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Pancreatic Lipase (pancreatic + lipase)
Selected AbstractsThe effect of an enzymatic pretreatment on the hydrolysis and size reduction of fat particles in slaughterhouse wastewaterJOURNAL OF CHEMICAL TECHNOLOGY & BIOTECHNOLOGY, Issue 6 2001L Masse Abstract The effect of an enzymatic pretreatment, Pancreatic Lipase 250 (PL-250), on the hydrolysis and size reduction of fat particles in slaughterhouse wastewater was characterised for enzyme doses ranging from 125 to 1000,mg,dm,3 and initial particle sizes (Din) varying between 53 and 383,µm. Treatment with PL-250 significantly reduced the size of pork fat particles in slaughterhouse wastewater. Particle size reduction increased with Din, possibly due to the more filamentous and plate-like configuration of the larger fat particles, which could be easily broken at weak points. The smaller particles were observed to be denser and more spherical. Size reduction also increased with enzyme concentration, but the benefit of adding more enzyme diminished greatly as enzyme dose was increased. The maximum long-chain fatty acid (LCFA) concentration in filtered samples was detected after 4,7,h of treatment and ranged from 8.2 to 34.9,mg,dm,3. The linear rate of LCFA released in solution during enzymatic pretreatment ranged from 39.4 to 169.9,mg,dm,3 d,1, and increased with enzyme concentration up to 500,mg,dm,3. At a PL-250 concentration of 1000,mg,dm,3, the LCFA release rate decreased, maybe due to excessive layering of adsorbed enzyme on the fat particles or increased degradation of released LCFAs. The pretreatment appeared to be more efficient with beef than pork fat particles. However, the effect of an enzymatic pretreatment on a downstream anaerobic treatment of slaughterhouse wastewater containing fat particles remains to be tested. © 2001 Society of Chemical Industry [source] The role of free fatty acids, pancreatic lipase and Ca2+ signalling in injury of isolated acinar cells and pancreatitis model in lipoprotein lipase-deficient miceACTA PHYSIOLOGICA, Issue 1 2009F. Yang Abstract Aim and methods:, Recurrent pancreatitis is a common complication of severe hypertriglyceridaemia (HTG) often seen in patients carrying various gene mutations in lipoprotein lipase (LPL). This study investigates a possible pathogenic mechanism of cell damage in isolated mouse pancreatic acinar cells and of pancreatitis in LPL-deficient and in wild type mice. Results:, Addition of free fatty acids (FFA) or of chylomicrons to isolated pancreatic acinar cells caused stimulation of amylase release, and at higher concentrations it also caused cell damage. This effect was decreased in the presence of the lipase inhibitor orlistat. Surprisingly, pancreatic lipase whether in its active or inactive state could act like an agonist by inducing amylase secretion, increasing cellular cGMP levels and converting cell damaging sustained elevations of [Ca2+]cyt to normal Ca2+ oscillations. Caerulein increases the levels of serum amylase and caused more severe inflammation in the pancreas of LPL-deficient mice than in wild type mice. Conclusion:, We conclude that high concentrations of FFA as present in the plasma of LPL-deficient mice and in patients with HTG lead to pancreatic cell damage and are high risk factors for the development of acute pancreatitis. In addition to its enzymatic effect which leads to the generation of cell-damaging FFA from triglycerides, pancreatic lipase also prevents Ca2+ overload in pancreatic acinar cells and, therefore, counteracts cell injury. [source] Molecular modeling of the dimeric structure of human lipoprotein lipase and functional studies of the carboxyl-terminal domainFEBS JOURNAL, Issue 18 2002Yoko Kobayashi Lipoprotein lipase (LPL) plays a key role in lipid metabolism. Molecular modeling of dimeric LPL was carried out using insight ii based upon the crystal structures of human, porcine, and horse pancreatic lipase. The dimeric model reveals a saddle-shaped structure and the key heparin-binding residues in the amino-terminal domain located on the top of this saddle. The models of two dimeric conformations , a closed, inactive form and an open, active form , differ with respect to how surface-loop positions affect substrate access to the catalytic site. In the closed form, the surface loop covers the catalytic site, which becomes inaccessible to solvent. Large conformational changes in the open form, especially in the loop and carboxyl-terminal domain, allow substrate access to the active site. To dissect the structure,function relationships of the LPL carboxyl-terminal domain, several residues predicted by the model structure to be essential for the functions of heparin binding and substrate recognition were mutagenized. Arg405 plays an important role in heparin binding in the active dimer. Lys413/Lys414 or Lys414 regulates heparin affinity in both monomeric and dimeric forms. To evaluate the prediction that LPL forms a homodimer in a ,head-to-tail' orientation, two inactive LPL mutants , a catalytic site mutant (S132T) and a substrate-recognition mutant (W390A/W393A/W394A) , were cotransfected into COS7 cells. Lipase activity could be recovered only when heterodimerization occurred in a head-to-tail orientation. After cotransfection, 50% of the wild-type lipase activity was recovered, indicating that lipase activity is determined by the interaction between the catalytic site on one subunit and the substrate-recognition site on the other. [source] Electrostatic-induced interfacial assembly of enzymes with nanosheets: Controlled orientation and optimized activityAICHE JOURNAL, Issue 10 2010Zhe An Abstract In this work, an electrostatic-induced interfacial assembly of porcine pancreatic lipase (PPL) with the nanosheets of layered double hydroxide (LDHNSs) is designed to rationally control the orientation of bound PPL. The PPL orientation in the bidimensional confinement spacing alters relying on the PPL loading, with the majority of active sites facing the LDH layer at low PPL loading and facing the adjacent protein molecule at high PPL loading. The biocatalytic activity of the bound PPL significantly depends on its orientation. Remarkable enhancement of the bio-activity has been observed when the PPL/LDHNSs mass ratio is less than 9, and a maximum activity is met with at PPL/LDHNSs = 0.5. In addition, the thermal stability of PPL-LDHNSs bioactivity has been obviously improved in comparison with soluble PPL. © 2010 American Institute of Chemical Engineers AIChE J, 2010 [source] ORIGINAL ARTICLE: Investigating the inhibitory activity of green coffee and cacao bean extracts on pancreatic lipaseNUTRITION BULLETIN, Issue 3 2010S. Almoosawi Summary The present study investigated the effects of green coffee bean extract and Theobroma cacao bean extract on pancreatic lipase activity in vitro. Green coffee bean extract produced a J-shaped dose-dependent inhibition of pancreatic lipase with the percentage inhibition of pancreatic lipase ranging from 11.8% to 61.5%. Similar concentrations of Theobroma cacao failed to produce any effect on pancreatic lipase. Non-linear regression analysis revealed that the concentration of green coffee bean extract required to elicit a 50% inhibition of pancreatic lipase activity (IC50) was approximately 43 µM. In conclusion, extracts of green coffee beans but not Theobroma cacao possess potent inhibitory activity against pancreatic lipase. [source] Pharmacology and safety of glycerol phenylbutyrate in healthy adults and adults with cirrhosis,,HEPATOLOGY, Issue 6 2010Brendan M. McGuire Phenylbutyric acid (PBA), which is approved for treatment of urea cycle disorders (UCDs) as sodium phenylbutyrate (NaPBA), mediates waste nitrogen excretion via combination of PBA-derived phenylacetic acid with glutamine to form phenylactylglutamine (PAGN) that is excreted in urine. Glycerol phenylbutyrate (GPB), a liquid triglyceride pro-drug of PBA, containing no sodium and having favorable palatability, is being studied for treatment of hepatic encephalopathy (HE). In vitro and clinical studies have been performed to assess GPB digestion, safety, and pharmacology in healthy adults and individuals with cirrhosis. GPB hydrolysis was measured in vitro by way of pH titration. Twenty-four healthy adults underwent single-dose administration of GPB and NaPBA and eight healthy adults and 24 cirrhotic subjects underwent single-day and multiple-day dosing of GPB, with metabolites measured in blood and urine. Simulations were performed to assess GPB dosing at higher levels. GPB was hydrolyzed by human pancreatic triglyceride lipase, pancreatic lipase-related protein 2, and carboxyl-ester lipase. Clinical safety was satisfactory. Compared with NaPBA, peak metabolite blood levels with GPB occurred later and were lower; urinary PAGN excretion was similar but took longer. Steady state was achieved within 4 days for both NaPBA and GPB; intact GPB was not detected in blood or urine. Cirrhotic subjects converted GPB to PAGN similarly to healthy adults. Simulations suggest that GPB can be administered safely to cirrhotic subjects at levels equivalent to the highest approved NaPBA dose for UCDs. Conclusion: GPB exhibits delayed release characteristics, presumably reflecting gradual PBA release by pancreatic lipases, and is well tolerated in adults with cirrhosis, suggesting that further clinical testing for HE is warranted. (HEPATOLOGY 2010;) [source] The effect of diet on the expression of lipase genes in the midgut of the lightbrown apple moth (Epiphyas postvittana Walker; Tortricidae)INSECT MOLECULAR BIOLOGY, Issue 1 2010J. T. Christeller Abstract We have identified lipase-like genes from an Epiphyas postvittana larval midgut EST library. Of the 10 pancreatic lipase family genes, six appear to encode active lipases and four encode inactive lipases, based on the presence/absence of essential catalytic residues. The four gastric lipase family genes appear to encode active proteins. Phylogenetic analysis of 54 lepidopteran pancreatic lipase proteins resolved the clade into five groups of midgut origin and a sixth of non-midgut lipases. The inactive proteins formed two separate groups with highly conserved mutations. The lepidopteran midgut lipases formed a ninth subfamily of pancreatic lipases. Eighteen insect and human gastric lipases were analysed phylogenetically with only very weak support for any groupings. Gene expression was measured in the larval midgut following feeding on five artificial diets and on apple leaves. The artificial diets contained different levels of triacylglycerol, linoleic acid and cholesterol. Significant changes in gene expression (more than 100-fold for active pancreatic lipases) were observed. All the inactive lipases were also highly expressed. The gastric lipase genes were expressed at lower levels and suppressed in larvae feeding on leaves. Together, protein motif analysis and the gene expression data suggest that, in phytophagous lepidopteran larvae, the pancreatic lipases may function in vivo as galactolipases and phospholipases whereas the gastric lipases may function as triacylglycerol hydrolases. [source] | ||||||||||||||||