Changes in lipase activity when using gelatinous agents

2021 ◽  
pp. 40-41
Author(s):  
Михаил Александрович Лаврухин ◽  
Алла Евгеньевна Баженова ◽  
Оксана Сергеевна Руденко ◽  
Николай Борисович Кодратьев
Keyword(s):  
Lipase Activity ◽  
Lipolytic Activity ◽  
Lipolytic Enzymes ◽  
Agar Solution ◽  
Confectionery Products

Липолитическая порча, приводящая к появлению мыльного привкуса, является браковочным признаком кондитерских изделий. Исследовано влияние студнеобразователей на активность липолитических ферментов, Растворы пектина и желатина не оказали влияния на липолитическую активность, а 1%-ный раствор агара увеличил ее на 10 %. Результаты работы способствуют повышению сохранности кондитерских изделий. Lipolytic spoilage, which leads to the appearance of a soapy taste, is a defective sign of confectionery products. The effect of gelatinous agents on the activity of lipolytic enzymes was studied, pectin and gelatin solutions did not affect the lipolytic activity, and 1 % agar solution increased by 10 %. The results of the work contribute to improving the safety of confectionery products.

scholarly journals Characterization of the Gene Encoding the Major Secreted Lysophospholipase A of Legionella pneumophila and Its Role in Detoxification of Lysophosphatidylcholine

2002 ◽  
Vol 70 (11) ◽  
pp. 6094-6106 ◽  
Author(s):  
Antje Flieger ◽  
Birgid Neumeister ◽  
Nicholas P. Cianciotto
Keyword(s):  
Fatty Acids ◽  
Legionella Pneumophila ◽  
Lipolytic Activity ◽  
Cholesterol Acyltransferase ◽  
Phospholipase A ◽  
Wild Type ◽  
Gene Encoding ◽  
Acyltransferase Activity ◽  
Lipolytic Enzymes ◽  
Cloned Gene

ABSTRACT We previously showed that Legionella pneumophila secretes, via its type II secretion system, phospholipase A activities that are distinguished by their specificity for certain phospholipids. In this study, we identified and characterized plaA, a gene encoding a phospholipase A that cleaves fatty acids from lysophospholipids. The plaA gene encoded a 309-amino-acid protein (PlaA) which had homology to a group of lipolytic enzymes containing the catalytic signature GDSL. In Escherichia coli, the cloned gene conferred trypsin-resistant hydrolysis of lysophosphatidylcholine and lysophosphatidylglycerol. An L. pneumophila plaA mutant was generated by allelic exchange. Although the mutant grew normally in standard buffered yeast extract broth, its culture supernatants lost greater than 80% of their ability to release fatty acids from lysophosphatidylcholine and lysophosphatidylglycerol, implying that PlaA is the major secreted lysophospholipase A of L. pneumophila. The mutant's reduced lipolytic activity was confirmed by growth on egg yolk agar and thin layer chromatography and was complemented by reintroduction of an intact copy of plaA. Overexpression of plaA completely protected L. pneumophila from the toxic effects of lysophosphatidylcholine, suggesting a role for PlaA in bacterial detoxification of lysophospholipids. The plaA mutant grew like the wild type in U937 cell macrophages and Hartmannella vermiformis amoebae, indicating that PlaA is not essential for intracellular infection of L. pneumophila. In the course of characterizing plaA, we discovered that wild-type legionellae secrete a phospholipid cholesterol acyltransferase activity, highlighting the spectrum of lipolytic enzymes produced by L. pneumophila.

scholarly journals Correlation of lipase activity and moisture transfer rate in gingerbread glazed with confectionery glaze based on lauric type fats

2020 ◽  
Vol 81 (4) ◽  
pp. 62-70
Author(s):  
O. S. Rudenko ◽  
N. B. Kondratiev ◽  
M. A. Pesterev ◽  
A. E. Bazhenova ◽  
N. V. Linovskaya
Keyword(s):  
Water Activity ◽  
Lipase Activity ◽  
Transfer Rate ◽  
Moisture Transfer ◽  
Raw Materials ◽  
Threshold Value ◽  
Layer By Layer ◽  
Organoleptic Evaluation ◽  
Organoleptic Characteristics ◽  
Confectionery Products

Ensuring the quality of confectionery products and controlling factors affecting changes in organoleptic characteristics during storage requires studying processes that affect lipase activity, one of which is the process of moisture migration. Lipase activity, the rate of the moisture transfer process, and the change in microbiota in various parts of the model samples of raw gingerbread with fruit filling, glazed with confectionery glaze based on lauric type fats, packed in a polypropylene film 40 ?m thick in an average layer-by-layer sample were studied: top layer with glaze, filling, baked semi-finished product. Studies have shown a correlation between analytical results and organoleptic evaluation. During storage during moisture transfer, moisture migrates from the filling to the baked semi-finished product and then to the upper layer with glaze, while in all layers the mass fraction of moisture stably remains above 5%, which is higher than the value at which lipase activity is maintained. The moisture transfer rate in the top layer was 1.12, in the baked semi-finished product – 1.34 and in the filling – 7.03 g/m2·s (· 10-4). Water activity decreased, but did not reach a threshold value of 0.6 after 12 weeks of storage. At the same time, at 6-8 weeks of storage, there is an increase in the activity of water in the baked semi-finished product, which indicates the release of free moisture. Organoleptic analysis revealed a “soapy” taste, starting from the 8th week of storage, which correlates with an increase in water activity. Microbiological studies showed a significant increase in the content of QMAFAnM from 8 weeks of storage, mold growth up to 410 CFU/g was observed at 10 weeks of storage. Studies have shown a correlation of lipase activity with moisture transfer processes and microbiota growth, which requires more stringent quality control of raw materials and storage conditions to prevent lipolytic damage to flour confectionery products glazed with confectionery glaze based on lauric type fats.

Cardiac triacylglycerol content and lipase activity during recovery from exercise

1989 ◽  
Vol 66 (3) ◽  
pp. 1099-1103 ◽  
Author(s):  
B. Podbielski ◽  
W. K. Palmer
Keyword(s):  
Lipase Activity ◽  
Temporal Relationship ◽  
Lipolytic Activity ◽  
Control Level ◽  
Female Rats ◽  
Lipolytic Enzyme ◽  
Glycogen Level ◽  
Control Activity ◽  
Triacylglycerol Content ◽  
Plasma Ffa

Female rats swam for 2-h to determine the temporal relationship between triglyceride (TG) repletion and TG lipase activity in the heart during recovery from exercise. Immediately after the exercise, plasma free fatty acids (FFA) had increased from a resting value of 0.44 +/- 0.04 to 0.84 +/- 0.04 mM. Heart TG concentration was reduced 75%, whereas the glycogen level was decreased 34% below control. TG lipase activity was elevated 33% above control activity. One hour after the end of the exercise, lipolytic activity was still 26% above control and did not return to the resting level until the 4th h of recovery. The cardiac TG concentration was back to control levels by the 2nd h after the swim. Plasma FFA concentrations remained elevated during the first 4 h of recovery and were back to the control level by h 8. Cardiac glycogen was “supercompensated” during recovery h 1 and 2 and returned to the preexercise level by h 4. These data indicate that TG is being synthesized in the heart while lipolytic enzyme activity is elevated above control levels. This points out that the rate of TG synthesis is in excess of the hydrolysis. Since plasma FFA concentrations are elevated during periods of augmented TG synthesis, substrate availability, namely plasma FFA, may play a key role in regulating the size of the intracellular TG pool.

Inhibition of a Mixture of Crude Pseudomonas Lipases by Selected Emulsifiers

1993 ◽  
Vol 56 (6) ◽  
pp. 541-542 ◽  
Author(s):  
P. L. HARRIS ◽  
S. L. CUPPETT
Keyword(s):  
Sodium Oleate ◽  
Lipase Activity ◽  
Lipolytic Activity ◽  
Sodium Stearate ◽  
Pseudomonas Spp ◽  
Dry Milk ◽  
Nonfat Dry Milk ◽  
The Individual ◽  
Emulsifier Concentration

Four commercial emulsifiers, sodium oleate, sodium stearate, sodium stearoyl-2-lactylate, and calcium stearoyl-2-lactylate, were evaluated for their effectiveness as inhibitors of Pseudomonas lipases. Each emulsifier was incubated at 0.5, 1.0, and 2.0% concentrations with the individual as well as a mixture of the crude lipase extracts obtained from three Pseudomonas spp. (P. fluorescens, P. putida, and P. cepacia), in reconstituted nonfat dry milk (10%) for 30 min. At a 2% concentration, all emulsifiers tested were potent inhibitors (100%) of lipase activity. The effectiveness of lipolysis inhibition declined with decreasing emulsifier concentration. Sodium oleate demonstrated significant (P < 0.05) lipolysis inhibition at a 1% concentration regardless of initial lipase level. Synergism in inhibiting lipolytic activity between these selected emulsifiers was not evident.

Lipolytic Activities in Post-Heparin Plasma in Man Measured with Different Substrate Emulsions

1978 ◽  
Vol 54 (2) ◽  
pp. 201-203
Author(s):  
B. Vessby ◽  
J. Boberg ◽  
H. Lithell
Keyword(s):  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipolytic Activity ◽  
Heparin Plasma ◽  
Post Heparin Lipolytic Activity

1. Post-heparin lipolytic activity in man has been studied by using a triglyceride substrate emulsion containing different emulsifiers. 2. The lipolytic activity measured was profoundly influenced by the type of emulsifier used in the substrate. Substrates stabilized by synthetic emulsifiers give higher lipolytic activity than Intralipid, which contains egg phospholipids as emulsifiers. This difference was solely explained by higher salt-resistant lipase activities found with emulsions containing synthetic emulsifiers. The salt-inhibited lipase activity, which has properties as a lipoprotein lipase, was not influenced by the type of emulsifier. 3. When used under specified conditions Intralipid seems to be virtually specific for extrahepatic post-heparin lipolytic activity.

scholarly journals Complete loss of heparin-releasable triacylglycerol lipase activity after collagenase treatment of the rat liver

1978 ◽  
Vol 172 (1) ◽  
pp. 177-179 ◽  
Author(s):  
J Thomas ◽  
L J Debeer ◽  
G P Mannaerts
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Lipase Activity ◽  
Lipolytic Activity ◽  
Complete Loss ◽  
Triacylglycerol Lipase ◽  
Collagenase Treatment ◽  
Membrane Bound

Lipolytic activity at pH 8.5-9.5 was lowered by approx. 80% in homogenates from livers perfused with collagenase or heparin. No heparin-releasable lipase activity was detected in hepatocytes isolated by collagenase treatment. It is concluded that crude collagenase completely inactivates the plasma-membrane-bound heparin-releasable lipase.

Modifications of Plasma Post-Heparin Lipolytic Activity and Tissue Lipoprotein Lipase Activity Induced in the Rat by Acute Administration of Ethanol or Propan-2-ol

1975 ◽  
Vol 48 (2) ◽  
pp. 153-156
Author(s):  
Y. Giudicelli ◽  
R. Nordmann ◽  
J. Nordmann
Keyword(s):  
Body Weight ◽  
Adipose Tissue ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipolytic Activity ◽  
Ethanol Administration ◽  
Acute Administration ◽  
Post Heparin Lipolytic Activity ◽  
Adipose Tissue Lipoprotein Lipase ◽  
Made In

1. The oral administration of propan-2-ol [isopropanol; 100 mmol (6 g)/kg body weight] or ethanol [130 mmol (6 g)/kg body weight] to starved rats produced no change in plasma post-heparin lipase activity (PHLA) compared with that observed in 154 mmol/l sodium chloride (saline)-treated rats. 2. An increase of adipose tissue lipoprotein lipase (LLA) and a decrease of heart LLA occurred in isopropanol-treated animals, whereas no significant changes were found in these activities after ethanol administration. 3. Since administration of isopropanol produces hyperglycaemia, observations were also made in rats receiving glucose infusion rather than saline. In these animals a rise in PHLA and adipose tissue LLA, and a fall in heart LLA, occurred. 4. It is suggested that the changes in tissue LLA produced by isopropanol are mediated by the rise in blood glucose.

Characterization of the triacylglycerol lipase activity in three types of rat skeletal muscle

1987 ◽  
Vol 65 (3) ◽  
pp. 317-322 ◽  
Author(s):  
Wayne C. Miller ◽  
Warren K. Palmer ◽  
David A. Arnall ◽  
Lawrence B. Oscai
Keyword(s):  
Skeletal Muscle ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipolytic Activity ◽  
Vastus Lateralis ◽  
High Energy ◽  
Glycolytic Flux ◽  
Ph Optimum ◽  
Triacylglycerol Lipase ◽  
Triglyceride Lipase

The purpose of this study was to characterize the lipolytic activity of the alkaline triglyceride lipase in homogenates of three types of skeletal muscle obtained from heparin-perfused rat hindlimb. Specifically, the red portion of the vastus lateralis, the white portion of the vastus lateralis, and the soleus muscles were examined. To remove capillary-bound lipoprotein lipase from the capillary beds, muscle was perfused with an erythrocyte-free buffer containing 4% albumin, 5 units of heparin/mL, and 7.5 μM adenosine. Adenosine reduced perfusion pressure from 117 ± 5 to 86 ± 6 mmHg (1 mmHg = 133.32 Pa), providing evidence for an effective vasodilation. This vasodilation increased the amount of lipoprotein lipase removed from the capillary beds. By the end of the experiment, perfusates were lipoprotein lipase-free. Oxygen supply to the perfused hindlimb appeared adequate as evidenced by similar high energy phosphate values for perfused and contralateral control tissues. For example, in soleus muscle, ATP content was 4.5 ± 0.6 vs. 4.2 ± 0.3 μmol/g, ADP concentration was 1.0 ± 0.2 vs. 1.4 ± 0.2 μmol/g, and creatine phosphate level was 12.9 ± 0.7 vs. 11.0 ± 0.6 μmol/g for perfused and contralateral control soleus, respectively. In addition, K+ output by the hindlimb was negligible, while glycolytic flux of perfused muscle was similar to that measured in control tissue. The findings that triglyceride levels of soleus and red vastus lateralis were decreased suggest that endogenous triglyceride was providing energy for the hindlimb during perfusion. Skeletal muscle triglyceride lipase activity was stimulated by serum and heparin, inhibited by NaCl and protamine, and had a pH optimum of 8.1. These results are consistent with the hypothesis that the major lipolytic activity present in the intracellular compartment of skeletal muscle is the alkaline triglyceride lipase with characteristics similar to those of lipoprotein lipase.

Adipocyte triglyceride lipase expression in human obesity

2007 ◽  
Vol 293 (4) ◽  
pp. E958-E964 ◽  
Author(s):  
Gregory R. Steinberg ◽  
Bruce E. Kemp ◽  
Matthew J. Watt
Keyword(s):  
Adipose Tissue ◽  
Protein Expression ◽  
Mrna Expression ◽  
Visceral Adipose Tissue ◽  
Lipase Activity ◽  
Subcutaneous Adipose Tissue ◽  
Lipolytic Enzymes ◽  
Obese Subjects ◽  
Visceral Adipose ◽  
Subcutaneous Adipose

We have investigated the gene and protein expression of adipose triglyceride lipase (ATGL) and triglyceride (TG) lipase activity from subcutaneous and visceral adipose tissue of lean and obese subjects. Visceral and subcutaneous adipose tissue was obtained from 16 age-matched lean and obese subjects during abdominal surgery. Tissues were analyzed for mRNA expression of lipolytic enzymes by real-time quantitative PCR. ATGL protein content was assessed by Western blot and TG lipase activity by radiometric assessment. Subcutaneous and visceral adipose tissue of obese subjects had elevated mRNA expression of PNPLA2 (ATGL) and other lipases including PNPLA3, PNPLA4, CES1, and LYPLAL1 ( P < 0.05). Surprisingly, ATGL protein expression and TG lipase activity were reduced in subcutaneous adipose tissue of obese subjects. Immunoprecipitation of ATGL reduced total TG lipase activity in adipose lysates by 70% in obese and 83% in lean subjects. No significant differences in the ATGL activator CGI-58 mRNA levels ( ABHD5) were associated with obesity. These data demonstrate that ATGL is important for efficient TG lipase activity in humans. They also demonstrate reduced ATGL protein expression and TG lipase activity despite increased mRNA expression of ATGL and other novel lipolytic enzymes in obesity. The lack of correlation between ATGL protein content and in vitro TG lipase activity indicates that small decrements in ATGL protein expression are not responsible for the reduction in TG lipase activity observed here in obesity, and that posttranslational modifications may be important.

scholarly journals Specificity and localization of lipolytic activity in adult Drosophila melanogaster

1994 ◽  
Vol 304 (3) ◽  
pp. 775-779 ◽  
Author(s):  
G M Smith ◽  
K Rothwell ◽  
S L Wood ◽  
S J Yeaman ◽  
M Bownes
Keyword(s):  
Drosophila Melanogaster ◽  
Lipase Activity ◽  
Specific Activity ◽  
Lipolytic Activity ◽  
Accessory Gland ◽  
Null Mutant ◽  
Male Accessory Gland ◽  
Accessory Glands ◽  
Esterase 6 ◽  
Adult Drosophila

The triacylglycerol lipases present in adult Drosophila melanogaster have been investigated. Different lipase activities are present in various tissues in the fly. In particular, an abundant lipase activity is present in the male accessory gland. An esterase null mutant was used to confirm that the enzyme activity was due to a distinct lipase and not non-specific activity from esterase 6 which is also abundant in accessory glands. The properties of the accessory-gland lipase were investigated, and pH optima and substrate utilization suggest that it has some similarities to vertebrate bile-salt-stimulated lipase. Lipase activity is significantly reduced in males and increased in females shortly after mating. This finding suggests that lipase activity is transferred to the female and may be important in mating and reproduction in Drosophila.

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