scholarly journals Comparative Studies on the Susceptibility of (R)-2,3-Dipalmitoyloxypropylphosphonocholine (DPPnC) and Its Phospholipid Analogues to the Hydrolysis or Ethanolysis Catalyzed by Selected Lipases and Phospholipases

Catalysts ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 129
Author(s):  
Paweł Mituła ◽  
Czesław Wawrzeńczyk ◽  
Witold Gładkowski
Keyword(s):  
Enzymatic Hydrolysis ◽  
Methylene Chloride ◽  
Reaction Rates ◽  
Bioactive Molecules ◽  
Porcine Pancreas ◽  
Chloride System ◽  
White Cabbage ◽  
Streptomyces Chromofuscus ◽  
Rate Of Hydrolysis ◽  
Bovine Pancreas

Susceptibility of soybean phosphatidylcholine, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and its phosphono analogue (R)-2,3-dipalmitoyloxypropylphosphonocholine (DPPnC) towards selected lipases and phospholipases was compared. The ethanolysis of substrates at sn-1 position was carried out by lipase from Mucor miehei (Lipozyme®) and lipase B from Candida antarctica (Novozym 435) in 95% ethanol at 30 °C, and the hydrolysis with LecitaseTM Ultra was carried out in hexane/water at 50 °C. Hydrolysis at sn-2 position was carried out in isooctane/Tris-HCl/AOT system at 40 °C using phospholipase A2 (PLA2) from porcine pancreas and PLA2 from bovine pancreas or 25 °C using PLA2 from bee venom. Hydrolysis in the polar part of the studied compounds was carried out at 30 °C in acetate buffer/ethyl acetate system using phospholipase D (PLD) from Streptococcus sp. and PLD from white cabbage or in Tris-HCl buffer/methylene chloride system at 35 °C using PLD from Streptomyces chromofuscus. The results showed that the presence of C-P bond between glycerol and phosphoric acid residue in DPPnC increases the rate of enzymatic hydrolysis or ethanolysis of ester bonds at the sn-1 and sn-2 position and decreases the rate of hydrolysis in the polar head of the molecule. The most significant changes in the reaction rates were observed for reaction with PLD from Streptococcus sp. and PLD from Streptomyces chromofuscus that hydrolyzed DPPnC approximately two times slower than DPPC and soybean PC. The lower susceptibility of DPPnC towards enzymatic hydrolysis by phospholipases D gives hope for the possibility of using DPPnC-like phosphonolipids as the carriers of bioactive molecules that, instead of choline, can be bounded with diacylpropylphosphonic acids (DPPnA).

scholarly journals Design of a New Gemini Lipoaminoacid with Immobilized Lipases Based on an Eco-Friendly Biosynthetic Process

Catalysts ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 164
Author(s):  
Patrícia M. Carvalho ◽  
Rita C. Guedes ◽  
Maria R. Bronze ◽  
Célia M. C. Faustino ◽  
Maria H. L. Ribeiro
Keyword(s):  
High Performance ◽  
Transfection Efficiency ◽  
Sol Gel ◽  
Reaction Rates ◽  
Solvent Free ◽  
Bioactive Molecules ◽  
Thermomyces Lanuginosus ◽  
Chemical Production ◽  
Immobilized Lipases ◽  
Free Media

Lipoaminoacids (LAA) are an important group of biosurfactants, formed by a polar hydrophilic part (amino acid) and a hydrophobic tail (lipid). The gemini LAA structures allow the formation of a supramolecular complex with bioactive molecules, like DNA, which provides them with good transfection efficiency. Since lipases are naturally involved in lipid and protein metabolism, they are an alternative to the chemical production of LAA, offering an eco-friendly biosynthetic process option. This work aimed to design the production of novel cystine derived gemini through a bioconversion system using immobilized lipases. Three lipases were used: porcine pancreatic lipase (PPL); lipase from Thermomyces lanuginosus (TLL); and lipase from Rizhomucor miehei (RML). PPL was immobilized in sol-gel lenses. L-cystine dihydrochloride and dodecylamine were used as substrates for the bioreaction. The production of LAA was evaluated by thin layer chromatography (TLC), and colorimetric reaction with eosin. The identification and quantification was carried out by High Performance Liquid Chromatographer-Mass Spectrometry (HPLC-MS/MS). The optimization of media design included co-solvent (methanol, dimethylsulfoxide), biphasic (n-hexane and 2-propanol) or solvent-free media, in order to improve the biocatalytic reaction rates and yields. Moreover, a new medium was tested where dodecylamine was melted and added to the cystine and to the biocatalyst, building a system of mainly undissolved substrates, leading to 5 mg/mL of LAA. Most of the volume turned into foam, which indicated the production of the biosurfactant. For the first time, the gemini derived cystine lipoaminoacid was produced, identified, and quantified in both co-solvent and solvent-free media, with the lipases PPL, RML, and TLL.

scholarly journals Determination of Surface Accessibility of the Cellulose Substrate According to Enzyme Sorption

Polymers ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 1201 ◽  
Author(s):  
Ekaterina M. Podgorbunskikh ◽  
Aleksey L. Bychkov ◽  
Oleg I. Lomovsky
Keyword(s):  
Enzymatic Hydrolysis ◽  
Mechanical Activation ◽  
Surface Area ◽  
Initial Rate ◽  
Plant Biomass ◽  
Inorganic Compounds ◽  
Cellulolytic Enzymes ◽  
Surface Accessibility ◽  
Cellulose Substrate ◽  
Rate Of Hydrolysis

As a heterogeneous process, enzymatic hydrolysis depends on the contact area between enzymes and the cellulose substrate. The surface area of a substrate is typically evaluated through the sorption of gases (nitrogen, argon, or water vapor) or sorption of high-molecular-weight pigments or proteins. However, lignocellulosic biomass uninvolved in the reaction because of inefficient binding or even the complete inhibition of the enzymes on the surface consisting of lignin or inorganic compounds is erroneously taken into account under these conditions. The initial rate of enzymatic hydrolysis will directly depend on the number of enzymes efficiently sorbed onto cellulose. In this study, the sorption of cellulolytic enzymes was used to evaluate the surface accessibility of the cellulose substrate and its changes during mechanical pretreatment. It was demonstrated that for pure cellulose, mechanical activation did not alter the chemical composition of the surface and the initial rate of hydrolysis increased, which was inconsistent with the data on the thermal desorption of nitrogen. New active cellulose sorption sites were shown to be formed upon. the mechanical activation of plant biomass (wheat straw), and the ultimate initial rate of hydrolysis corresponding to saturation of the accessible surface area with enzyme molecules was determined.

KINETICS OF THE ENZYMATIC HYDROLYSIS OF SARIN

1956 ◽  
Vol 34 (1) ◽  
pp. 80-82 ◽  
Author(s):  
P. A. Adie ◽  
F. C. G. Hoskin ◽  
G. S. Trick
Keyword(s):  
Enzymatic Hydrolysis ◽  
Reaction Rates ◽  
Order Reaction ◽  
First Order Reaction ◽  
Optical Isomers ◽  
First Order ◽  
Kinetics Of ◽  
Hydrolysis Of

The enzymatic hydrolysis of sarin is apparently a single first-order reaction. There is no evidence of different reaction rates for the two possible optical isomers of sarin. During both the enzymatic and the non-enzymatic hydrolyses, sarin appears to be detoxified somewhat more rapidly than the manometric results would indicate. However, the detoxification parallels the manometric results sufficiently to stand in contrast to results obtained using tabun.

THE HYDROLYSIS OF ACID AMIDES IN CONCENTRATED HYDROCHLORIC ACID SOLUTIONS

1942 ◽  
Vol 20b (5) ◽  
pp. 73-81 ◽  
Author(s):  
B. S. Rabinovitch ◽  
C. A. Winkler
Keyword(s):  
Activation Energy ◽  
Hydrochloric Acid ◽  
Acid Concentration ◽  
Reaction Rates ◽  
Activation Energies ◽  
Acid Solutions ◽  
Hydrochloric Acid Solutions ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

The Arrhenius constants have been evaluated for the hydrolysis of formamide, acetamide, propionamide, and benzamide in hydrochloric acid solutions over the concentration range 1 to 10 N. There is approximate correspondence between reaction rates and activation energies for the series of amides. An increase in observed activation energy with increasing acid concentration was found for all amides. The maximum in rate of hydrolysis, which occurs at higher acid concentrations, is discussed and accounted for by the variation in the Arrhenius constants with acid concentration.

Characteristics of Aerobacter beta-lactamase

1968 ◽  
Vol 14 (2) ◽  
pp. 139-145 ◽  
Author(s):  
M. Goldner ◽  
D. G. Glass ◽  
P. C. Fleming
Keyword(s):  
Reaction Rates ◽  
Penicillin G ◽  
Cephalosporin C ◽  
Beta Lactamase ◽  
Beta Lactam ◽  
Lactam Ring ◽  
Rate Of Hydrolysis ◽  
High Concentrations ◽  
Hydrolysis Of ◽  
Pseudomonas Pyocyanea

In this investigation, Aerobacter cloacae is shown to inactivate cephalosporin by hydrolysis of its beta-lactam ring. This was demonstrated by iodine absorption and infrared absorption spectra.The values of the Michaelis constant obtained with cephalosporin C and deacetyl cephalosporin C indicate a great affinity of the Aerobacter's beta-lactamase for its substrate. The enzyme was most active at pH 7.0 and 37 C. Aqueous washings of the Aerobacter cells were a potent source of enzyme.The beta-lactamase of A. cloacae was active on both cephalosporin and penicillin. A higher rate of hydrolysis was observed with cephalosporin C and deacetyl cephalosporin C than with cephalothin and cephaloridine. The ratio of reaction rates on cephalosporin C to that on penicillin G was consistently of the order of 100 to 1. The activity on V, N, and especially the semisynthetic penicillins was also low.The A. cloacae enzyme was easily demonstrable in large amount without added inducer. By contrast, the activity of the beta-lactamase from Pseudomonas pyocyanea cannot be detected unless high concentrations of inducer are used.

Viscosimetric analysis of solvent quality in a cellulose triacetate-methylene chloride system

1976 ◽  
Vol 18 (11) ◽  
pp. 2854-2860 ◽  
Author(s):  
I.I. Ryskina ◽  
V.P. Lozgacheva ◽  
E.D. Pokhvalenskii ◽  
V.M. Averyanova
Keyword(s):  
Methylene Chloride ◽  
Cellulose Triacetate ◽  
Chloride System ◽  
Solvent Quality

KINETICS OF THE ENZYMATIC HYDROLYSIS OF SARIN

1956 ◽  
Vol 34 (1) ◽  
pp. 80-82 ◽  
Author(s):  
P. A. Adie ◽  
F. C. G. Hoskin ◽  
G. S. Trick
Keyword(s):  
Enzymatic Hydrolysis ◽  
Reaction Rates ◽  
Order Reaction ◽  
First Order Reaction ◽  
Optical Isomers ◽  
First Order ◽  
Kinetics Of ◽  
Hydrolysis Of

The enzymatic hydrolysis of sarin is apparently a single first-order reaction. There is no evidence of different reaction rates for the two possible optical isomers of sarin. During both the enzymatic and the non-enzymatic hydrolyses, sarin appears to be detoxified somewhat more rapidly than the manometric results would indicate. However, the detoxification parallels the manometric results sufficiently to stand in contrast to results obtained using tabun.

Glucosinolates and Derived Products in Cruciferous Vegetables: Total Glucosinolates by Retention on Anion Exchange Resin and Enzymatic Hydrolysis to Measure Released Glucose

1977 ◽  
Vol 60 (4) ◽  
pp. 946-949 ◽  
Author(s):  
Cecil H VanEtten ◽  
Melvin E Daxenbichler
Keyword(s):  
Liquid Chromatography ◽  
Enzymatic Hydrolysis ◽  
Anion Exchange ◽  
Coefficient Of Variation ◽  
Methylene Chloride ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Gas Liquid Chromatography ◽  
Other Substances ◽  
Hydrolysis Of

Abstract Details are given for determining total glucoginolates in Cruciferae plants by a procedure measuring released glucose. The glucosinolates are separated from about 90% of other material in the plant extract by adsorption on an anion exchange resin. Then, by a selective thioglucosidase hydrolysis of the glucosinolates retained on the exchange resin, the glucose and aglucons are separated from other substances retained by the resin. Glucose is released into an aqueous medium and is equivalent to the total glucosinolates. The aglucons formed by the hydrolysis are extracted into methylene chloride and determined by gas-liquid chromatography. Based on 29 determinations of the glucose from sinigrin, analyzed under different conditions, accuracy of the total glucosinolate determination was 94.8 ± 7.3%. The coefficient of variation, determined by duplicate analyses on extracts from 58 cabbage samples, was 4.6%.

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