HYDROLYSIS OF LECITHIN BY PLANT PLASTID ENZYMES

1955 ◽  
Vol 33 (1) ◽  
pp. 575-589 ◽  
Author(s):  
Morris Kates
Keyword(s):  
Phosphatidic Acid ◽  
Inorganic Phosphate ◽  
Organic Phosphate ◽  
Water Soluble ◽  
Lag Phase ◽  
Carrot Root ◽  
First Order ◽  
Spinach Chloroplasts ◽  
Egg Lecithin ◽  
Hydrolysis Of

Enzymatic liberation of choline from egg lecithin by plastid fractions from sugar beet, spinach, and cabbage leaves and from carrot root was a rapid, first order reaction (up to 70% hydrolysis), and was not preceded by a lag phase. None of the choline-containing products of lecithin degradation (lysolecithin, glycerylphosphorylcholine, or phosphorylcholine) lost choline on incubation with spinach chloroplasts. Inorganic phosphate liberation from lecithin by the plastids was preceded by a lag phase and was much slower than choline liberation. Spinach chloroplasts catalyzed the liberation of inorganic phosphate from L-α-phosphatidic acid and from L-α-glycerophosphate. The water-soluble organic phosphate liberated from lecithin by spinach chloroplasts was identified chromatographically as phosphorylcholine. The ether-soluble organic phosphate produced during the hydrolysis of egg lecithin by carrot plastids was isolated and identified as L-α-phosphatidic acid. These observations suggest that the enzymatic hydrolysis of lecithin by plant plastids involves the following reactions: (1) lecithin → L-α-phosphatidic acid + choline; (2) L-α-phosphatidic acid → inorganic phosphate + diglyceride and/or (3) L-α-phosphatidic acid → glycerophosphate + fatty acids and (4) glycerophosphate → inorganic phosphate + glycerol; and (5) lecithin → phosphorylcholine + diglyceride. The L-α-structure for egg lecithin was confirmed.

HYDROLYSIS OF LECITHIN BY PLANT PLASTID ENZYMES

1955 ◽  
Vol 33 (4) ◽  
pp. 575-589 ◽  
Author(s):  
Morris Kates
Keyword(s):  
Phosphatidic Acid ◽  
Inorganic Phosphate ◽  
Organic Phosphate ◽  
Water Soluble ◽  
Lag Phase ◽  
Carrot Root ◽  
First Order ◽  
Spinach Chloroplasts ◽  
Egg Lecithin ◽  
Hydrolysis Of

Enzymatic liberation of choline from egg lecithin by plastid fractions from sugar beet, spinach, and cabbage leaves and from carrot root was a rapid, first order reaction (up to 70% hydrolysis), and was not preceded by a lag phase. None of the choline-containing products of lecithin degradation (lysolecithin, glycerylphosphorylcholine, or phosphorylcholine) lost choline on incubation with spinach chloroplasts. Inorganic phosphate liberation from lecithin by the plastids was preceded by a lag phase and was much slower than choline liberation. Spinach chloroplasts catalyzed the liberation of inorganic phosphate from L-α-phosphatidic acid and from L-α-glycerophosphate. The water-soluble organic phosphate liberated from lecithin by spinach chloroplasts was identified chromatographically as phosphorylcholine. The ether-soluble organic phosphate produced during the hydrolysis of egg lecithin by carrot plastids was isolated and identified as L-α-phosphatidic acid. These observations suggest that the enzymatic hydrolysis of lecithin by plant plastids involves the following reactions: (1) lecithin → L-α-phosphatidic acid + choline; (2) L-α-phosphatidic acid → inorganic phosphate + diglyceride and/or (3) L-α-phosphatidic acid → glycerophosphate + fatty acids and (4) glycerophosphate → inorganic phosphate + glycerol; and (5) lecithin → phosphorylcholine + diglyceride. The L-α-structure for egg lecithin was confirmed.

PHOSPHORYLATION OF DIGLYCERIDES BY RAT BRAIN

1962 ◽  
Vol 40 (2) ◽  
pp. 247-259 ◽  
Author(s):  
K. P. Strickland
Keyword(s):  
Phosphatidic Acid ◽  
Rat Brain ◽  
Inorganic Phosphate ◽  
Specific Activity ◽  
Alkaline Treatment ◽  
Water Soluble ◽  
Two Dimensional ◽  
Relative Specific Activity ◽  
Hydrolysis Products ◽  
Stimulation Of

The addition of D-α,β-dimyristin was observed to stimulate by three to six times the labelling of phospholipids from radioactive inorganic phosphate (Pi32) by glycolysing homogenates and respiring mitochondria of rat brain. The increase in labelling was confined to the glycerophosphate (GP) isolated by two-dimensional chromatography from the water-soluble hydrolysis products obtained on weak alkaline treatment of the labelled phospholipids. The GP formed under these conditions is presumed to be derived mainly from phosphatidic acid formed by the phosphorylation of the diglyceride. A similar effect was observed for D-α,β-dipalmitin, D-α,β-diolein, and natural diglycerides prepared from either egg lecithin or spinal cord lecithin, but not for D-α-β-distearin. L-α,β-Diolein was much less effective than the D-isomer, suggesting a stereospecificity on the part of the enzymic phosphorylation of diglyceride. Experiments on the effects of the omission of Mg++ and the addition of glycolytic inhibitors on the stimulation of the labelling from Pi32 caused by D-α,β-dimyristin and D-α,β-diolein in the anaerobic homogenate system suggested that the increased phosphorylation caused by added diglycerides was closely coupled to active glycolysis. A comparison of the relative specific activity of the lipid P, following incubation of Pi32 and ATP32 in the anaerobic homogenate system inhibited by fluoride with and without D-α,β-diolein added, showed that the phosphate of the newly formed phosphatidic acid was derived from ATP, suggesting the presence of a D-α,β-diglyceride kinase.

THE NON-ENZYMATIC HYDROLYSIS OF ADENOSINE DIPHOSPHATE

1957 ◽  
Vol 35 (12) ◽  
pp. 1496-1503 ◽  
Author(s):  
K. A. Holbrook ◽  
Ludovic Ouellet
Keyword(s):  
Activation Energy ◽  
Aqueous Solution ◽  
Enzymatic Hydrolysis ◽  
Inorganic Phosphate ◽  
Adenosine Diphosphate ◽  
Hydrogen Ions ◽  
Kcal Mole ◽  
First Order ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of the non-enzymatic hydrolysis of adenosine diphosphate in aqueous solution have been studied at pH 3.5 to 10.5 and temperatures from 80° to 95 °C. The reaction has been followed by measuring colorimetrically the inorganic phosphate liberated according to the over-all reaction[Formula: see text]The reaction has been found to be first order with respect to ADP concentration and to be catalyzed by hydrogen ions. From rate studies at pH 8.0 an activation energy of 24.2 kcal./mole was derived. A mechanism is proposed to account for the observed facts and the mechanism for the hydrolysis of adenosine triphosphate is also discussed.

LECITHINASE SYSTEMS IN SUGAR BEET, SPINACH, CABBAGE, AND CARROT

1954 ◽  
Vol 32 (1) ◽  
pp. 571-583 ◽  
Author(s):  
Morris Kates
Keyword(s):  
Sugar Beet ◽  
High Speed ◽  
Thermal Inactivation ◽  
Enzyme Concentration ◽  
Organic Phosphate ◽  
Water Soluble ◽  
Optimum Conditions ◽  
Carrot Root ◽  
Enzyme Systems ◽  
Influence Of Ph

Lecithinase activity of aqueous extracts of sugar beet, spinach, or cabbage leaves, and of carrot root was found to be associated entirely with the plastid fractions, separated by high-speed centrifugation. The supernatant cell sap–cytoplasm fractions were not only inactive but actually inhibitory. The rate of enzymatic liberation of choline from lecithin by all plastid fractions was found to be greatly increased by saturation with diethyl ether. The influence of pH, enzyme concentration, substrate concentration, and temperature on the rate of ether-activated choline liberation was studied and optimum conditions for the reaction were determined. Under optimum conditions, liberation of choline from lecithin by each of the plastid fractions was rapid and was accompanied by a much slower liberation of inorganic and water-soluble organic phosphate; liberation of phosphates was much greater with spinach than with the other species. Thermal inactivation and fluoride inhibition of the enzyme systems were also studied.

LECITHINASE SYSTEMS IN SUGAR BEET, SPINACH, CABBAGE, AND CARROT

1954 ◽  
Vol 32 (5) ◽  
pp. 571-583 ◽  
Author(s):  
Morris Kates
Keyword(s):  
Sugar Beet ◽  
High Speed ◽  
Thermal Inactivation ◽  
Enzyme Concentration ◽  
Organic Phosphate ◽  
Water Soluble ◽  
Optimum Conditions ◽  
Carrot Root ◽  
Enzyme Systems ◽  
Influence Of Ph

Lecithinase activity of aqueous extracts of sugar beet, spinach, or cabbage leaves, and of carrot root was found to be associated entirely with the plastid fractions, separated by high-speed centrifugation. The supernatant cell sap–cytoplasm fractions were not only inactive but actually inhibitory. The rate of enzymatic liberation of choline from lecithin by all plastid fractions was found to be greatly increased by saturation with diethyl ether. The influence of pH, enzyme concentration, substrate concentration, and temperature on the rate of ether-activated choline liberation was studied and optimum conditions for the reaction were determined. Under optimum conditions, liberation of choline from lecithin by each of the plastid fractions was rapid and was accompanied by a much slower liberation of inorganic and water-soluble organic phosphate; liberation of phosphates was much greater with spinach than with the other species. Thermal inactivation and fluoride inhibition of the enzyme systems were also studied.

PHOSPHORYLATION OF DIGLYCERIDES BY RAT BRAIN

1962 ◽  
Vol 40 (1) ◽  
pp. 247-259 ◽  
Author(s):  
K. P. Strickland
Keyword(s):  
Phosphatidic Acid ◽  
Rat Brain ◽  
Inorganic Phosphate ◽  
Specific Activity ◽  
Alkaline Treatment ◽  
Water Soluble ◽  
Two Dimensional ◽  
Relative Specific Activity ◽  
Hydrolysis Products ◽  
Stimulation Of

The addition of D-α,β-dimyristin was observed to stimulate by three to six times the labelling of phospholipids from radioactive inorganic phosphate (Pi32) by glycolysing homogenates and respiring mitochondria of rat brain. The increase in labelling was confined to the glycerophosphate (GP) isolated by two-dimensional chromatography from the water-soluble hydrolysis products obtained on weak alkaline treatment of the labelled phospholipids. The GP formed under these conditions is presumed to be derived mainly from phosphatidic acid formed by the phosphorylation of the diglyceride. A similar effect was observed for D-α,β-dipalmitin, D-α,β-diolein, and natural diglycerides prepared from either egg lecithin or spinal cord lecithin, but not for D-α-β-distearin. L-α,β-Diolein was much less effective than the D-isomer, suggesting a stereospecificity on the part of the enzymic phosphorylation of diglyceride. Experiments on the effects of the omission of Mg++ and the addition of glycolytic inhibitors on the stimulation of the labelling from Pi32 caused by D-α,β-dimyristin and D-α,β-diolein in the anaerobic homogenate system suggested that the increased phosphorylation caused by added diglycerides was closely coupled to active glycolysis. A comparison of the relative specific activity of the lipid P, following incubation of Pi32 and ATP32 in the anaerobic homogenate system inhibited by fluoride with and without D-α,β-diolein added, showed that the phosphate of the newly formed phosphatidic acid was derived from ATP, suggesting the presence of a D-α,β-diglyceride kinase.

The effect of polymeric and model imidazolium halides on the rate of hydrolysis of 4-acetoxy-3-nitrobenzoic acid

1985 ◽  
Vol 50 (4) ◽  
pp. 845-853 ◽  
Author(s):  
Miloslav Šorm ◽  
Miloslav Procházka ◽  
Jaroslav Kálal
Keyword(s):  
Catalyst Concentration ◽  
Low Molecular Weight ◽  
Imidazolium Chloride ◽  
First Order ◽  
Nitrobenzoic Acid ◽  
Rate Of Hydrolysis ◽  
Acid Catalyzed ◽  
Hydrolysis Of ◽  
Ethanol In Water ◽  
Direct Attack

The course of hydrolysis of an ester, 4-acetoxy-3-nitrobenzoic acid catalyzed with poly(1-methyl-3-allylimidazolium bromide) (IIa), poly[l-methyl-3-(2-propinyl)imidazolium chloride] (IIb) and poly[l-methyl-3-(2-methacryloyloxyethyl)imidazolium bromide] (IIc) in a 28.5% aqueous ethanol was investigated as a function of pH and compared with low-molecular weight models, viz., l-methyl-3-alkylimidazolium bromides (the alkyl group being methyl, propyl, and hexyl, resp). Polymers IIb, IIc possessed a higher activity at pH above 9, while the models were more active at a lower pH with a maximum at pH 7.67. The catalytic activity at the higher pH is attributed to an attack by the OH- group, while at the lower pH it is assigned to a direct attack of water on the substrate. The rate of hydrolysis of 4-acetoxy-3-nitrobenzoic acid is proportional to the catalyst concentration [IIc] and proceeds as a first-order reaction. The hydrolysis depends on the composition of the solvent and was highest at 28.5% (vol.) of ethanol in water. The hydrolysis of a neutral ester, 4-nitrophenyl acetate, was not accelerated by IIc.

scholarly journals MW irradiation and ionic liquids as green tools in hydrolyses and alcoholyses

2020 ◽  
Vol 10 (1) ◽  
pp. 001-010 ◽  
Author(s):  
Nikoletta Harsági ◽  
Betti Szőllősi ◽  
Nóra Zsuzsa Kiss ◽  
György Keglevich
Keyword(s):  
Ionic Liquids ◽  
Alkaline Hydrolysis ◽  
Alkyl Group ◽  
Phosphinic Acid ◽  
Reaction Times ◽  
Alternative Possibility ◽  
First Order ◽  
Pseudo First Order ◽  
Mw Irradiation ◽  
Hydrolysis Of

Abstract The optimized HCl-catalyzed hydrolysis of alkyl diphenylphosphinates is described. The reaction times and pseudo-first-order rate constants suggested the iPr > Me > Et ∼ Pr ∼ Bu order of reactivity in respect of the alkyl group of the phosphinates. The MW-assisted p-toluenesulfonic acid (PTSA)-catalyzed variation means a better alternative possibility due to the shorter reaction times, and the alkaline hydrolysis is another option. The transesterification of alkyl diphenylphosphinates took place only in the presence of suitable ionic liquids, such as butyl-methylimidazolium hexafluorophosphorate ([bmim][PF6]) and butyl-methylimidazolium tetrafluoroborate ([bmim][BF4]). The application of ethyl-methylimidazolium hydrosulfate ([emim][HSO4]) and butyl-methylimidazolium chloride ([bmim][Cl]) was not too efficient, as the formation of the ester was accompanied by the fission of the O–C bond resulting in the formation of Ph2P(O)OH. This surprising transformation may be utilized in the phosphinate → phosphinic acid conversion.

scholarly journals Optimizing Chitin Depolymerization by Lysozyme to Long-Chain Oligosaccharides

Marine Drugs ◽  
2021 ◽  
Vol 19 (6) ◽  
pp. 320
Author(s):  
Arnaud Masselin ◽  
Antoine Rousseau ◽  
Stéphanie Pradeau ◽  
Laure Fort ◽  
Rodolphe Gueret ◽  
...  
Keyword(s):  
Time Course ◽  
Water Soluble ◽  
Organic Fertilizers ◽  
Symbiotic Associations ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Ecological Transition ◽  
Optimized Conditions ◽  
Hydrolysis Of ◽  
Long Chain

Chitin oligosaccharides (COs) hold high promise as organic fertilizers in the ongoing agro-ecological transition. Short- and long-chain COs can contribute to the establishment of symbiotic associations between plants and microorganisms, facilitating the uptake of soil nutrients by host plants. Long-chain COs trigger plant innate immunity. A fine investigation of these different signaling pathways requires improving the access to high-purity COs. Here, we used the response surface methodology to optimize the production of COs by enzymatic hydrolysis of water-soluble chitin (WSC) with hen egg-white lysozyme. The influence of WSC concentration, its acetylation degree, and the reaction time course were modelled using a Box–Behnken design. Under optimized conditions, water-soluble COs up to the nonasaccharide were formed in 51% yield and purified to homogeneity. This straightforward approach opens new avenues to determine the complex roles of COs in plants.

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