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.

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.

Stabilization of Immobilized Enzymes Against Water-Soluble Organic Cosolvents and Generation of Hyper-Hydrophilic Micro-Environments Surrounding Enzyme Molecules

2001 ◽  
Vol 19 (5-6) ◽  
pp. 489-503 ◽  
Author(s):  
O. Abian ◽  
C. Mateo ◽  
G. Fernández-Lorente ◽  
J. M. Palomo ◽  
R. Fernández-Lafuente ◽  
...  
Keyword(s):  
Immobilized Enzymes ◽  
Water Soluble ◽  
Organic Cosolvents ◽  
Enzyme Molecules

Brain glutaminases

2010 ◽  
Vol 1 (1) ◽  
pp. 3-15 ◽  
Author(s):  
Javier Márquez ◽  
Mercedes Martín-Rufián ◽  
Juan A. Segura ◽  
José M. Matés ◽  
José A. Campos-Sandoval ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Therapeutic Target ◽  
Short Review ◽  
Mammalian Brain ◽  
Key Factors ◽  
Differential Distribution ◽  
Potential Therapeutic Target ◽  
Glutaminase Activity ◽  
Hazardous Compounds

AbstractGlutaminase is considered as the main glutamate producer enzyme in brain. Consequently, the enzyme is essential for both glutamatergic and gabaergic transmissions. Glutamine-derived glutamate and ammonia, the products of glutaminase reaction, fulfill crucial roles in energy metabolism and in the biosynthesis of basic metabolites, such as GABA, proteins and glutathione. However, glutamate and ammonia are also hazardous compounds and danger lurks in their generation beyond normal physiological thresholds; hence, glutaminase activity must be carefully regulated in the mammalian brain. The differential distribution and regulation of glutaminase are key factors to modulate the metabolism of glutamate and glutamine in brain. The discovery of novel isoenzymes, protein interacting partners and subcellular localizations indicate new functions for brain glutaminase. In this short review, we summarize recent findings that point consistently towards glutaminase as a multifaceted protein able to perform different tasks. Finally, we will highlight the involvement of glutaminase in pathological states and its consideration as a potential therapeutic target.

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

scholarly journals Differences in the SNARE evolution of fungi and metazoa

2009 ◽  
Vol 37 (4) ◽  
pp. 787-791 ◽  
Author(s):  
Nickias Kienle ◽  
Tobias H. Kloepper ◽  
Dirk Fasshauer
Keyword(s):  
Eukaryotic Cell ◽  
Simple Explanation ◽  
Key Factors ◽  
Vertebrate Lineage ◽  
Helix Bundle ◽  
Protein Receptor ◽  
Close Proximity ◽  
History Of ◽  
Major Increase ◽  
Four Helix Bundle

Proteins of the SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor) family are key factors in all vesicle-fusion steps in the endocytic and secretory pathways. SNAREs can assemble into a tight four-helix bundle complex between opposing membranes, a process that is thought to pull the two membranes into close proximity. The complex-forming domains are highly conserved, not only between different species, but also between different vesicular trafficking steps. SNARE protein sequences can be classified into four main types (Qa, Qb, Qc and R), each reflecting their position in the four-helix bundle. Further refinement of these main types resulted in the identification of 20 distinct conserved groups, which probably reflect the original repertoire of a proto-eukaryotic cell. We analysed the evolution of the SNARE repertoires in metazoa and fungi and unveiled remarkable differences in both lineages. In metazoa, the SNARE repertoire appears to have undergone a substantial expansion, particularly in the endosomal pathways. This expansion probably occurred during the transition from a unicellular to a multicellular lifestyle. We also observed another expansion that led to a major increase of the secretory SNAREs in the vertebrate lineage. Interestingly, fungi developed multicellularity independently, but in contrast with plants and metazoa, this change was not accompanied by an expansion of the SNARE set. Our findings suggest that the rise of multicellularity is not generally linked to an expansion of the SNARE set. The structural and functional diversity that exists between fungi and metazoa might offer a simple explanation for the distinct evolutionary history of their SNARE repertoires.

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.

Manufacture, Wet and Dry Corrosion, and Plasma Nitridation of Novel Nanocrystalline Ni-Cr Nanoparticle Nanocomposites: A Brief Review

2008 ◽  
Vol 32 ◽  
pp. 17-20
Author(s):  
X. Peng
Keyword(s):  
Chromium Oxide ◽  
Hot Corrosion ◽  
Protective Layer ◽  
Short Review ◽  
Coarse Grained ◽  
Second Phase ◽  
Fast Diffusion ◽  
Nacl Solution ◽  
Plasma Nitridation ◽  
Conventional Alloy

The paper is a short review of the fabrication, wet and dry corrosion, as well as plasma nitridation of novel Ni-Cr nanocomposites. The nanocomposites, fabricated by co-electrodeposition of Ni and nanometer-sized Cr particles, have the nanocrystalline Ni matrix dispersing the second phase of nanoparticles. They, compared to conventionally coarse-grained Ni-Cr alloys, exhibit dramatically increased resistance to liquid corrosion in a 3.5% NaCl solution, and to hot corrosion under molten salt of Na2SO4-Na2SO4-NaCl at 700oC. The reason for these is correlated with the unique structure of the nanocomposite, which guarantees the fast diffusion of chromium from the composite interior to the corrosion front for the formation of a continuous, protective layer of chromium oxide-rich films severing the composites from environmental corrosive species. During plasma nitridation at 560oC the Ni-Cr nanocomposite forms a thick nitriding layer which cannot be achieved on the conventional alloy counterpart with a comparable composition, due to enhanced nitridation kinetics.

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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