Immobilized enzymatic biocatalysts and their application for destruction of organophosphorus compounds in water, soil and air systems

2020 ◽  
pp. 340-360
Author(s):  
Olga Maslova ◽  
Elena Efremenko ◽  
Il'ya Lyagin ◽  
Ol'ga Sen'ko ◽  
Aslanli Aslanli
Keyword(s):  
Organophosphorus Compounds ◽  
Immobilized Enzymes ◽  
Methylphosphonic Acid ◽  
Biological Products ◽  
Diisopropyl Fluorophosphate ◽  
Natural Objects ◽  
Immobilization Of Enzymes

Undecomposed residues of organophosphorus compounds (OPC) after treatment with pesticides of plants or animals often fall into natural objects (water, soil and air). Modern approaches to the immobilization of enzymes allowing obtaining of stable biological products are described, as well as the possible using of immobilized enzymes for the decomposition of different OPC: paraoxone, methyl and ethyl paraoxone, coumaphos, parathion, methyl and ethyl parathion, chlorpyrifos, soman, VX, methylphosphonic acid and its isobutyl and diisobutyl ethers, diisopropyl fluorophosphate.

Enzymes and Their Forms Used in Detection of Organophosphorus Compounds

2021 ◽  
pp. 22-41
Keyword(s):  
Organophosphorus Compounds ◽  
Degradation Products ◽  
Rapid Development ◽  
Hydrolytic Enzymes ◽  
Immobilized Enzymes ◽  
Amino Acid Sequences ◽  
Practical Implementation ◽  
Scientific Results ◽  
Physical And Chemical

Еnzymes are able to effectively interact with various organophosphorus compounds (OPC), entering into (bio)chemical reactions with them. Changes in the initial activity of enzymes as a result of their inhibition by OPC, the formation of OPC degradation products under the action of hydrolytic enzymes, etc. can be determined using different physical and chemical methods and used in bioanalytic systems to determine the concentrations of OPC. The purpose of the review is to analyze the main scientific results achieved over the past 10 years in the development of analytical systems based on enzymes intended for the determination of OPC. It is shown in the article, that the requirements for the sensitivity of biosensors are based on the norms of the content of the analyzed substances detected in/at the objects of mandatory control. The cholinesterases compose a basis for the development of the largest number of ultra-sensitive biosensors, although other enzymes can be successfully used as a biosensitive element. The most technologically advanced solution that is close to the practical implementation seems to be bioanalytical systems using immobilized enzymes. Improving the detection limits of the OPC can be achieved by using nanoobjects together with modern methods of signal transducers, for example, with nanomechanical detectors and signal converters. This combination of technical solutions ensures the sensitivity of the OPC analysis up to pg/l. At present, «reagentless» systems have received significant development, which have become the basis for the production of a large number of commercially available strips for the express determination of OPC. Modern demands stimulate the rapid development of portable and, especially, wearable biosensors that can be attached to various surfaces, including a clothing. The progress in the development of affine amino acid sequences, in the future, will allow the creation of enzyme biosensors on any surface.

Immobilization of enzymes on alumina by means of pyridoxal 5′-phosphate

1988 ◽  
Vol 8 (3) ◽  
pp. 263-269 ◽  
Author(s):  
M. Pugnière ◽  
C. San Juan ◽  
M-A. Coletti-Previero ◽  
A. Previero
Keyword(s):  
Molecular Weight ◽  
Physical Properties ◽  
High Activity ◽  
Immobilized Enzymes ◽  
Second Step ◽  
Low Molecular Weight ◽  
Step Procedure ◽  
Immobilization Of Enzymes

A number of proteases have been immobilized on alumina in a two-step procedure: the first step converted them into semisynthetic phosphoproteins which, in the second step, spontaneously bonded to alumina through their phosphate function. The immobilized enzymes thus obtained showed the physical properties typical of the inorganic carrier and a high activity on low molecular weight substrates.

scholarly journals Magnetic Nanoparticle-Containing Supports as Carriers of Immobilized Enzymes: Key Factors Influencing the Biocatalyst Performance

Nanomaterials ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 2257
Author(s):  
Valentina G. Matveeva ◽  
Lyudmila M. Bronstein
Keyword(s):  
Protective Layer ◽  
Immobilized Enzymes ◽  
Short Review ◽  
Key Factors ◽  
Magnetic Attraction ◽  
Hierarchical Porous ◽  
Close Proximity ◽  
Immobilization Of Enzymes ◽  
Enzyme Molecules ◽  
Biocatalytic Process

In this short review (Perspective), we identify key features of the performance of biocatalysts developed by the immobilization of enzymes on the supports containing magnetic nanoparticles (NPs), analyzing the scientific literature for the last five years. A clear advantage of magnetic supports is their easy separation due to the magnetic attraction between magnetic NPs and an external magnetic field, facilitating the biocatalyst reuse. This allows for savings of materials and energy in the biocatalytic process. Commonly, magnetic NPs are isolated from enzymes either by polymers, silica, or some other protective layer. However, in those cases when iron oxide NPs are in close proximity to the enzyme, the biocatalyst may display a fascinating behavior, allowing for synergy of the performance due to the enzyme-like properties shown in iron oxides. Another important parameter which is discussed in this review is the magnetic support porosity, especially in hierarchical porous supports. In the case of comparatively large pores, which can freely accommodate enzyme molecules without jeopardizing their conformation, the enzyme surface ordering may create an optimal crowding on the support, enhancing the biocatalytic performance. Other factors such as surface-modifying agents or special enzyme reactor designs can be also influential in the performance of magnetic NP based immobilized enzymes.

Large scale applications of immobilized enzymes call for sustainable and inexpensive solutions: rice husks as renewable alternatives to fossil-based organic resins

RSC Advances ◽  
2016 ◽  
Vol 6 (68) ◽  
pp. 63256-63270 ◽  
Author(s):  
L. Corici ◽  
V. Ferrario ◽  
A. Pellis ◽  
C. Ebert ◽  
S. Lotteria ◽  
...  
Keyword(s):  
Rice Husk ◽  
Large Scale ◽  
Immobilized Enzymes ◽  
Covalent Immobilization ◽  
Rice Husks ◽  
Immobilization Of Enzymes

Rice husk for physical and covalent immobilization of enzymes: a sustainable and economic alternative to fossil-based organic resins.

scholarly journals An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes

2015 ◽  
Vol 29 (2) ◽  
pp. 205-220 ◽  
Author(s):  
Nur Royhaila Mohamad ◽  
Nur Haziqah Che Marzuki ◽  
Nor Aziah Buang ◽  
Fahrul Huyop ◽  
Roswanira Abdul Wahab
Keyword(s):  
Surface Analysis ◽  
Immobilized Enzymes ◽  
Analysis Techniques ◽  
Surface Analysis Techniques ◽  
Immobilization Of Enzymes

Short-term Clinical and Neuropathologic Effects of Cholinesterase Inhibitors in Rats

1993 ◽  
Vol 12 (1) ◽  
pp. 55-68 ◽  
Author(s):  
Marion Ehrich ◽  
Linda Shell ◽  
Michael Rozum ◽  
B. S. Jortner
Keyword(s):  
Cholinesterase Inhibitors ◽  
Organophosphorus Compounds ◽  
Myelinated Fiber ◽  
Dependent Manner ◽  
Short Term ◽  
Diisopropyl Fluorophosphate ◽  
Neurotoxic Effects ◽  
High Doses ◽  
Dose Dependent ◽  
Neurotoxic Esterase

Adult male Long Evans rats were given a single administration of 3 dosage levels of the organophosphorus compounds tri-ortho-tolyl phosphate (TOTP), diisopropyl fluorophosphate (DFP), phenyl saligenin phosphate (PSP), mipafox, malathion, and dichlorvos or the carbamate carbaryl. Acetylcholinesterase and neurotoxic esterase activities were inhibited in a dose-dependent manner, with the highest dosages of all of these compounds inhibiting activities of these enzymes in brain by at least 37% and 64%, respectively, at 4 and 48 hours after administration. Rats given the high doses of TOTP (1000 mg/kg), DFP (3 mg/kg), malathion (2000 mg/kg), and carbaryl (160 mg/kg) weighed significantly less than control rats 14 days after administration. A functional observational battery (FOB) was used to screen for neurotoxic effects 1, 2, and 3 weeks after exposure. All 7 test compounds were capable of causing changes in parameters indicative of behavioral and central nervous system excitability. In addition, dose-related alterations in response to approach were seen in rats given DFP, malathion, dichlorvos, and carbaryl. Mild to moderate myelinated fiber degeneration was seen in the rostral levels of the fasciculus gracilis in rats given TOTP, DFP, PSP and mipafox, but no significant neuropathologic lesions were noted in rats given dichlorvos, malathion, or carbaryl.

Main steps of developing chemical organophosphorus agents abroad

2020 ◽  
pp. 17-34
Author(s):  
Alexander Zlobin ◽  
Valeriy Inozemcev ◽  
Sergey Komissarenko ◽  
Igor Medveckiy ◽  
Igor Nelga ◽  
...  
Keyword(s):  
World War Ii ◽  
Great Britain ◽  
Organophosphorus Compounds ◽  
Nobel Laureate ◽  
Chemical Weapons ◽  
World War ◽  
Diisopropyl Fluorophosphate ◽  
Wide Range ◽  
Warfare Agents ◽  
The Usa

Organophosphorus compounds (OPC) occupy a special place among chemical warfare agents (CWA). High level of toxicity, a wide range of physicochemical properties, polyapplication of action already in the 1930s attracted the close attention of foreign military experts. In 1936, the German chemist Gerhard Schrader for the first time synthesized O-ethyl-dimethylamidocyanophosphate, known today as a herd. By the beginning of the Second World War, the staff of his laboratory synthesized over two thousand new OPC. Some of these compounds were selected for further study as CW agents and subsequently were adopted as weapons by the German army. In 1938 the same Gerhard Schrader have synthesized the organophosphorus compound, closed to tabun, but more toxic: O-isopropyl methyl fluorophosphate, called sarin. In 1944 the German chemist, the 1938 Nobel laureate in chemistry Richard Kuhn synthesized soman and revealed the damaging effect of organophosphorus CWA’s. In 1941 the British chemist Bernard Saunders synthesized diisopropyl fluorophosphate. During World War II the industrial production of organophosphorus CWA’s was organized in Germany, Great Britain and in the USA. Germany produced tabun, sarin and soman, the western allies: diisopropyl fluorophosphate. Till the end of World War II the leadership in the sphere of the development of nerve agents belonged to Nazi Germany. After the end of the war the German scientists, many of whom were devoted Nazis, continued their work under the auspices of military departments of the USA and Great Britain. Subsequently phosphorylated thiocholine esters: V-series substances (VG, VM, VR, VX, EA 3148, EA3317 agents etc.) were synthesized with their participation. The wide range of organophosphorus compounds was tested on volunteers in Porton Down (Great Britain) and in the Edgewood arsenal (USA). But after the synthesis of V-series agents the work on organophosphorus CWA’s did not stop. In recent years there appeared the tendency of the transformation of real threats connected with the chemical weapons use, to propaganda sphere. In recent years, there has been a tendency toward the transformation of real threats associated with the use of chemical weapons into provocation and an advocacy field, but this does not mean that the search for new CWA in Western countries has been stopped.

Fibrin Membrane Endowed With Biological Function: Immobilization Of Enzymes And Living Cells

1981 ◽  
Author(s):  
Y Inada ◽  
H Hagiwara ◽  
Y Saito ◽  
A Matsushima
Keyword(s):  
Biological Function ◽  
Urea Cycle ◽  
Glyoxylic Acid ◽  
Coagulation Factor ◽  
Immobilized Enzymes ◽  
Living Cells ◽  
Inorganic Pyrophosphatase ◽  
Multienzyme System ◽  
Immobilization Of Enzymes ◽  
Fibrin Membrane

Fibrin membrane formed from fibrinogen with thrombin and blood coagulation factor XIII was a superior matrix for preparing immobilized enzymes and living cells. Enzymes such as asparaginase, chloroplast ATPase or catalase and living cells such as Chlorella cells or sea urchin eggs were embedded in fibrin membrane without imparing their functions. The enzymes participating in degradation of purine bases(uric acid), uricase, allantoinase and allantoicase together with catalase were embedded simultaneously in matrices of fibrin molecules. The multienzyme complex thus prepared had an ability to degrade urate to glyoxylic acid and urea via allantoin and allantoic acid. Four enzymes in urea cycle, ornithine carbamoyltransferase, argininosuccinate synthetase, argininosuccinate lyase and orginase together with inorganic pyrophosphatase, were immobilized into matrices of fibrin molecules. The immobilized multienzyme system not only had an ability to carry out urea cycle continuously at least over several hours, but also had a greately improved efficiency over the corresponding soluble system. To the best of our knowledge this is the first report to show an immobilization of efficient cyclic enzyme system.

Preparation of p-aminobenzyl cellulose and its utilization for immobilization of enzymes

1980 ◽  
Vol 45 (10) ◽  
pp. 2847-2854 ◽  
Author(s):  
Peter Gemeiner ◽  
Ľudovít Kuniak ◽  
Jiří Zemek
Keyword(s):  
Immobilized Enzymes ◽  
The Other ◽  
Carboxyl Groups ◽  
Cross Linking ◽  
Side Reactions ◽  
Reaction Conditions ◽  
Other Hand ◽  
Immobilization Of Enzymes ◽  
Molecular Substrates

The O-alkylation of non cross-linked celluloses with p-nitrobenzyl chloride according to Campbell does not afford satisfying results (alkylation degree Da ⪬ 0.025). On the other hand, the use of cross-linked celluloses makes it possible to prepare p-nitrobenzyl cellulose under substantially milder reaction conditions (Da ⪬ 0.42); the degree of cross linking of cellulose considerably affected the Da of p-nitrobenzyl cellulose. The same also holds for O-alkylation of cross-linked celluloses with p-nitrobenzyl chloride according to Hakomori. Reduction of p-nitrobenzyl cellulose with dithionite is considerably associated with side reactions in which sulfur became embodied, whereas reduction with titanous chloride resulted in noticeable losses of p-nitrobenzyl groups. p-Aminobenzyl cellulose is, after activation with carboxyl groups, a suitable carrier for immobilization of enzymes as acetylcholinesterase, glucoamylase and α-amylase. The respective immobilized enzymes retained relatively high relative activities, in the last two cases also for high-molecular substrates.

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