Hydrolysis of sunflower oil by means of hydrophobic membrane with lipolytic activity

1989 ◽  
Vol 11 (3) ◽  
pp. 167-172 ◽  
Author(s):  
Magdalena Rucka ◽  
Bozena Turkiewicz ◽  
Maria Tomaszewska ◽  
Nikodem Chlubek
Keyword(s):  
Sunflower Oil ◽  
Lipolytic Activity ◽  
Hydrophobic Membrane ◽  
Hydrolysis Of

Continuous hydrolysis of olive oil by lipase in microporous hydrophobic membrane bioreactor

1985 ◽  
Vol 62 (6) ◽  
pp. 1016-1021 ◽  
Author(s):  
Mohammad Mozammel Hoq ◽  
Tsuneo Yamane ◽  
Shoichi Shimizu ◽  
Tadashi Funada ◽  
Shiro Ishida
Keyword(s):  
Olive Oil ◽  
Membrane Bioreactor ◽  
Hydrophobic Membrane ◽  
Hydrolysis Of

Preparation and properties of rennets from lamb's and kid's abomasa

1980 ◽  
Vol 47 (2) ◽  
pp. 221-230 ◽  
Author(s):  
Emmanuel Anifantakis ◽  
Margaret L. Green
Keyword(s):  
Milk Fat ◽  
Ph Value ◽  
Lipolytic Activity ◽  
Agar Gel ◽  
Milk Clotting ◽  
Ph Values ◽  
Cathepsin Activity ◽  
Maximum Stability ◽  
Hydrolysis Of ◽  
Gel Diffusion

SummaryLamb and kid rennets were prepared by extraction of dried abomasa with 6% (w/v) NaCl-2% (w/v) H3BO3 and activation of the proenzymes at pH 2·0. Each gave one zone of precipitation on casein-agar gel diffusion, enabling them to be differentiated from calf rennet and pig pepsin. After agarose gel electrophoresis, the proteinase activity of lamb rennet occurred in chymosin and pepsin bands only, whereas kid rennet contained an additional proteinase of intermediate mobility. Relative to their milk-clotting activities, lamb and kid rennets contained less pepsin and were less proteolytic on both haemoglobin at pH 1·8 and casein at pH 5·3 than calf rennet. The milk-clotting activities of lamb and kid rennets increased less with decrease in pH and were more stable to storage at both the pH value of maximum stability and lower pH values than that of calf rennet. Neither cathepsin activity nor lipolytic activity on milk fat was detected in any of the 3 rennets, but lamb rennet caused slight hydrolysis of tributyrin.

scholarly journals INVESTIGATION OF ENZYMATIC HYDROLYSIS OF FATTY WASTE PROCESSING OF SUNFLOWER SEEDS BY IMMOBILIZED LIPASE

2020 ◽  
Vol 20 (1) ◽  
pp. 5-11
Author(s):  
V. Skliar ◽  
G. Krusir ◽  
V. Zakharchuk
Keyword(s):  
Crop Production ◽  
Agricultural Sector ◽  
Lipolytic Activity ◽  
Immobilized Lipase ◽  
Immobilized Enzymes ◽  
Lipase Immobilization ◽  
Ph Optimum ◽  
Prolonged Incubation ◽  
Physical And Chemical ◽  
Hydrolysis Of

Ukraine has a developed agricultural sector, in particular crop production, which is a source of large quantities of production residues and waste. One of the most promising areas for solving environmental problems in the production of grain products is the processing of industrial waste by enzymes and the use of processing products in other industries. The current needs of sustainable environmental practices have increased the use of enzymatic technologies in production processes. Lipases be used in the processing of waste from oil and fat enterprises, namely, waste from the stage of demetallization of hydrogenated fat from vegetable oils by enzymatic hydrolysis.The work is devoted to the study of conditions of enzyme Rhizopus japonicus lipase immobilization and its physical and chemical characteristics. Factors for obtaining immobilized biocatalysts, methods and conditions for determining the activity and stability of immobilized enzymes are highlighted. Lipolytic activity of the enzyme immobilized under these conditions remains more than 30% compared to native, which is a high indicator of activity retention. It has been shown that immobilization promotes the expansion of the pH- and thermo-optimum of the lipase. It was determined that for the Rhizopus japonicus immobilized lipase, the pH optimum increased with a shift from 7.0 to 6.5, and there was an increase in pH stability during prolonged incubation of the immobilized enzyme for alkaline and acidic pH values. It has been established that lipase immobilization leads to expansion of the thermo-optimum, as well as stabilization of the enzyme during prolonged incubation at 40 ° C and at higher temperatures (+60-80 ° C), which are possible when drying the final product. The high activity and stability of the immobilized lipase make it possible to recommend it for biotechnological processing ofoil-fat waste.

scholarly journals Evolving a lipase for hydrolysis of natural triglycerides along with enhanced tolerance towards a protease and surfactants

2019 ◽  
Vol 32 (3) ◽  
pp. 129-143
Author(s):  
Ana L Alfaro-Chávez ◽  
Jian-Wei Liu ◽  
Bradley J Stevenson ◽  
Adrian Goldman ◽  
David L Ollis
Keyword(s):  
Olive Oil ◽  
Lipolytic Activity ◽  
Sodium Dodecyl ◽  
Wild Type Enzyme ◽  
Naturally Occurring ◽  
Low Concentrations ◽  
Secondary Screen ◽  
Enhanced Properties ◽  
Low Levels ◽  
Hydrolysis Of

Abstract In the accompanying paper, we described evolving a lipase to the point where variants were soluble, stable and capable of degrading C8 TAG and C8 esters. These variants were tested for their ability to survive in an environment that might be encountered in a washing machine. Unfortunately, they were inactivated both by treatment with a protease used in laundry detergents and by very low concentrations of sodium dodecyl sulfate (SDS). In addition, all the variants had very low levels of activity with triglycerides with long aliphatic chains and with naturally occurring oils, like olive oil. Directed evolution was used to select variants with enhanced properties. In the first 10 rounds of evolution, the primary screen was selected for variants capable of hydrolyzing olive oil whereas the secondary screen was selected for enhanced tolerance towards a protease and SDS. In the final six rounds of evolution, the primary and secondary screens identified variants that retained activity after treatment with SDS. Sixteen cycles of evolution gave variants with greatly enhanced lipolytic activity on substrates that had both long (C16 and C18) as well as short (C3 and C8) chains. We found variants that were stable for more than 3 hours in protease concentrations that rapidly degrade the wild-type enzyme. Enhanced tolerance towards SDS was found in variants that could break down naturally occurring lipid and resist protease attack. The amino acid changes that gave enhanced properties were concentrated in the cap domain responsible for substrate binding.

Purified postheparin plasma lipoprotein lipase in primary hyperlipoproteinemias

1975 ◽  
Vol 39 (6) ◽  
pp. 1022-1033 ◽  
Author(s):  
D. Ganesan ◽  
R. H. Bradford ◽  
G. Ganesan ◽  
W. J. McConathy ◽  
P. Alaupovic ◽  
...  
Keyword(s):  
Lipoprotein Lipase ◽  
Specific Activity ◽  
Lipolytic Activity ◽  
Plasma Lipoprotein ◽  
Type I ◽  
Activity Type ◽  
Type Iii ◽  
Protein Peak ◽  
Enzyme Specific Activity ◽  
Hydrolysis Of

Purified postheparin plasma lipoprotein lipase (LPL) of normolipidemic and primary hyperlipoproteinemic subjects was characterized by lipoprotein C polypeptide activation and specificity for triglycerides in chylomicrons and VLDL. Chromatography of normal LPL on Sephadex G-100 resulted in two protein peaks, LPLC-1 (activated by C-I but not C-II) and LPLC-II (activated by C-II but not C-I). LPL from type I hyperlipoproteinemic subjects was not activated by C-I and C-II activation was reduced to 40% of control. Hydrolysis of chylomicron and VLDL triglycerides was severely impaired. Although chromatography of type I LPL resulted in two protein peaks, the protein peak corresponding to LPLC-I did not exhibit lipolytic activity and LPLC-II was reduced to 50% of control in protein and enzyme specific activity. Type III LPL was normal in respect to LPLC-I while LPLC-II averaged 40% of control. Hydrolysis of chylomicron and VLDL was reduced to 50% and 10% of control, respectively. An etiological implication for LPLC-I and/or LPLC-II in type I and III hyperlipoproteinemias is suggested.

Bio-hydrogen Production By Enzymic Hydrolysis of Sunflower Oil Sludge

2015 ◽  
Vol 43 (11) ◽  
pp. 1547-1555
Author(s):  
Punniavan Sakthiselvan ◽  
Balakrishnan Naveena ◽  
Kannapan Panchamoorthy Gopinath ◽  
Nagarajan Partha
Keyword(s):  
Hydrogen Production ◽  
Sunflower Oil ◽  
Oil Sludge ◽  
Enzymic Hydrolysis ◽  
Hydrolysis Of

Continuous Flow Hydrolysis of Sunflower Oil for Biodiesel

2010 ◽  
Vol 32 (5) ◽  
pp. 460-468 ◽  
Author(s):  
R. Alenezi ◽  
M. Baig ◽  
J. Wang ◽  
R. Santos ◽  
G. A. Leeke
Keyword(s):  
Sunflower Oil ◽  
Continuous Flow ◽  
Hydrolysis Of
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