↗
PubMed1986

Effects of exogenous fatty acids on calcium uptake by brush-border membrane vesicles from rabbit small intestine.

The uptake of a variety of fatty acids by isolated brush-border membranes from rabbit small intestine was studied. This uptake increased with acyl chain-length and was not diminished by washing of the lipid-treated membranes with 0.25 M CsBr. The binding of fatty acid was not accompanied by a decrease in endogenous acyl groups or of cholesterol and therefore corresponded to a net uptake accountable qualitatively and quantitatively by the fatty acid added to the membranes. The uptake of Ca2+ was stimulated by treatment of the membranes with low concentrations of unsaturated fatty acids (0.05 mM) as well as with various concentrations of caprylic acid (0.10-3.00 mM) and inhibited by treatment with higher concentrations of unsaturated fatty acids (0.20-0.60 mM). Saturated fatty acids had no marked effects on Ca2+ uptake. The stimulatory concentrations of unsaturated fatty acids did not change the Ca2+-binding characteristics of the membranes, whereas the higher concentrations decreased equilibrium binding of Ca2+ and very probably the number of high-affinity binding sites. The results of this study are assessed in terms of the effects of normal fatty acids found in the diet on the absorptive properties of the brush-border membranes.

Animals↗
PubMed1991

EPR studies on the influence of chain length on the segmental motion of spin-labelled fatty acids in dimyristoylphosphatidylcholine bilayers.

The rotational dynamics of spin-labelled fatty acids of different chainlengths (9, 10, 12, 14, 16 and 18 C-atoms) and different positions of labelling (5-C, 6-C and 7-C) have been studied in dimyristoylphosphatidylcholine bilayers using EPR spectroscopy. The segmental flexibility at a given label position is found to vary considerably with the length of the lipid chain, when this is less than that of the dimyristoylphosphatidylcholine host lipid. For both the charged and protonated forms of labelled fatty acids with chainlengths of 9, 10, and 12 C-atoms, the spectral anisotropy decreases steadily with decreasing chainlength in fluid phase bilayers. The differences become especially pronounced at the 7-C position of caprylic acid and the 6-C position of nonanoic acid, where the label is located close to the terminal methyl end of the chain. An unusually high degree of motional freedom is found for both these spin-labels, even in gel phase bilayers. There is relatively little effect of chainlength of the labelled fatty acid when this is longer or comparable to that of the host lipid (i.e., for fatty acid chainlengths of 18, 16 and 14 C-atoms), except if the label position is close to the terminal methyl end of the chain. The implications for the heterogeneous lipid chain composition in biological membranes are discussed.

Dimyristoylphosphatidylcholine↗
PubMed1988

Utilization of mevalonate by aorta for the synthesis of medium-chain n-fatty acids (C8, C10) and acylglycerols.

[2-14C]Mevalonate was incorporated into acylglycerols by bovine aorta. The majority of the radioactivity was found in diacylglycerols. Hydrolysis, followed by analysis by thin-layer chromatography, paper chromatography, gas chromatography, and gas chromatography-mass spectrometry showed that the radioactivity was greatest in the medium-chain n-fatty acids, caprylic (C8) and capric (C10) acids. Triacylglycerols and diacylglycerols have important functions in the maintenance of the metabolic integrity of organs and their constituent cells. Therefore, medium-chain fatty acids may play significant roles, such as solubilization and transport of cholesterol and regulation of metabolism, as constituents of diacylglycerols. The results suggest that the trans-methylglutaconate shunt of mevalonate metabolism functions in the aorta.

Animals↗
PubMed1988

Co-solubility of saturated cholesteryl esters: a comparison of calculated and experimental binary phase diagrams.

Based on ideal solution theory, phase diagrams are calculated for binary compositions of cholesteryl esters and compared to experimental data from pairwise combinations in a saturated acyl chain series from caprylate to arachidate, which encompasses three crystal packing motifs in the solid state. Within a crystal structure class, nearly ideal co-solubility is found for binary solids, where the acyl chain lengths of the pure components differ by one methylene group. Beyond this chain length difference, nonideal solutions occur until fractionation occurs at e.g., six methylene unit increments between the components. The observed liquidus lines of the eutectic are near the theoretical curves when the combinations of two compounds packing in the same crystal structure fractionate. Fractionation also is found when liquids composed of two esters which favor different crystal structures are solidified from the melt, no matter what the chain length difference is; the liquidus curves for re-heated solids, however, are not necessarily predicted by the Schröder equation. In general, co-miscibility can be found in mesophases formed from compounds with two different crystal structures.

Algorithms↗
PubMed1989

Nonesterified fatty acids inhibit iron-dependent lipid peroxidation.

The effect of various fatty acids on lipid peroxidation of liver microsomes induced by different methods in vitro was studied using oxygen uptake and malonaldehyde (MDA) production. It was observed that fatty acids with a single double bond are effective inhibitors of peroxidation. Stereo and positional isomers of oleic acid were equally effective as oleic acid. There was an absolute requirement for a free carboxyl group, since methyl esters of fatty acids and long-chain saturated and unsaturated hydrocarbons could not inhibit peroxidation. Saturated fatty acids with a chain length of 12-16 carbon atoms showed inhibition, whereas more than 18 carbon atoms reduced the inhibitory capacity. Fatty acids of lower chain length such as capric and caprylic acids did not show inhibition. Fatty acid inhibition was partially reversed by increasing the concentration of iron in the system. Peroxidation induced by methods which were independent of iron was not inhibited by fatty acids. It was observed that intestinal microsomes which were resistant to peroxidation due to the presence of nonesterified fatty acids in their membrane lipids were able to peroxidise by methods which do not require iron. These results suggest that certain fatty acids inhibit peroxidation by chelating available free iron. In addition, they may also be involved in competing with the esterified fatty acids in the membrane lipids which are the substrates for peroxidation.

Adenosine Diphosphate↗
PubMed1990

Eutectic interactions between saturated and unsaturated chain cholesteryl esters: comparison of calculated and observed phase diagrams.

Binary phase behavior of saturated chain with unsaturated chain cholesteryl esters is evaluated by analysis of the phase diagrams in terms of ideal solution theory. Cholesteryl palmitate, which crystallizes in the bilayer structure, forms a eutectic with either cholesteryl oleate or cholesteryl linoleate and, as indicated by low angle X-ray data, the components are nearly totally fractionated in the solid state. The fit of the two experimental liquidus curves by a calculation of freezing point depression for an ideal solution indicates that the molecular interactions are nonspecific in the binary liquid state. Cholesteryl caprylate and cholesteryl oleate, both of which crystallize as the monolayer II form, also form a eutectic. X-ray data again indicate nearly total fractionation. The liquidus curve is reasonably well matched by calculation of ideal freezing point depression. However, dissimilar molecular volumes can cause the melt-cholesteric transition line to deviate from an ideal concentration dependence. Possible fractionation mechanisms for cholesteryl esters in arterial lesions are thereby indicated. For example, when the molecules have greatly different volumes, clustering can occur in the liquid crystalline state. Even when the molecular volumes are similar, the saturated component can solidify in regions where it is relatively abundant, because of the incompatibility of two crystal structures with greatly different layer structures.

Calorimetry, Differential Scanning↗
PubMed1991

Effects of various non-esterified fatty acids on the transfer of cholesteryl esters from HDL to LDL induced by the cholesteryl ester transfer protein.

The effects of saturated, monounsaturated and polyunsaturated non-esterified fatty acids on the rate of transfer of radiolabeled cholesteryl esters from high density lipoproteins (HDL) to low density lipoproteins (LDL), induced by the cholesteryl ester transfer protein (CETP), have been studied. Human high-density lipoproteins-subfraction 3 (HDL3) containing radiolabeled cholesteryl esters were incubated with LDL at 37 degrees C with or without CETP and in the absence or in the presence of non-esterified fatty acids. Less than 6% of the total radioactivity was recovered in the LDL fraction after incubation of HDL3, and LDL for 3 h at 37 degrees C in the absence of CETP, regardless of whether or not non-esterified fatty acids were added. The addition of CETP to the incubation mixture induced a time-dependent redistribution of radiolabeled cholesteryl esters from HDL3 to LDL. Non-esterified fatty acids were found to alter the rate of transfer of cholesteryl esters induced by CETP. While short chain saturated non-esterified fatty acids (caprylic and capric acids) had no effect on the rate of transfer of cholesteryl esters, the medium and long chain ones (lauric, myristic, palmitic and stearic acids) significantly increased the CETP-mediated transfers from HDL3 to LDL. At low concentrations, unsaturated fatty acids also stimulated the CETP-mediated redistribution of radiolabeled cholesteryl esters from HDL3 to LDL. As the concentration of either oleic, linoleic or arachidonic acids increased to higher levels, a significant proportion of fatty acids remained unassociated with lipoprotein particles. Under these circumstances the transfer process was inhibited. These results show that non-esterified fatty acids can modulate the CETP-mediated transfer of cholesteryl esters from HDL to LDL and that this effect is dependent on both the length and the degree of unsaturation of their monomeric carbon chain.

Carrier Proteins↗
PubMed1995

Purification and characterization of a fatty acyl-ester hydrolase from post-germinated sunflower seeds.

Fatty acyl-ester hydrolase was not detectable in dry sunflower seeds using various p-nitrophenyl-acyl-esters, 1,2-O-didodecyl-rac-glycero-3-glutaric acid-resorufin ester or emulsified sunflower oil as substrate. After inhibition of the seeds, acyl-ester hydrolase activity slowly developed in cotyledon extracts and was maximal after 5 days. No activity was directly measurable on oil bodies. The enzyme was purified 615-fold to apparent homogeneity, as determined by performing SDS-PAGE electrophoresis, and biochemically characterized. With p-nitrophenyl-caprylate the optimum pH was around 8.0. The purification procedure involved an acetone powder from 5-day dark-germinated seedlings, chloroform-butanol extraction and three chromatography steps. We obtained 35 micrograms of pure enzyme from 250 g of fresh cotyledons with an activity yield of around 7%. It should be possible to subsequently improve this low recovery as we gave priority here, in the first instance, to purity at the expense of the yield. The enzyme consisted of one glycosylated polypeptide chain with a molecular mass of approx. 45 kDa and, as far as we could tell, it did not seem to require metal ions to be fully active, as it was not inhibited by EDTA or o-phenanthroline and not activated by various mono or bivalent metal ions. The amino acid composition showed the presence of four cysteine and four tryptophan residues. The enzyme was partially inhibited by dithiothreitol, DTNB and PCMB. The fact that high inhibition was observed in the presence of PMSF indicates that a serine residue may possibly be involved in the catalytic mechanism. The hydrophobicity index was about 53.6% which places this enzyme in the class of the soluble proteins in good agreement with the fact that it was mainly present in the soluble part of the crude extract. Partial characterization of glycan chains, using antiglycan antibodies, showed the presence of complex Asn-linked glycans. The enzyme was active on purified sunflower glycerol derivatives. It was also able to hydrolyze monooleyl and dioleyl glycerols, as well as phosphatidylcholine, but not cholesteryl esters. Using p-nitrophenyl-acyl-esters as substrate, the highest activity was observed with middle-chain derivatives (C6 and C8). Its maximum activity was about 0.015 units mg-1 with sunflower oil. It was not activated by an organic solvent such as isooctane. This enzyme probably is involved in acyl-ester hydrolysis which follows triacylglycerol mobilization by true lipases.

Amino Acids↗