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PubMed1991

The effect of pancreatic procolipase and colipase on pancreatic lipase activation.

Intestinal fat digestion is carried out by the concerted action of pancreatic lipase and its protein cofactor colipase. Colipase is secreted from pancreas as a procolipase and is transformed into colipase by the trypsin cleavage of the Arg5-Gly6 bond during liberation of an N-terminal pentapeptide. The kinetic parameters for the lipase-colipase system compared to the lipase-procolipase system has been compared using trioctanoin and Intralipid as substrates. It was found that at pH 7.0 the Kmapp using Intralipid as substrate was the same for procolipase and colipase, 0.06 mM and 0.05 mM, respectively. At pH 8.0, however, the Kmapp were different-0.23 mM for procolipase and 0.08 mM for colipase. In a similar way the binding between colipase and lipase had a dissociation constant of 2.4 x 10(-6) M at pH 7.0, while for procolipase--lipase binding the dissociation constant was 4.1 x 10(-6) M with no significant difference. At pH 8.0 the binding between colipase and lipase was stronger, Kd being 2.0 x 10(-7) M, while weaker for procolipase and lipase, Kd being 1.0 x 10(-5) M. It is concluded that at the physiological pH value as is found in the intestine, the activation of procolipase to colipase has no influence on the hydrolysis of trioctanoin or Intralipid in the presence of bile salt.

Animals↗
PubMed1995

Macrocyclic lactone synthesis by lipases in water-in-oil microemulsions.

Five microbial lipases from Chromobacterium viscosum, Candida cylindracea, Pseudomonas (source Fluka), Pseudomonas (source Genzyme) and lipoprotein lipase ex Microbial (Genzyme) have been screened for lactonisation activity towards 16-hydroxyhexadecanoic acid (HHA) in a variety of different w/o microemulsion systems. With the exception of Candida cylindracea (CC), all the lipases exhibited lactonisation activity although they were inherently more active in microemulsion systems based on the anionic surfactant sodium bis(2-ethylhexyl)sulphosuccinate (AOT) than in those based on the cationic surfactant cetyltrimethylammonium bromide (CTAB). Lactone yields are typically 50-60% and are markedly better than those reported previously using microemulsions in combination with chemical catalysts. Lipase stability is superior in the CTAB microemulsion systems, while lipase stability in the low water content AOT microemulsion systems was still good with the exception of CC lipase, which is rapidly inactivated. Buffering the water pools of AOT microemulsions using diglycine buffer at pH 8.0 improved biocatalyst stability. The lactonisation activity of lipases in CTAB w/o microemulsion systems compares favourably with that obtained using the same preparations as a solid suspension in the corresponding water-saturated organic solvent. In addition, the unusual solubility properties of microemulsions allowed the use of considerably higher concentrations of substrate in the microemulsion systems as compared to water-saturated organic solvents such as n-heptane. Lactone yields obtained at equivalent concentrations in the corresponding organic solvents containing conventional condensation catalysts were consistently measured at approx. 10%.

4-Aminopyridine↗
PubMed1996

Effect of lipid transfer proteins on lipoprotein lipase induced transformation of VLDL and HDL.

Lipoprotein lipase-induced lipolysis of human plasma VLDL usually does not yield a complete conversion of VLDL to LDL due to insufficient loss of surface and core lipids and apolipoprotein E. In order to assess the role of lipid transfer proteins in this process human VLDL and apo E free HDL, in approximately physiologic proportions, and with sufficient albumin to bind all released fatty acids, were subjected to 90% lipolysis of triglycerides in 2 h by lipoprotein lipase in the presence or absence of partially purified human cholesteryl ester and phospholipid transfer proteins. Lipoprotein lipase caused a partial transfer of VLDL unesterified cholesterol (16%) and phospholipid (11%), apo E (19%) and almost complete transfer of apo CII and CIII to HDL. VLDL remnants possessed excess apo E and surface and core lipids when compared to plasma LDL, and densities ranging from that of VLDL/IDL to LDL. With addition of the lipid transfer proteins to the lipolysis incubation there was an increased transfer of phospholipid and unesterified cholesterol (2-fold) and apo E (1.6-fold) to HDL over that for lipoprotein lipase incubations. The source of transferred material was primarily from remnants which isolated in the LDL density range in lipoprotein lipase incubations. This transfer resulted in LDL-like particles which had a smaller particle size but lighter density compared to those in lipoprotein lipase incubation. Transfer of cholesteryl esters to VLDL from HDL in exchange for triglyceride was absent or substantially reduced in incubations containing lipoprotein lipase and lipid transfer proteins compared to incubations with only lipid transfer proteins. It is concluded that during rapid lipolysis lipid transfer proteins promote the loss of phospholipid, unesterified cholesterol and apo E from VLDL remnants but do not promote the transfer of cholesteryl ester from HDL to VLDL.

Apolipoprotein C-II↗
PubMed1983

The interaction between pancreatic lipase and colipase: a protein-protein interaction regulated by a lipid.

Pancreatic lipase readily adsorbs to a triglyceride droplet. In the intestine the triglyceride droplets are covered with bile salt and phospholipids which will prevent the adsorption of lipase. In this situation the activity of lipase is restored by colipase, another pancreatic protein. Lipase and colipase in solution form a 1:1 molar complex. I emphasize the fact that the binding and conformation of the two proteins in the complex is dependent on the type of lipids present and suggest that this lipid-determined structure of the complex is responsible for the actual function of lipase/colipase. It determines whether colipase assists lipase in binding to the bile salt-covered triglyceride droplet as is the case with tributyrin as substrate, and whether colipase in addition activates lipase as is the case with a mixed trioctanoin/lecithin monolayer substrate. In other words, lipase activity is regulated by the combined action of colipase and the lipid substrate.

Colipases↗
PubMed1990

Gastric lipase in alcoholic pancreatitis. Comparison of secretive profiles following pentagastrin stimulation in normal adults and patients with pancreatic insufficiency.

The aims of this study were to evaluate the amount of gastric lipase secreted by the stomach in normal adults and to elucidate a possible adaptative secretion of this enzyme in response to pancreatic insufficiency secondary to alcoholic chronic pancreatitis. Forty-one subjects underwent a gastric intubation. Pentagastrin (6 micrograms.kg-1.h-1 IV) significantly increased gastric lipase concentration and output. Stimulated gastric lipase output in seven normal subjects was 12,598 +/- 2036 U/h (by using tributyrin as substrate). Outputs where higher (P less than 0.02) in 17 patients with pancreatic insufficiency who were not drinking alcohol, but were not significantly different in nine patients who continued to drink (20,413 +/- 1778 U/h and 21,953 +/- 4973 U/h, respectively). On the other hand, high gastric lipase outputs were found in eight patients with duodenal ulcers and no evidence of pancreatic dysfunction (23,180 +/- 262 U/h). The time required to reach maximal lipase output (peak output) following pentagastrin stimulation was the same in all groups (approximately 38 minutes) except for the group of patients with pancreatic insufficiency who did not drink alcohol, in whom it was significantly reduced (approximately 26.5 minutes). Secretory patterns of gastric lipase and pepsin were closely comparable. Gastric lipase secretion could be increased in several clinical conditions and particularly in patients with pancreatic insufficiency caused by alcoholic chronic pancreatitis who have been abstinent for a long time.

Adult↗
PubMed1991

Gastric lipase: evidence of an adaptive response to dietary fat in the rabbit.

In the rabbit, the stomach is the only source of preduodenal lipase, and in humans, it is quantitatively the most important. Thus, the adaptive response of gastric and pancreatic lipases to dietary fat was studied in the adult rabbit. Effect of duration was studied by feeding rabbits 12% dietary fat for 1, 2, or 4 weeks or 2.7% for 2 weeks (control). To study the effects of the amount of fat, rabbits were fed the control diet (2.7% fat) or 6% and 12% dietary fat for 2 weeks. The influence of sunflower oil and butter was compared by feeding rabbits 12% dietary fat for 2 weeks. Approximately doubling (6% vs. 2.7%) the usual amount of dietary fat was sufficient to induce a maximum increase in gastric lipase activity in the fundus [+ 66.3% (units per gram tissue) or + 85.2% (units per milligram protein)] and the total stomach mucosa [+ 84.5% (units per mucosa)], whereas pancreatic lipase activity only significantly increased when rabbits were fed 12% dietary fat. A full adaptive response was observed for both gastric and pancreatic lipases after 2 weeks of diet. Triglyceride composition did not noticeably change the adaptive response of both lipolytic enzymes. The present results agree closely with those concerning lingual lipase in the rat and evidence that gastric lipase shows an adaptive response to moderate fat intake. The implications of these findings concerning humans are discussed.

Adaptation, Physiological↗
PubMed1995

Ontogeny of human gastric lipase and pepsin activities.

BACKGROUND/AIMS: The developmental profile of human gastric lipase activity as well as the secretory capacity of the immature gastric mucosa are still unknown. The aims of this study were to establish tissue activity levels for lipase and pepsin in the various anatomical regions of the developing stomach and to assess whether lipase is secreted by the fetal gastric mucosa. METHODS: Lipase and pepsin activities were assayed in 49 specimens of different gestational ages. Gastric explants were cultured in chemically defined medium for up to 5 days, and enzymic activities were measured in tissues and in the culture media. RESULTS: Lipolytic activity was present in gastric tissues at 10-13 weeks and steadily increased for up to 20 weeks, whereas pepsin activity did not vary significantly over the periods of study. There was a clear decreasing gradient of lipase activity; the highest activity was in the fundic area, and the lowest activity was in the antrum. Quantitative pepsin activity did not vary over the gastric regions. During culture, total lipolytic and pepsin activity increased 3.8-fold, and both enzymes were secreted into the culture medium. CONCLUSIONS: Gastric lipase appears as early as 10-13 weeks. Adult distribution of the enzyme became established by 16 weeks' gestation. The secretion of lipase into the organ culture suggests that the gastric mucosa is the main source of lipolytic activity in gastric aspirates of premature infants.

Female↗
PubMed1990

Acid triacyglycerol lipase inhibitor in chicken plasma: purification and properties.

1. Acid triacylglycerol lipase inhibitor was highly purified from chicken plasma by ammonium sulfate fractionation (0.6-1 saturation) followed by successive chromatographies on Hydroxyapatite, Blue-Cellulofine, Phenyl-Sepharose and Cellulofine GCL-2000 columns, and isoelectric focusing. 2. The lipase inhibitor showed its inhibitory action on triacylglycerol lipases in chicken erythrocytes ghosts and in chicken liver lysosome, but did not on pancreatic lipase, Rhizopus arrhizus lipase, or wheat germ lipase. 3. The inhibitor showed its molecular weight of 32,000 by Cellulofine GCL-2000 gel filtration. The inhibitor showed some heterogeneity on isoelectric focusing, and the main band had a pI of 5.10. 4. The lipase inhibitor did not show any inhibitory action on trypsin or chymotrypsin.

Ammonium Sulfate↗
PubMed1977

Heparin-induced release of lipase activity in the human forearm: an immunological study.

Low doses of heparin were injected into the brachial artery of three volunteers. The lipase activities in the deep vein of the same forearm, draining mainly muscle tissue, and in the artery were monitored over a 10-min period. Lipase activity, rapidly released by heparin in the deep vein, was immunologically similar to lipoprotein lipase (E.C. 3.1.1.3), i.e. (1) it did not react with antiserum against human post-heparin plasma hepatic lipase and (2) it was inhibited by an antiserum against bovine milk lipoprotein lipase, which cross reacts with human post-heparin plasma lipoprotein lipase. The evidence that human muscle contains lipoprotein lipase is discussed.

Adult↗
PubMed1988

Studies on the function of hepatic lipase in the cat after immunological blockade of the enzyme in vivo.

In order to investigate the in vivo function of hepatic lipase, cats were injected with anti-cat hepatic lipase antibodies which produced a complete and specific inhibition of heparin-releasable hepatic lipase. The cat was chosen as an animal model because it displays, like man, a relative deficiency of lipoprotein lipase compared to hepatic lipase and because the possession of two subfractions of high density lipoproteins, HDL2 and HDL3. In fasted cats no changes were observed in plasma triglycerides or phospholipids. In fed animals triglycerides increased considerably, indicating that hepatic lipase may have a function in the postprandial phase. In fat-loaded cats (6 g of fat/kg) triglycerides in the d less than 1.019 g/ml fraction increased from 4 h after the blockade due to accumulation of lipoproteins with pre-beta-mobility containing the apoproteins, apo B-100, apo E and apo A-I. Apo B-48 did not accumulate consistently. Phospholipids in the HDL2-fraction and those in the HDL3-fraction of the fat-loaded cats tended to increase and decrease from 6 and 9 h after the blockade, respectively. The absolute change in HDL2 phospholipids approximated that of HDL3-phospholipids. Overall, the density of HDL particles decreased, apparently secondary to the accumulation of apo A-I in the d less than 1.019 g/ml fraction. Our findings suggest that hepatic lipase is involved in the hydrolysis of a special class of apo A-I containing triglyceride-rich lipoproteins synthesised in the postprandial phase.

Animals↗
PubMed2004

Inhibitory effect of lysophosphatidylcholine on pancreatic lipase-mediated hydrolysis in lipid emulsion.

In the lipid metabolism pathway, dietary lipid emulsified with bile salts and phospholipids is mainly digested by pancreatic lipase into free fatty acids and monoacylglycerols. In order to study substrate recognition mechanism of a pancreatic lipase, we investigated its catalytic property toward the lipid emulsion prepared with long- or intermediate-chain acylglycerols and several physiological surfactants. When lysophosphatidylcholine (LysoPC), rather than bile salts or phospholipid, was incorporated into the lipid emulsion, it caused an increase in the Km(app) and a decrease in the Vmax(app) values in the interactions between the lipase and triacylglycerol (triolein or tricaprin). This indicated that LysoPC inhibited hydrolysis by decreasing both the substrate affinities and the catalytic activity of this lipase. Interestingly, further addition of taurodeoxycholic acid sodium salts or phospholipid completely restored the inhibitory effect of LysoPC on hydrolysis by lipase. On the other hand, the change in these kinetic values between the lipase and two 1-monoacylglycerols (1-monocaprin and 1-monoolein) were not particularly large when LysoPC was added. Particle size analysis of the lipid emulsion composed of LysoPC and triacylglycerols showed that most of the particles were less than 200 nm in size, which was smaller than the particle size in the triacylglycerol emulsions containing bile salts or phospholipid. The composition of the emulsion would affect its surface characteristics and thus contribute to changing lipase activity.

Animals↗
PubMed2006

Purification, cloning and regulation of a novel acid-lipase-like protein of hamster expressed in lacrimal glands and tears during lactation.

We report a novel 48-kDa tear acid-lipase-like protein (TALLP), which is markedly induced in lacrimal glands (LG) and secreted in tears of hamster dams during lactation. TALLP is undetectable in LG and tears of normal hamsters, but is also induced after gonadectomy in both sexes and this is prevented by androgen, estrogen or thyroid hormone treatment. These observations and the obliteration of TALLP upon cessation of lactation suggest that endogenous estrogens (in females) and androgens (in males) completely repress TALLP expression. Purified TALLP is monomeric, contains approximately 18% N-glycosylation and several pI isoforms. TALLP expression was tissue-specific and immunolocalized in LG acinar cells. The cDNA deduced amino-acid sequence of TALLP precursor (398 residue, containing a 19 residues signal-peptide) showed only 43-48% identity with all known mammalian acid-lipases, including even those of other rodents, suggesting that TALLP is a prototype of a new category, within the acid-lipase family. Surprisingly, although the catalytic triad residues and other sequence features important for lipolytic activity are conserved in TALLP, it has no detectable lipase activity. However, TALLP binds the polarity sensitive hydrophobic probe, 1-aminoanthracene (K(d)=12 microM). TALLP might have a unique substrate-specificity or a lipid-binding/carrier function in tears of hamster dams. This is the first report of an acid-lipase-like protein secreted in tears of any species. Since TALLP lacks the usual lipase activity, it can be an excellent model to understand better what other structural features in acid-lipases influence their catalytic activity.

Amino Acid Sequence↗
PubMed2005

Chitosan-tethered poly(acrylonitrile-co-maleic acid) hollow fiber membrane for lipase immobilization.

A protocol was used to prepare a dual-layer biomimetic membrane as support for enzyme immobilization by tethering chitosan on the surface of poly(acrylonitrile-co-maleic acid) (PANCMA) ultrafiltration hollow fiber membrane in the presence of 1-ethyl-3-(dimethylaminopropyl) carbodiimide hydrochloride (EDC)/N-hydroxylsuccin-imide (NHS). The chemical change of the chitosan-modified PANCMA membrane surface was confirmed with Fourier transform infrared spectroscopy and X-ray photoelectron spectroscopy. Lipase from Candida rugosa was immobilized on this dual-layer biomimetic membrane using glutaraldehyde (GA), and on the nascent PANCMA membrane using EDC/NHS as coupling agent. The properties of the immobilized enzymes were assayed and compared with those of the free one. It was found that both the activity retention of the immobilized lipase and the amount of bound protein on the dual-layer biomimetic membrane (44.5% and 66.5 mg/m2) were higher than those on the nascent PANCMA membrane (33.9% and 53.7 mg/m2). The kinetic parameters of the free and immobilized lipases, Km and Vmax, were also assayed. The Km values were similar for the immobilized lipases, while the Vmax value of the immobilized lipase on the dual-layer biomimetic membrane was higher than that on the nascent PANCMA membrane. Results indicated that the pH and thermal stabilities of lipase increased upon immobilization. The residual activity of the immobilized lipase after 10 uses was 53% on the dual-layer biomimetic membrane and 62% on the nascent PANCMA membrane.

Acrylic Resins↗
PubMed2004

Lipase-mediated stereoselective hydrolysis of stampidine and other phosphoramidate derivatives of stavudine.

Enzymatic hydrolysis of stampidine and other aryl phosphate derivatives of stavudine were investigated using the Candida Antarctica Type B lipase. Modeling studies and comparison of the hydrolysis rate constants revealed a chiral preference of the lipase active site for the putative S-stereoisomer. The in vitro anti-HIV activity of these compounds correlated with their susceptibility to lipase- (but not esterase-) mediated hydrolysis. We propose that stampidine undergoes rapid enzymatic hydrolysis in the presence of lipase according to the following biochemical pathway: During the first step, hydrolysis of the ester group results in the formation of carboxylic acid. Subsequent step involves an intramolecular cyclization at the phosphorous center with simultaneous elimination of the phenoxy group to form a cyclic intermediate. In the presence of water, this intermediate is converted into the active metabolite Ala-d4T-MP. We postulate that the lipase hydrolyzes the methyl ester group of the l-alanine side chain to form the cyclic intermediate in a stereoselective fashion. This hypothesis was supported by experimental data showing that chloroethyl substituted derivatives of stampidine, which possess a chloroethyl linker unit instead of a methyl ester side chain, were resistant to lipase-mediated hydrolysis, which excludes the possibility of a direct hydrolysis of stampidine at the phosphorous center. Thus, our model implies that the lipase-mediated formation of the cyclic intermediate is a key step in metabolism of stampidine and relies on the initial configuration of the stereoisomers.

Amides↗
PubMed2004

Expression, purification, and aggregation studies of His-tagged thermoalkalophilic lipase from Bacillus thermocatenulatus.

The His-tagged lipase BTL2 from Bacillus thermocatenulatus was expressed in Escherichia coli and purified to homogeneity by a simple, one-step purification protocol using immobilized metal affinity chromatography. The success of protein separation and purification was pH-dependent and increased with decreasing pH. The purified BTL2 lipase showed a strong tendency to aggregate upon concentration, which prevented a reproducible crystallization. Aggregation studies using dynamic light-scattering (DLS) analysis were performed to improve the purification and concentration of BTL2 lipase. Different chemical classes of additives were tested to manipulate the aggregation behaviour of BTL2 lipase with the aim of obtaining a monodisperse sample to use for crystallization. For the process of concentration of BTL2 lipase in monomeric form, the alcohol 2-propanol and the ionic detergent dodecyl dimethylamine-N-oxide (LDAO) were found to be necessary. For the concentrated lipase, the availability of 5% 2-propanol was sufficient to hold the lipase in monomeric form and no additional detergent was needed.

2-Propanol↗
PubMed2005

Overexpression and characterization of a lipase from Bacillus subtilis.

A novel plasmid, pBSR2, was constructed by incorporating a strong lipase promoter and a terminator into the original pBD64. A mature lipase gene from Bacillus subtilis strain IFFI10210, an existing strain for lipase expression, was cloned into the plasmid pBSR2 and transformed into B. subtilis A.S.1.1655. Thus, an overexpression strain, BSL2, was obtained. The yield of lipase is about 8.6 mg protein/g of wet weight of cell mass and 100-fold higher than that in B. subtilis strain IFFI10210. The recombinant lipase was purified in a three-step procedure involving ammonium sulfate fractionation, ion exchange, and gel filtration chromatography. Characterizations of the purified enzyme revealed a molecular mass of 24 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, maximum activity at 43 degrees C and pH 8.5 for hydrolysis of p-nitrophenyl caprylate. The values of Km and Vm were found to be 0.37 mM and 303 micromol mg-1 min-1, respectively. The substrate specificity study showed that p-nitrophenyl caprylate is a preference of the enzyme. The metal ions Ca2+, K+, and Mg2+ can activate the lipase, whereas Fe2+, Cu2+, and Co2+ inhibited it. The activity of the lipase can be increased about 48% by sodium taurocholate at the concentration of 7 mM and inhibited at concentrations over 10 mM.

Bacillus subtilis↗
PubMed2006

Safety evaluation of a lipase enzyme preparation, expressed in Pichia pastoris, intended for use in the degumming of edible vegetable oil.

BD16449 lipase is the product of a phospholipid-specific lipase gene expressed in the yeast Pichia pastoris strain DVSA-PLC-004. This type C phospholipid lipase (EC 3.1.4.3) is intended for use in the degumming of edible vegetable oil. BD16449 lipase was tested as a refined test article preparation (DV16449) for its effects on genotoxicity and in acute, inhalation, and subchronic toxicity studies. Dosages ranged from 5000 microg/plate for in vitro toxicity studies to 2000 mg/kg/day for in vivo toxicity studies. The highest oral dose tested in vivo (NOAEL of 2000 mg/kg/day) resulted in a safety margin of 133,000 based on the conservative estimate of the total human consumption of BD16449 lipase of 0.015 mg/kg/day. When adjusted for total organic solids (TOS), the highest oral dose tested in vivo (NOAEL of 1680 mg TOS/kg/day) resulted in a safety margin of 18,300 based on the conservative estimate of the total human consumption of BD16449 lipase of 0.092 mg TOS/kg/day [corrected] There was no toxicity reported for any of these studies including additional safety studies. A review of the literature indicates that P. pastoris fulfills recognized safety criteria pertinent to microbial production strains used in the manufacture of food enzyme preparations. The results of the toxicity studies presented herein attest to the safety of BD16449 lipase for use in the degumming of edible vegetable oil.

Animals↗
PubMed1999

Molecular dynamics of microbial lipases as determined from their intrinsic tryptophan fluorescence.

We have studied the intrinsic tryptophan fluorescence of the lipases from Chromobacterium viscosum (CVL), Pseudomonas species (PSL), and Rhizopus oryzae (ROL) in aqueous buffer, zwitterionic detergent micelles, and isopropanol-water mixtures. It was the purpose of this study to obtain information about biophysical properties of the respective enzymes under conditions that modulate enzyme activities and stereoselectivities to a significant extent. According to their decay-associated emission spectra, CVL tryptophans are located in the hydrophobic interior of the protein. In contrast, the PSL and ROL tryptophans are probably confined to the core and the surface of the lipase. From the tryptophan lifetime distributions it can be concluded that the conformation of CVL is not much affected by detergent or organic solvent (isopropanol). Accordingly, CVL is enzymatically active in these systems and most active in the presence of isopropanol. In contrast, ROL and PSL show high conformational mobility, depending on the solvent, because their lifetime distributions are very different in the presence and absence of detergent or isopropanol. Time-resolved anisotropy studies provided evidence that the lipases exhibit very high internal molecular flexibility. This peculiar feature of lipases is perhaps the key to the great differences in activity and stereoselectivity observed in different reaction media. Furthermore, information about self-association of the lipases in different solvents could be obtained. PSL, but not CVL and ROL, forms aggregates in water. Lipase aggregation can be reversed by the addition of detergent or isopropanol, which competes for the hydrophobic surface domains of this protein. This dissociation could efficiently contribute to the increase in lipase activity in the presence of a detergent or isopropanol.

2-Propanol↗