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Showing papers on "Lipase published in 1984"


Journal ArticleDOI
15 Jun 1984-Science
TL;DR: Porcine pancreatic lipase catalyzes the transesterification reaction between tributyrin and various primary and secondary alcohols in a 99 percent organic medium and exhibits a high catalytic activity at that temperature.
Abstract: Porcine pancreatic lipase catalyzes the transesterification reaction between tributyrin and various primary and secondary alcohols in a 99 percent organic medium. Upon further dehydration, the enzyme becomes extremely thermostable. Not only can the dry lipase withstand heating at 100 degrees C for many hours, but it exhibits a high catalytic activity at that temperature. Reduction in water content also alters the substrate specificity of the lipase: in contrast to its wet counterpart, the dry enzyme does not react with bulky tertiary alcohols.

992 citations


Journal ArticleDOI
TL;DR: It is indicated that the magnitude of postprandial lipemia determines the proportion of triglyceride in pp-HDL2, which in turn determines whether or not HDL2 are converted to HDL3 by hepatic lipase action.
Abstract: In this study, we have investigated the effects of alimentary lipemia in 15 normotriglyceridemic individuals on high density lipoproteins2 (HDL2) with respect to structure, composition, and substrate efficacy for hepatic lipase in vitro. In the study subjects, HDL2 levels ranged widely from 4.7 to 151.7 mg/dl plasma. HDL2 were isolated in the postabsorptive (pa) state and in the postprandial (pp) state, i.e., 7 h after ingestion of a standard fatty meal. In going from the pa state to the pp state, HDL2 exhibited higher flotation rates and lower densities due to a decreased proportion of protein (38.7----36.2%) and a higher abundance in phospholipid (32.5----34.9%). There was a variable increase in triglyceride at the expense of cholesteryl esters; this increase was correlated positively with the magnitude of pp lipemia (r = 0.69, P less than 0.01) and inversely with HDL2 levels (r = -0.72, P less than 0.01). Hdl2 fractions were incubated with human hepatic lipase in vitro. Product lipoproteins formed from lipolysis of pa-HDL2 and triglyceride-poorer pp-HDL2 were reduced in phospholipid content (by 25 and 50%, respectively) but remained in the size and density range of native HDL2. By contrast, a major fraction of triglyceride-richer pp-HDL2 was converted to particles with density, size, and apoprotein composition of native HDL3. Changes consistent with these findings in vitro were observed in vivo also, where 15 h postprandially, individuals with high-level lipemia showed a decrease in HDL2 and rise in HDL3, while those with lower-level lipemia did not. This study indicates that the magnitude of postprandial lipemia determines the proportion of triglyceride in pp-HDL2, which in turn determines whether or not HDL2 are converted to HDL3 by hepatic lipase action.

249 citations


Journal ArticleDOI
TL;DR: Control of adipose tissue lipolysis by fast-acting lipolytic hormones and by insulin is exerted through the regulation of the phosphorylation state of a single phosphoserine residue in the hormone-sensitive lipase.
Abstract: In isolated adipocytes, fast-acting lipolytic hormones and insulin have been shown previously to control lipolysis by regulating the activity of hormone-sensitive lipase, the rate-limiting enzyme, through an increase or decrease, respectively, of the extent of phosphorylation of the enzyme. Here, we demonstrate that exposure to lipolytic hormones (corticotropin, noradrenaline) led to phosphorylation at two sites on the Mr 84,000 lipase subunit. One, designated "basal site," was phosphorylated also in the absence of any hormonal stimulation, its phosphorylation apparently not being influenced by hormones. The second, designated "regulatory site," was identical to that phosphorylated by cyclic AMP-dependent protein kinase on the isolated lipase. The regulatory site was not appreciably phosphorylated in the absence of hormones, but exposure of the cells to noradrenaline increased its phosphorylation extent to that of the basal site. Insulin or the beta-adrenergic antagonist propranolol decreased the extent of phosphorylation of the regulatory site to the low level before stimulation, apparently without effect on the basal site. Phosphoserine was the only phosphorylated amino acid residue at both sites. Limited proteolytic digestion indicated that the two sites were separated by less than about 170 amino acid residues. Thus, control of adipose tissue lipolysis by fast-acting lipolytic hormones and by insulin is exerted through the regulation of the phosphorylation state of a single phosphoserine residue in the hormone-sensitive lipase.

221 citations


Journal ArticleDOI
TL;DR: In this paper, a survey of enzymes that hydrolyze glycidol esters indicated that E.C. 3.1.3, Sigma Type II, from porcine pancreas, has the best combination of activi ty, select ivi ty and cost.
Abstract: equation implies absolute stereochemistry only for l) . The structure of R4 is indicated for each compound in Figure L The substi tuents are hydrogens unless indicated otherwise. We are interested in this reaction partly because it offers a practical synthetic route to certain members of a useful class of chiral substances and partly because it provides an opportunity to compare the characteristics of enantioselective biological and abiological synthetic methods. An init ial survey of enzymesT'8 that hydrolyze glycidol esters indicated that l ipase (E.C. 3.1.1.3, Sigma Type II , from porcine pancreas) has the best combination of act ivi ty, select ivi ty, and cost.e Racemic esters of several epoxy alcohols and related substances were subjected to hydrolysis using this l ipase.l0 To faci l i tate comparison, most reactions were carr ied to 607o complet ion (based on the quanti ty of acid released) under the same condit ions (pH 7.8, T = 25 oC). Unhydrolyzed ester was recovered by extraction (recoveries ranged 60-90Vo of the amount estimated to be present based on acid released). Enantiomeric excesses of recovered ester were measured using Eu(hfc)tr (Figure l ) . These data provide the basis for several observations bearing on the utility of this method. Lipase is not deactivated by reaction

202 citations


Journal ArticleDOI
TL;DR: The modified lipase was modified with 2,4-bis(o-methoxy-polyethylene glycol)-6-chloro-s-triazine(activated PEG2) to catalyze ester synthesis reaction in benzene and was soluble in organic solvents such as benzene, toluene, chloroform and dioxane.

173 citations


Journal ArticleDOI
TL;DR: Lipase from Candida cylindracea has been found to be a highly stereospecific catalyst suitable for preparative resolution of racemic acids and alcohols, and lipase‐catalyzed asymmetric transesterification has been judged to be the method of choice for the practical resolution of Racemic alcohols.
Abstract: Lipase from Candida cylindracea has been found to be a highly stereospecific catalyst suitable for preparative resolution of racemic acids and alcohols. Using (R, S)-2-(p-chlorophenoxy) propionic acid (whose R isomer is a herbicide) and (R, S)-sec-butanol (a versatile synthon) as model compounds, three alternative approaches to lipase-catalyzed resolutions-asymmetric hydrolysis, esterification, and transesterification-have been compared. Enzymatic esterification in biphasic systems has been ruled out for preparative resolutions because addition of the acids lowers the pH of the aqueous phase thereby greatly reducing the efficiency of the procedure. Both enzymatic hydrolysis and biphasic transesterification afforded resolution of the racemates on a gram scale. From the standpoint of productivity, ease of product separation, and the amount of steps required, lipasecatalyzed asymmetric hydrolysis has been judged to be superior for the practical resolution of racemic acids, and lipase-catalyzed asymmetric transesterification to be the method of choice for the practical resolution of racemic alcohols.

171 citations


Journal ArticleDOI
TL;DR: The first-order kinetics model for tallow, coconut and olive oil hydrolysis was studied in this article, and the results showed that tallow and coconut can be hydrolyzed within 72 hours.
Abstract: The hydrolysis of tallow, coconut oil and olive oil, by lipase fromCandida rugosa, was studied. The reaction approximates a firstorder kinetics model. Its rate is unaffected by temperature in the range of 26–46 C. Olive oil is more rapidly hydrolyzed compared to tallow and coconut oil. Hydrolysis is adversely affected by hydrocarbon solvents and a nonionic surfactant. Since amounts of fatty acids produced are almost directly proportional to the logarithms of reaction time and enzyme concentration, this relationship provides a simple means of determining these parameters for a desired extent of hydrolysis. All three substrates can be hydrolyzed, almost quantitatively, within 72 hr. Lipase fromAspergillus niger performs similarly. The lipase fromRhizopus arrhizus gives a slow hydrolysis rate because of its specificity for the acyl groups attached to the α-hydroxyl groups of glycerol. Esterification of glycerol with fatty acid was studied with the lipase fromC. rugosa andA. niger. All expected five glycerides are formed at an early stage of the reaction. Removal of water and use of excess fatty acid reverse the reaction towards esterification. However, esterification beyond a 70% triglyceride content is slow.

140 citations


Journal ArticleDOI
TL;DR: In this article, the authors attempted to synthesize carbohydrate esters of fatty acids enzymatically in order to overcome the problems associated with the chemical processes for the synthesis of commercial sucrose esters.
Abstract: The authors attempted to synthesize carbohydrate esters of fatty acids enzymatically in order to overcome the problems associated with the chemical processes for the synthesis of commercial sucrose esters. The enzymes used were lipases from microorganisms belonging toRhyzopus, Enterbacterium, Aspergillus, Pseudomonas, Chromobacterium, Candida, Mucor andPenicillium. Fatty acids (stearic, oleic and linoleic) and carbohydrates (sucrose, glucose, fructose and sorbitol) used for the reaction were obtained from commercial sources. The enzyme reaction was performed by mixing the enzyme and the substrates in the buffer solution and incubating at 40 C; after freeze-drying the mixture, the products were extracted and subjected to thin layer chromatography (TLC) and high performance liquid chromatography (HPLC). It was observed by TLC and HPLC that carbohydrate esters of fatty acid were produced by the enzyme reaction, and their structures were confirmed by infra red (IR) and nuclear magnetic resonance (NMR) spectrometries. The lipase fromCandida cylindracea was the most enzyme active on the synthesis of carbohydrate esters. The optimum conditions for its activity were as follows: molar ratio of carbohydrate to fatty acid: 0.05mol/l : 0.2mol/l; amount of lipase: 4g/l; pH of the reaction mixture: 5.4 in phosphate buffer; reaction period: 72 hr.

132 citations


Journal ArticleDOI
TL;DR: A membrane bioreactor was developed for continuous synthesis of glycerides by lipase to overcome the drawbacks associated with the usual operation in an emulsion system, yielding a conversion above 70% when 1% CaCl2 was added in the glycerol solution.
Abstract: A membrane bioreactor was developed for continuous synthesis of glycerides by lipase to overcome the drawbacks associated with the usual operation in an emulsion system. One unit (total area: 726 cm2) of flat, plate-type dialyzer was used as the membrane bioreactor at 40 C. The glycerol solution, containing bacterial lipase and water, was supplied continuously to 1 side of a sheet of microporous polypropylene membrane (strongly hydrophobic) and the effluent was recycled, while undiluted liquid fatty acid (oleic or linoleic) was fed continuously to the opposite side of the membrane and came in contact with a glycerol-water-lipase solution to cause the reaction. The product, glycerides, was obtained at the outlet, in a pure state, with no other phase. Highest conversion (ca. 90%) was obtained when the water content of the glycerol solution was 3–4%. As the accumulation of water produced by the reaction lowered the conversion, molecular sieves in a column that the glycerol solution passed through were used for optimal water content. The reaction could be continued at least for 1 month, yielding a conversion above 70% when 1% CaCl2 was added in the glycerol solution. The main component of glycerides formed was almost equimolar amounts of mono-and diglycerides.

124 citations


Journal ArticleDOI
TL;DR: Hemodialysis patients with 'low' hepatic lipase activities had a significantly higher prevalence of 'mid-bands' than did those with 'normal' activities, and no evidence was developed to prove that the ' mid-band' lipoproteins were remnant particles.

119 citations


Journal ArticleDOI
TL;DR: Hydrolysis of dietary fat by lingual lipase may not be limited to the stomach but may continue in the upper small intestine, especially during the neonatal period, when the luminal pH is under 6.5.
Abstract: Ten to 30% of dietary fat is hydrolyzed in the stomach by lingual lipase, an enzyme secreted from lingual serous glands. We investigated the substrate specificity of this enzyme as well as the potential of lingual lipase to act in the upper small intestine i.e., in the presence of bile salts and lecithin. The data presented show that partially purified preparations of rat lingual lipase and the lipase in gastric aspirates of newborn infants have identical substrate specificity: medium-chain triglycerides were hydrolyzed at rates 5-8-fold higher than long-chain triglycerides; the rat and human enzymes do not hydrolyze the ester bond of lecithin or cholesteryl-ester. In contrast to pancreatic lipase, the hydrolysis of triglycerides by lingual lipase is not inhibited by lecithin. But, similar to pancreatic lipase the activity of lingual lipase is inhibited by bile salts, the extent of inhibition varying with its nature and concentration. This inactivation is not prevented by colipase but is partially averted by lipids and protein, suggesting that lingual lipase can remain active in the duodenum. The pH optimum of the enzyme (2.2-6.5 in the rat and 3.5-6.0 in human gastric aspirates) is compatible with continued activity in the upper small intestine, especially during the neonatal period, when the luminal pH is under 6.5. The marked variation in lipase activity levels in gastric aspirates of newborn infants is probably due to individual variations in enzyme amounts. The characteristics of the lipase are however identical in infants with low, intermediate or high activity levels.(ABSTRACT TRUNCATED AT 250 WORDS)

Journal ArticleDOI
TL;DR: In this paper, three grades of diatomaceous earth (Celite 560, Filtercel and Hyflo Supercel) and a controlled-pore silica have been examined for their suitability as support materials for lipase (triacyglycerol acylhydrolase, EC 3.1.3).

Journal ArticleDOI
TL;DR: It is concluded that recognition by the extrahepatic receptors depends on the native conformation of the lipase, and internalization-inactivation-degradation occur only slowly in extrahePatic tissues.

Journal ArticleDOI
TL;DR: From the hydrolysis data, an empirical relationship was developed that shows that the percentage of free fatty acid formed is almost a linear function of the logarithm of reaction time and the logarshipm of enzyme concentration.
Abstract: Commercial dry lipase fromCandida rugosa (formerlyC. cylindracea) was used to catalyze hydrolysis of tallow, coconut oil and olive oil at 26–40 C. A methodology was developed to yield results reproducible within ±10% and to achieve essentially complete hydrolysis. From the hydrolysis data, an empirical relationship was developed that shows that the percentage of free fatty acid formed is almost a linear function of the logarithm of reaction time and the logarithm of enzyme concentration. A 95–98% hydrolysis of the 3 substrates was achieved experimentally in 72 hr, requiring 15 units lipase per milliequivalent (U/meq) of coconut oil or tallow and 6 U/meq of olive oil. The kinetics of lipolysis were determined for all 3 substrates and were found to approximate first order. Lipolysis rate was higher for olive oil than for tallow and coconut oil; no significant differences were observed between the latter 2 substrates. No statistically significant change in overall reaction rate was found when the hydrolysis was run at 26 C, 36 C or 46 C. Although the literature cites calcium or sodium ions and albumin as beneficial adjuvants to enzymatic lipolysis, these additives appeared to have no significant beneficial effect on the reaction. On the other hand, hydrocarbon solvents and nonionic surfactants showed an adverse effect.

Journal ArticleDOI
TL;DR: Inhibition of lipase activity by amphiphiles such as proteins or detergents appears to be a general phenomenon not directly related to a decrease in tension at the triacylglycerol-water interface.

Journal ArticleDOI
TL;DR: It has been confirmed that, during intestinal lipolysis of dietary fats, bile salts play an essential role for the activation of the lipase-colipase system in the presence of inhibitory proteins.

Journal ArticleDOI
TL;DR: 1,2-diacylglycerol could be replaced by several kinds of aliphatic alcohols as fatty acid acceptors in the reverse micellar system, and those alcohols with chain length more than 4 carbons were effectively used for ester formation.
Abstract: Triacylglycerols were synthesized from 1,2-diacylglycerol and fatty acids by lipase entrapped in phosphatidylcholine reverse micelles in n-hexane. In the reaction system without reverse micelles, however, 1,2-diacylglycerol was hydrolyzed into 2-monoacylglycerol and fatty acid, and triacylglycerol was not synthesized. The maximum activity of synthetic reaction was obtained at Wo=10 (Wo=mol water/mol surfactant), which was the water content of this reverse micellar system. Though the optimal pH of theR. delemar lipase reaction is about pH 5.6 in a bulk water system, the enzyme was active for triacylglycerol synthesis at pH’s from 5 to 9 in the reverse micellar system. For the synthesis of triacylglycerols, lauric, myristic, palmitic, stearic, oleic and arachidic acids were effectively used as the fatty acid substrate. 2-Monoacylglycerol was also effective as a substrate of triacylglycerol synthesis. Furthermore, 1,2-diacylglycerol could be replaced by several kinds of aliphatic alcohols as fatty acid acceptors in the reverse micellar system. In this case, those alcohols with chain length more than 4 carbons were effectively used for ester formation.

Journal ArticleDOI
TL;DR: The greatest potential for biomodification by fermentation with C. lipolytica seems to be in altering glyceride structure, and the fatty acid composition of the yeast oil was quite similar to that of the substrate oil under optimum conditions of deposition.
Abstract: Various oil-accumulating yeasts were tested for their ability to produce lipase and live on fats and oils as carbon sources. Of these,Candida lipolytica seemed most promising, and the possibility was explored of modifying fats and oils by fermenting them withC. lipolytica and extracting the modified oil deposited in the yeast cells. Oxygen was required for the growth of yeast on fats and oils, but unless the oxygen level was controlled at a low value after cell populations peaked, most of the substrate oil was converted to citrates rather than accumulating as oil. Oil accumulation byC. lipolytica from a corn oil substrate was slightly depressed by excess nitrogen in the medium. The yeasts were able to use about 18 g/l of oil in 72 hr. At substrate oil levels greater than 18 g/l, the dry yeasts were 60% oil, and about 45–57% of the substrate oil was recovered as yeast oil. The fatty acid composition of the yeast oil was quite similar to that of the substrate oil under optimum conditions of deposition. Sterols, but not tocopherols, were transferred from the substrate to the yeast oil.Candida lipolytica oil was high in free fatty acids. The greatest potential for biomodification by fermentation withC. lipolytica seems to be in altering glyceride structure.

Journal ArticleDOI
TL;DR: Brain LP lipase activity in adult rats was decreased in all four regions examined, most significantly in the hypothalamus, after 72 hr of food deprivation, suggesting that this enzyme may be regulated by metabolic or nutritional factors.
Abstract: Lipoprotein lipase (LP lipase, triacylglycero-protein acylhydrolase EC 3.1.1.34) activity was found in four dissimilar brain regions (hypothalamus, cortex, cerebellum, and midbrain) of adult male rats. Progressive accumulation of LP lipase activity in cultured fetal rat hypothalamic cells was also observed, indicating de novo synthesis of the lipase. The brain LP lipase activity was serum-dependent and was inhibited by 1 M NaCl and by protamine sulfate. Kinetic analysis revealed an apparent Km of 0.79 mM very similar to that of rat adipose tissue LP lipase. That the lipase was functioning in the cultured brain cells was indicated by uptake and incorporation of radioactivity from tri[( 1-14C]oleoyl)glycerol into cellular triacylglycerols, and into more polar lipids, such as phosphatidylcholine. Furthermore, brain LP lipase activity in adult rats was decreased in all four regions examined, most significantly in the hypothalamus, after 72 hr of food deprivation. Thus, authentic LP lipase is present in adult rat brain and can be synthesized by isolated brain cells in vitro. LP lipase also mediates the uptake of triacylglycerol fatty acids and their subsequent incorporation into cellular lipids of cultured brain cells. Decreased brain LP lipase activity after fasting suggests that this enzyme may be regulated by metabolic or nutritional factors. Because the largest changes in LP lipase activity in response to food deprivation occurred in the hypothalamus, the enzyme may have a role in hypothalamic control of food intake or in body-weight regulation.

Journal ArticleDOI
TL;DR: The possible reaction sequence in synthesis of ester oligomer by Aspergillus niger lipase is described and the dominant components of synthesized esters were pentamer and heptamer.
Abstract: Lipase from Aspergillus niger NRRL 337 catalyzed the synthesis of esters from various dicarboxylic acids and diols. Among the esters synthesized, those from 1,13-tridecanedioic acid and 1,3-propanediol were separated by gel permeation chromatography. The constitution of the purified ester was determined by using IR and MS. The dominant components of synthesized esters were pentamer and heptamer, and both end groups of the pentamer and heptamer were hydroxyl.The possible reaction sequence in synthesis of ester oligomer by Aspergillus niger lipase is described.

Journal ArticleDOI
TL;DR: Findings indicate that nutritional regulation in the tissue levels of pancreatic enzymes and proenzymes is mediated by changes in the content of active cytoplasmic mRNAs.
Abstract: The mechanism by which changes in diet mediate levels of exportable enzymes and proenzymes in pancreatic tissue were studied in rats. The relative levels of mRNA coding for pancreatic amylase, lipase, procarboxypeptidases A and B, and the family of serine protease zymogens have been determined by the ability of isolated RNA to direct the synthesis of these products in a high-fidelity micrococcal nuclease-treated reticulocyte-lysate translation system. Translation products synthesized in vitro correlated directly with products synthesized in vivo in pancreatic lobules. Dietary adaptation was observed when dietary carbohydrate was increased from 0 to 58% at the expense of protein (81–23%). The increase in dietary carbohydrate over this range resulted in a 2-fold increase in amylase synthesis in pancreatic lobules and a 1.8-fold increase in mRNA-directed synthesis of amylase in the translation system in vitro. Concomitant with the decrease in dietary protein, synthesis of serine protease zymogens in pancreatic lobules and in the system in vitro decreased by approximately 50%. Over this range of dietary manipulation, ratios of amylase to serine proteases showed a 3.6-fold change. When dietary carbohydrate was further increased to 81% and protein reduced to 0, non-adaptive changes were observed since there was a decrease in amylase synthesis under conditions both in vivo and in vitro. mRNAs coding for pancreatic lipase and procarboxypeptidases A and B were unaffected by the dietary changes. These findings indicate that nutritional regulation in the tissue levels of pancreatic enzymes and proenzymes is mediated by changes in the content of active cytoplasmic mRNAs.

Journal ArticleDOI
TL;DR: Lipase and protease were produced simultaneously by Pseudomonas fluorescens 27 in three types of broth and on a dialysis membrane resting on semisolid media as discussed by the authors.

Journal ArticleDOI
TL;DR: Serial measurements of these three enzyme levels in patients recovering from acute pancreatitis indicated that pancreatic isoamylase and lipase were elevated above normal to a greater extent and remained elevated much longer than did the total amylase.
Abstract: We compared results of measurements of total serum amylase, pancreatic isoamylase, and lipase measurements in patients with hyperamylasemia. Serial measurements of these three enzyme levels in patients recovering from acute pancreatitis indicated that pancreatic isoamylase and lipase were elevated above normal to a greater extent and remained elevated much longer than did the total amylase. This finding indicates an appreciable sensitivity advantage of the pancreatic isoamylase and lipase over total amylase measurement during the recovery phase of pancreatitis. Comparison of pancreatic isoamylase and lipase levels in selected sera indicated a good correlation (r=0.84) between these two measurements in patients who did not have macroamylasemia. Lipase was normal in sera with amylase elevations due solely to salivary isoamylase. Thus, in nonmacroamylsemic sera, pancreatic isoamylase and lipase appear to be roughly interchangeable markers of the level of pancreatic enzymes in the blood. An advantage of the lipase assay is that this enzyme is normal in hyperamylasemia caused by macroamylasemia, whereas the inhibitor assay indicates that the pancreatic isoamylase is elevated. Development of automated assays for either pancreatic isoamylase or lipase should lead to the routine use of one of these assays in place of the present reliance on total amylase measurements in the diagnosis of pancreatitis.

Journal ArticleDOI
TL;DR: A role of hepatic lipase in the catabolism of phospholipids of VLDL and possibly HDL is suggested, resulting in prominence of larger, lipid-enriched HDL particles in HDL3 and HDL2a subclasses.

Journal ArticleDOI
K.J. Gaskin1, Peter R. Durie1, Linda Lee1, R. Hill1, Gordon G. Forstner1 
TL;DR: It was indicated that fat digestion and subsequent fat absorption depended on colipase secretion up to at least a level of 25% fecal fat excretion and nonpancreatic factors could well govern the extent of fat absorption above this level, ascolipase secretory values in this range were uniformly low.

Journal ArticleDOI
TL;DR: Lipoprotein lipase modified with polyethylene glycol dissolved in benzene, and catalyzed various reactions of ester synthesis, ester exchange and aminolysis had a high stability.
Abstract: Lipoprotein lipase modified with polyethylene glycol dissolved in benzene, and catalyzed various reactions of ester synthesis, ester exchange and aminolysis. This modified enzyme had a high stability; 50% of the initial enzymic activity were retained after about 3 months-storage in benzene at room temperature. We can repeatedly re-use the enzyme by recovering from benzene solution; the enzyme precipitates upon addition of n-hexane(or petroleum ether).

Patent
22 Jun 1984
TL;DR: In this article, an enzymatic detergent additive the active component of which is a microbially produced lipase, characterised in that the lipase is producible by means of a lipase producing strain of fusarium oxysporum, was provided.
Abstract: There is provided an enzymatic detergent additive the active component of which is a microbially produced lipase, characterised in that the lipase is producible by means of a lipase producing strain of fusarium oxysporum, as well as a detergent comprising such an enzymatic additive and a washing process suing such a detergent.

Journal ArticleDOI
01 Dec 1984-Lipids
TL;DR: The results revealed that iso-octane and cyclohexane are superior to the other solvents examined for enzymatic fat splitting in organic solvent systems.
Abstract: The effect of organic solvents on the stability and catalytic activity of the microbial lipase fromCandida rugosa for hydrolysis of triglyceride (fat splitting) has been examined. The solvents examined were 5 hydrocarbons (n-hexane, n-heptane, n-octane, iso-octane and cyclohexane) and 3 ethers (diethyl-ether, diisopropylether and di-n-butylether). The results revealed that iso-octane and cyclohexane are superior to the other solvents examined for enzymatic fat splitting in organic solvent systems.

Journal ArticleDOI
TL;DR: It is suggested that interaction of the lipase with substrate and associated intracellular membranes may be a novel feature of the regulation of lipolysis in 3T3-L1 cells.

Journal ArticleDOI
TL;DR: In this method for measuring lipoprotein lipase (LPL) and hepatic triglyceridelipase (H-TGL) in post-heparin plasma, the released free fatty acids enzymically are determined and the method is as sensitive as the radioisotopic method.
Abstract: In this method for measuring lipoprotein lipase (LPL) and hepatic triglyceride lipase (H-TGL) in post-heparin plasma, we determine the released free fatty acids enzymically. After release, they are extracted by Dole 's method (J. Biol. Chem. 235: 2595-2599, 1960), solubilized with Triton X-100, then measured with an enzymic kit (NEFA Kit-K; Nippon Shoji Kaisha Ltd.) after residual turbidity is removed by centrifugation with chloroform. A 5-microL sample of post-heparin plasma suffices to measure the activity of LPL and H-TGL; thus the method is as sensitive as the radioisotopic method. Selective assay of LPL and H-TGL, by adding sodium dodecyl sulfate to inactivate H-TGL or NaCl to inactivate LPL, is also feasible. The mean activities +/- SD of LPL and H-TGL in plasma of normal healthy men were respectively 9.4 +/- 2.3 mumol/h per milliliter (157 +/- 38 U/L) and 20.1 +/- 10.4 (335 +/- 173 U) mumol/h per milliliter (U/L).