Long-Chain Triacylglycerol Acyl Hydrolase (Lipase) Activity in Wheat Grain

1987 ◽  
pp. 365-367
Author(s):  
T. Galliard ◽  
M. Lond ◽  
D. M. Gallagher
Keyword(s):  
Lipase Activity ◽  
Wheat Grain ◽  
Long Chain

Gastric Lipolysis and Fat Absorption in Preterm Infants: Effect of Medium-Chain Triglyceride or Long-Chain Triglyceride-Containing Formulas

PEDIATRICS ◽  
1989 ◽  
Vol 83 (1) ◽  
pp. 86-92 ◽  
Author(s):  
Margit Hamosh ◽  
Joel Bitman ◽  
Teresa H. Liao ◽  
N. R. Mehta ◽  
R. J. Buczek ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Weight Gain ◽  
Preterm Infants ◽  
Lipase Activity ◽  
Medium Chain Triglyceride ◽  
Fat Absorption ◽  
Medium Chain ◽  
Long Chain ◽  
Long Chain Triglyceride

The extent of gastric lipolysis, fat absorption, and infant weight gain was studied in 12 preterm infants (gestational age 28.75 ± 0.50 weeks, postnatal age 6.08 ± 0.81 weeks) fed medium-chain triglyceride or long-chain triglyceride formula for 1 week in a crossover design. The former formula contained 42% of 8:0 and 10:0 and 19% of 12:0, 14:0, and 16:0; the latter formula contained only 7% of 8:0 and 10:0 and 46% of 12:0, 14:0, and 16:0. Gastric aspirates were obtained on the second and third day of formula feeding for quantitation of lipase activity and of the extent of gastric lipolysis. Fat balance studies were conducted during the last three days of each feeding regimen. The study showed that (1) there was marked hydrolysis of formula fat in the stomach during feeding of either medium-chain triglyceride formula or long-chain triglyceride formula (20% and 16%, respectively); (2) lipase activity in the gastric aspirates was less during feeding of medium-chain triglyceride formula than before the meal, which suggested stimulation of lipase secretion by long-chain fatty acid released from long-chain triglyceride formula fat or more rapid binding of lipase to ingested lipid in the medium-chain triglyceride formula; (3) fatty acid distribution in glycerides and free fatty acids showed preferential release of medium-chain (8:0, 10:0) and long-chain unsaturated (18:1, 18:2) fatty acids in the stomach. The low content of 8:0 and 10:0 in gastric triglyceride and free fatty acids suggested that medium-chain fatty acids were absorbed directly in the stomach. (4) fat balance studies showed almost identical absorption rates (84.6% ± 3.1% and 82.8% ± 4.0%) and weight gain (23.0 ± 1.5 g/d and 20.8 ± 1.8 g/d) during feeding of either medium-chain triglyceride or long-chain triglyceride formula. In this study, in which each infant was fed either formula alternately, it was shown that although the extent of fat digestion varied among infants, medium-chain and long-chain triglyceride were absorbed to the same extent by most infants.

The lipase activity of a partially purified lipolytic enzyme of Escherichia coli

1978 ◽  
Vol 56 (5) ◽  
pp. 324-328 ◽  
Author(s):  
G. Nantel ◽  
Georgia Baraff ◽  
P. Proulx
Keyword(s):  
Escherichia Coli ◽  
Lipase Activity ◽  
Slow Rate ◽  
Water Soluble ◽  
Lipolytic Enzyme ◽  
Ph Optimum ◽  
Chain Acyl ◽  
Marked Preference ◽  
Hydrolysis Of ◽  
Long Chain

Escherichia coli lipase was found to have a broad pH optimum between pH 8 and 10. Long-chain acyl triacylglycerols such as trioleoylglycerol were hydrolysed at a relatively slow rate, whereas, the shorter-chain acyl derivative tricapryloylglycerol was not. Triacylglycerols and diacylglycerols were broken down at a rate 10- to 15-fold greater than that for monoacylglycerol. Simple esters such as methyloieate and cetylpalmitate were hydrolysed at rates greater than that of triacylglycerol. Water-soluble esters such as p-nitrophenylacetate were not attacked. Hydrolysis of lipase substrates occurred more readily in the presence of an anionic detergent such as taurocholate. The enzyme had no marked preference for the 1- or 3-position of triacylglycerols but attacked these positions much more readily than position 2. The enzyme also catalyzed transacylation reactions with simple alcohols such as methanol or ethanol.

Long-chain fatty acids decrease lipoprotein lipase activity of cultured rat adipocyte precursors

Metabolism ◽  
1994 ◽  
Vol 43 (2) ◽  
pp. 144-151 ◽  
Author(s):  
James L. Kirkland ◽  
Charles H. Hollenberg ◽  
Sarah Kindler ◽  
Daniel A.K. Roncari
Keyword(s):  
Fatty Acids ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Long Chain Fatty Acids ◽  
Lipoprotein Lipase Activity ◽  
Long Chain ◽  
Chain Fatty Acids

Changes in biochemical and physicochemical indicators of food grain of wheat during long-term laboratory storage

2021 ◽  
Vol 30 (1) ◽  
pp. 40-43
Author(s):  
L.G. Priezzheva ◽  
◽  
V.F. Sorochinskiy ◽  
I.A. Vereznikova ◽  
A.I. Koval ◽  
...  
Keyword(s):  
Lipase Activity ◽  
Natural Increase ◽  
Acid Number ◽  
Food Storage ◽  
Chemical Quality ◽  
Wheat Grain ◽  
Physico Chemical ◽  
Different Temperatures ◽  
Food Grain

The results of changes in the biochemical and physico-chemical quality indicators of food grain of wheat crops in 2015 and 2018 are presented during long-term laboratory storage at elevated (+ 30°C), moderate (+ 20°C), and low (+ 10°C) temperatures at standard humidity for wheat grain (no higher than 14%). We found that food storage of wheat grain impacted at different temperatures for 19 months leads to a natural increase in the acid number of the fat (ANF) at different initial values, which indicates the preservation of lipase activity and the possibility of using this indicator to establish the terms of safe storage and shelf life.

Lipase secretion from dispersed rabbit gastric glands

1985 ◽  
Vol 248 (1) ◽  
pp. G68-G72 ◽  
Author(s):  
C. S. Fink ◽  
M. Hamosh ◽  
P. Hamosh ◽  
S. J. DeNigris ◽  
D. K. Kasbekar
Keyword(s):  
Lipase Activity ◽  
Opposite Effect ◽  
Dry Weight ◽  
Gastric Glands ◽  
Stomach Mucosa ◽  
Isolated Gastric Glands ◽  
Gastric Lipase ◽  
Carbonyl Cyanide ◽  
Hydrolysis Of ◽  
Long Chain

We have measured gastric lipase activity in dispersed glands of rabbit stomach by quantitating the hydrolysis of tri[3H]olein. Lipase activity in isolated gastric glands was 200-400 nmol [3H]oleic acid released per milligram dry weight per minute. The percentage of lipase activity released during incubation for 30 min at 37 degrees C under basal conditions was 1.5-4.5%. Lipase release was stimulated by secretagogues: 10 nM cholecystokinin octapeptide (CCK-8) and 100 microM carbachol led to four- to sixfold and two- to threefold higher enzyme secretion, respectively, while histamine had no effect. Carbonyl cyanide m-chlorophenylhydrazone (30 microM) completely inhibited the CCK-8-induced lipase release, indicating that lipase secretion is dependent on mitochondrial oxidative energy; dibutyryl cGMP (1 mM) inhibited 1 nM CCK-8-stimulated but not 100 microM carbachol-stimulated secretion; atropine (1 microM) had the opposite effect. These studies suggest that secretion of lipase from isolated gastric glands is stimulated by at least two receptor mechanisms. These studies show that a lipase that hydrolyzes long-chain triglyceride is secreted by rabbit stomach mucosa and that the secretion of gastric lipase is stimulated by two different receptor mechanisms.

scholarly journals Partial purification of a diacylglycerol lipase from bovine aorta

1994 ◽  
Vol 298 (1) ◽  
pp. 213-219 ◽  
Author(s):  
M W Lee ◽  
D L Severson
Keyword(s):  
Lipase Activity ◽  
Specific Activity ◽  
Competitive Inhibitor ◽  
Short Chain ◽  
Partial Purification ◽  
Diacylglycerol Lipase ◽  
Bivalent Cations ◽  
Triton X ◽  
Hydrolysis Of ◽  
Long Chain

A diacylglycerol (DG) lipase has been purified from a soluble subcellular fraction of bovine aorta by (NH4)2SO4 precipitation in the presence of 5.0% (w/v) Triton X-100, followed by chromatography on DEAE-Sephacel, heparin-Sepharose and octyl-Sepharose in the presence of either CHAPS or Triton X-100 detergents. Under basal conditions, the hydrolysis of a short-chain [3H]dioctanoylglycerol ([3H]diC8) substrate was much greater than that of a long-chain 1-[1-14C]palmitoyl-2-oleoyl-sn-glycerol (1-[14C]POG) substrate. Lipase activity measured with 1-[14C]POG was markedly enhanced by Triton X-100. In the presence of 0.1% Triton X-100, specific enzyme activities in the octyl-Sepharose fraction determined with 1-[14C]POG or 1-stearoyl-2-[1-14C]-arachidonoyl-sn-glycerol as substrates were the same as that measured with [3H]diC8. MgCl2 (5mM) or CaCl2 (2 mM) also selectively stimulated lipase activity (up to 10-13-fold) measured with the long-chain (1-[14C]POG) substrate only. The increase in relative specific activity in the octyl-Sepharose fraction was 60-fold and 155-fold, based on hydrolysis of [3H]diC8 and 1-[14C]POG (+ Triton X-100), respectively. Unlabelled diC8 was a competitive inhibitor of 1-[14C]POG hydrolysis, suggesting that a single lipase hydrolyses both the short-chain and long-chain DG substrates; selective stimulatory effects of non-ionic detergents and bivalent cations on the hydrolysis of 1-[14C]POG may be due to effects on the physical properties of the substrate preparation. Monoacylglycerol lipase, DG kinase and cholesterol esterase activities could not be detected in the partially purified lipase preparation.

An Ultraviolet Spectrophotometric Assay for Measuring Lipase Activity Using Long-Chain Triacyglycerols from Aleurites fordii Seeds

2002 ◽  
Vol 303 (1) ◽  
pp. 17-24 ◽  
Author(s):  
Gaëlle Pencreac'h ◽  
Jean Graille ◽  
Michel Pina ◽  
Robert Verger
Keyword(s):  
Lipase Activity ◽  
Spectrophotometric Assay ◽  
Long Chain

scholarly journals Adipose triglyceride lipase activity is inhibited by long-chain acyl-coenzyme A

2014 ◽  
Vol 1841 (4) ◽  
pp. 588-594 ◽  
Author(s):  
Harald M. Nagy ◽  
Margret Paar ◽  
Christoph Heier ◽  
Tarek Moustafa ◽  
Peter Hofer ◽  
...  
Keyword(s):  
Lipase Activity ◽  
Coenzyme A ◽  
Adipose Triglyceride Lipase ◽  
Triglyceride Lipase ◽  
Chain Acyl ◽  
Acyl Coenzyme A ◽  
Long Chain

Effect of Wheat Grain Steaming and Washing on Lipase Activity in Whole Grain Flour

2014 ◽  
Vol 91 (4) ◽  
pp. 321-326 ◽  
Author(s):  
Juliano Luiz De Almeida ◽  
Bram Pareyt ◽  
Lien R. Gerits ◽  
Jan A. Delcour
Keyword(s):  
Lipase Activity ◽  
Whole Grain ◽  
Wheat Grain ◽  
Whole Grain Flour

Regulation of lipolytic activity by long-chain acyl-coenzyme A in islets and adipocytes

2005 ◽  
Vol 289 (6) ◽  
pp. E1085-E1092 ◽  
Author(s):  
Liping Hu ◽  
Jude T. Deeney ◽  
Christopher J. Nolan ◽  
Marie-Line Peyot ◽  
Ada Ao ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Lipase Activity ◽  
Lipolytic Activity ◽  
Inhibitory Effect ◽  
Hormone Sensitive Lipase ◽  
Major Pathway ◽  
Chain Acyl ◽  
Increase Insulin Secretion ◽  
Acyl Coenzyme A ◽  
Long Chain

Intracellular lipolysis is a major pathway of lipid metabolism that has roles, not only in the provision of free fatty acids as energy substrate, but also in intracellular signal transduction. The latter is likely to be particularly important in the regulation of insulin secretion from islet β-cells. The mechanisms by which lipolysis is regulated in different tissues is, therefore, of considerable interest. Here, the effects of long-chain acyl-CoA esters (LC-CoA) on lipase activity in islets and adipocytes were compared. Palmitoyl-CoA (Pal-CoA, 1–10 μM) stimulated lipase activity in islets from both normal and hormone-sensitive lipase (HSL)-null mice and in phosphatase-treated islets, indicating that the stimulatory effect was neither on HSL nor phosphorylation dependent. In contrast, we reproduced the previously published observations showing inhibition of HSL activity by LC-CoA in adipocytes. The inhibitory effect of LC-CoA on adipocyte HSL was dependent on phosphorylation and enhanced by acyl-CoA-binding protein (ACBP). In contrast, the stimulatory effect on islet lipase activity was blocked by ACBP, presumably due to binding and sequestration of LC-CoA. These data suggest the following intertissue relationship between islets and adipocytes with respect to fatty acid metabolism, LC-CoA signaling, and lipolysis. Elevated LC-CoA in islets stimulates lipolysis to generate a signal to increase insulin secretion, whereas elevated LC-CoA in adipocytes inhibits lipolysis. Together, these opposite actions of LC-CoA lower circulating fat by inhibiting its release from adipocytes and promoting fat storage via insulin action.

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