magnetic techniques for the isolation and purification of proteins and peptides | biomagnetic research and technology | full text

magnetic techniques for the isolation and purification of proteins and peptides | biomagnetic research and technology | full text

Isolation and separation of specific molecules is used in almost all areas of biosciences and biotechnology. Diverse procedures can be used to achieve this goal. Recently, increased attention has been paid to the development and application of magnetic separation techniques, which employ small magnetic particles. The purpose of this review paper is to summarize various methodologies, strategies and materials which can be used for the isolation and purification of target proteins and peptides with the help of magnetic field. An extensive list of realised purification procedures documents the efficiency of magnetic separation techniques.

Isolation, separation and purification of various types of proteins and peptides, as well as of other specific molecules, is used in almost all branches of biosciences and biotechnologies. Separation science and technology is thus very important area necessary for further developments in bio-oriented research and technology. New separation techniques, capable of treating dilute solutions or solutions containing only minute amounts of target molecules in the presence of vast amounts of accompanying compounds in both small and large-scale processes, even in the presence of particulate matter, are necessary.

In the area of biosciences and biotechnology the isolation of proteins and peptides is usually performed using variety of chromatography, electrophoretic, ultrafiltration, precipitation and other procedures, affinity chromatography being one of the most important techniques. Affinity ligand techniques represent currently the most powerful tool available to the downstream processing both in term of their selectivity and recovery. The strength of column affinity chromatography has been shown in thousands of successful applications, especially in the laboratory scale. However, the disadvantage of all standard column liquid chromatography procedures is the impossibility of the standard column systems to cope with the samples containing particulate material so they are not suitable for work in early stages of the isolation/purification process where suspended solid and fouling components are present in the sample. In this case magnetic affinity, ion-exchange, hydrophobic or adsorption batch separation processes, applications of magnetically stabilized fluidized beds or magnetically modified two-phase systems have shown their usefulness.

The basic principle of batch magnetic separation is very simple. Magnetic carriers bearing an immobilized affinity or hydrophobic ligand or ion-exchange groups, or magnetic biopolymer particles having affinity to the isolated structure, are mixed with a sample containing target compound(s). Samples may be crude cell lysates, whole blood, plasma, ascites fluid, milk, whey, urine, cultivation media, wastes from food and fermentation industry and many others. Following an incubation period when the target compound(s) bind to the magnetic particles the whole magnetic complex is easily and rapidly removed from the sample using an appropriate magnetic separator. After washing out the contaminants, the isolated target compound(s) can be eluted and used for further work.

Magnetic separation techniques have several advantages in comparison with standard separation procedures. This process is usually very simple, with only a few handling steps. All the steps of the purification procedure can take place in one single test tube or another vessel. There is no need for expensive liquid chromatography systems, centrifuges, filters or other equipment. The separation process can be performed directly in crude samples containing suspended solid material. In some cases (e.g., isolation of intracellular proteins) it is even possible to integrate the disintegration and separation steps and thus shorten the total separation time [1]. Due to the magnetic properties of magnetic adsorbents (and diamagnetic properties of majority of the contaminating molecules and particles present in the treated sample), they can be relatively easily and selectively removed from the sample. In fact, magnetic separation is the only feasible method for recovery of small magnetic particles (diameter ca 0.1 1 m) in the presence of biological debris and other fouling material of similar size. Moreover, the power and efficiency of magnetic separation procedures is especially useful at large-scale operations. The magnetic separation techniques are also the basis of various automated procedures, especially magnetic-particle based immunoassay systems for the determination of a variety of analytes, among them proteins and peptides. Several automated systems for the separation of proteins or nucleic acids have become available recently.

Magnetic separation is usually very gentle to the target proteins or peptides. Even large protein complexes that tend to be broken up by traditional column chromatography techniques may remain intact when using the very gentle magnetic separation procedure [2]. Both the reduced shearing forces and the higher protein concentration throughout the isolation process positively influence the separation process.

Separation of target proteins using standard chromatography techniques often leads to the large volume of diluted protein solution. In this case appropriate magnetic particles can be used for their concentration instead of ultrafiltration, precipitation etc. [3].

The purpose of this review is to summarize various methodologies and strategies which can be employed for the isolation and purification of target proteins and peptides with the help of magnetic materials. An extensive list of realised purification procedures documents the efficiency of magnetic separation techniques. All these information will help the scientists to select the optimal magnetic material and the purification procedure.

The basic equipment for laboratory experiments is very simple. Magnetic carriers with immobilized affinity or hydrophobic ligands, magnetic particles prepared from a biopolymer exhibiting affinity for the target compound(s) or magnetic ion-exchangers are usually used to perform the isolation procedure. Magnetic separators of different types can be used for magnetic separations, but many times cheap strong permanent magnets are equally efficient, especially in preliminary experiments.

Magnetic carriers and adsorbents can be either prepared in the laboratory, or commercially available ones can be used. Such carriers are usually available in the form of magnetic particles prepared from various synthetic polymers, biopolymers or porous glass, or magnetic particles based on the inorganic magnetic materials such as surface modified magnetite can be used. Many of the particles behave like superparamagnetic ones responding to an external magnetic field, but not interacting themselves in the absence of magnetic field. This is important due to the fact that magnetic particles can be easily resuspended and remain in suspension for a long time. In most cases, the diameter of the particles differs from ca 50 nm to approx. 10 m. However, also larger magnetic affinity particles, with the diameters up to millimetre range, have been successfully used [4]. Magnetic particles having the diameter larger than ca 1 m can be easily separated using simple magnetic separators, while separation of smaller particles (magnetic colloids with the particle size ranging between tens and hundreds of nanometers) may require the usage of high gradient magnetic separators.

Commercially available magnetic particles can be obtained from a variety of companies. In most cases polystyrene is used as a polymer matrix, but carriers based on cellulose, agarose, silica, porous glass or silanized magnetic particles are also available. Examples of magnetic particles used (or usable) for proteins and peptides separation can be found elsewhere [57].

Particles with immobilised affinity ligands are available for magnetic affinity adsorption. Streptavidin, antibodies, protein A and Protein G are used most often in the course of protein and peptides isolation. Magnetic particles with above mentioned immobilised ligands can also serve as generic solid phases to which native or modified affinity ligands can be immobilised (e.g., antibodies in the case of immobilised protein A, protein G or secondary antibodies, biotinylated molecules in the case of immobilised streptavidin).

Also some other affinity ligands (e.g., nitrilotriacetic acid, glutathione, trypsin, trypsin inhibitor, gelatine etc.) are already immobilised to commercially available carriers. To immobilise other ligands of interest to both commercial and laboratory made magnetic particles standard procedures used in affinity chromatography can be employed. Usually functional groups available on the surface of magnetic particles such as -COOH, -OH or -NH2 are used for immobilisation, in some cases magnetic particles are available already in the activated form (e.g., tosylactivated, epoxyactivated etc).

In the laboratory magnetite (or similar magnetic materials such as maghemite or ferrites) particles can be surface modified by silanization. This process modifies the surface of the inorganic particles so that appropriate functional groups become available, which enable easy immobilisation of affinity ligands [8]. In exceptional cases enzyme activity can be decreased as a result of usage of magnetic particles with exposed iron oxides. In this case encapsulated microspheres, having an outer layer of pure polymer, will be safer.

Biopolymers such as agarose, chitosan, kappa carrageenan and alginate can be easily prepared in a magnetic form. In the simplest way the biopolymer solution is mixed with magnetic particles and after bulk gel formation the magnetic gel formed is mechanically broken into fine particles [9]. Alternatively biopolymer solution containing dispersed magnetite is dropped into a mixed hardening solution [4] or water-in-oil suspension technique is used to prepare spherical particles [10].

In another approach used standard affinity or ion-exchange chromatography material was post-magnetised by interaction of the sorbent with water-based ferrofluid. Magnetic particles accumulated within the pores of chromatography adsorbent thus modifying this material into magnetic form [12, 13]. Alternatively magnetic Sepharose or other agarose gels were prepared by simple contact with freshly precipitated or finely powdered magnetite [12, 14].

Magnetoliposomes (magnetic derivatives of standard liposomes), either in the original form or after immobilization of specific proteins, have the potential for the separation of antiphospholipid antibodies [15], IgG antibodies [16] and other proteins of interest [17].

Magnetic separators are necessary to separate the magnetic particles from the system. In the simplest approach, a small permanent magnet can be used, but various magnetic separators employing strong rare-earth magnets can be obtained at reasonable prices. Commercial laboratory scale batch magnetic separators are usually made from magnets embedded in disinfectant-proof material. The racks are constructed for separations in Eppendorf micro-tubes, standard test tubes or centrifugation cuvettes, some of them have a removable magnetic plate to facilitate easy washing of separated magnetic particles. Other types of separators enable separations from the wells of microtitration plates and the flat magnetic separators are useful for separation from larger volumes of suspensions (up to approx. 500 1000 ml). Examples of typical batch magnetic separators are shown in Fig. 1.

Examples of batch magnetic separators applicable for magnetic separation of proteins and peptides. A: Dynal MPC -S for six microtubes (Dynal, Norway); B: Dynal MPC 1 for one test tube (Dynal, Norway); C: Dynal MPC L for six test tubes (Dynal, Norway); D: magnetic separator for six Eppendorf tubes (New England BioLabs, USA); E: MagneSphere Technology Magnetic Separation Stand, two position (Promega, USA); F: MagnaBot Large Volume Magnetic Separation Device (Promega, USA); G: MagneSphere Technology Magnetic Separation Stand, twelve-position (Promega, USA); H: Dynal MPC 96 S for 96-well microtitre plates (Dynal, Norway); I: MagnaBot 96 Magnetic Separation Device for 96-well microtitre plates (Promega, USA); J: BioMag Solo-Sep Microcentrifuge Tube Separator (Polysciences, USA); K: BioMag Flask Separator (Polysciences, USA); L: MagneSil Magnetic Separation Unit (Promega, USA); M: MCB 1200 processing system for 12 microtubes based on MixSep process (Sigris Research, USA); N: PickPen magnetic tool (Bio-Nobile, Finland). Reproduced with the permission of the above mentioned companies; the photos were taken from their www pages.

Flow-through magnetic separators are usually more expensive, and high gradient magnetic separators (HGMS) are the typical examples. Laboratory scale HGMS is composed from a column packed with fine magnetic grade stainless steel wool or small steel balls which is placed between the poles of an appropriate magnet. The suspension is pumped through the column, and magnetic particles are retained within the matrix. After removal the column from the magnetic field, the particles are retrieved by flow and usually by gentle vibration of the column.

For work in dense suspensions, open gradient magnetic separators may be useful. A very simple experimental set-up for the separation of magnetic affinity adsorbents from litre volumes of suspensions was described [19].

Currently many projects require the analysis of a high number of individual proteins or variants. Therefore, methods are required that allows multiparallel processing of different proteins. There are several multiple systems for high throughput nucleic acid and proteins preparation commercially available. The most often used approach for proteins isolation is based on the isolation and assay of 6xHis-tagged recombinant proteins using magnetic beads with Ni-nitriloacetic acid ligand [20]. The commercially available platforms can be obtained from several companies such as Qiagen, USA (BioRobot and BioSprint series), Tecan, Japan (Te-MagS) or Thermo Electron Corporation, USA (KingFisher).

Proteins and peptides in the free form can be directly isolated from different sources. Membrane bound proteins have to be usually solubilized using appropriate detergents. When nuclei are broken during sample preparation, DNA released into the lysate make the sample very viscous. This DNA may be sheared by repeated passage up and down through a 21 gauge hypodermic syringe needle before isolation of a target protein. Alternatively, DNase can be added to enzymatically digest the DNA.

Magnetic beads in many cases exhibit low non-specific binding of non-target molecules present in different samples. Certain samples may still require preclearing to remove molecules which have high non-specific binding activity. If preclearing is needed, the sample can be mixed with magnetic beads not coated with the affinity ligand. In the case of immunomagnetic separation, magnetic beads coated with secondary antibody or with irrelevant antibodies have been used. The non-specific binding can also be minimised by adding a non-ionic detergent both in the sample and in the washing buffers after isolation of the target.

In general, magnetic affinity separations can be performed in two different modes. In the direct method, an appropriate affinity ligand is directly coupled to the magnetic particles or biopolymer exhibiting the affinity towards target compound(s) is used in the course of preparation of magnetic affinity particles. These particles are added to the sample and target compounds then bind to them. In the indirect method the free affinity ligand (in most cases an appropriate antibody) is added to the solution or suspension to enable the interaction with the target compound. The resulting complex is then captured by appropriate magnetic particles. In case antibodies are used as free affinity ligands, magnetic particles with immobilised secondary antibodies, protein A or protein G are used for capturing of the complex. Alternatively the free affinity ligands can be biotinylated and magnetic particles with immobilised streptavidin or avidin are used to capture the complexes formed. In both methods, magnetic particles with isolated target compound(s) are magnetically separated and then a series of washing steps is performed to remove majority of contaminating compounds and particles. The target compounds are then usually eluted, but for specific applications (especially in molecular biology, bioanalytical chemistry or environmental chemistry) they can be used still attached to the particles, such as in the case of polymerase chain reaction, magnetic ELISA etc.

The two methods perform equally well, but, in general, the direct technique is more controllable. The indirect procedure may perform better if affinity ligands have poor affinity for the target compound.

In most cases, magnetic batch adsorption is used to perform the separation step. This approach represents the simplest procedure available, enabling to perform the whole separation in one test-tube or flask. If larger magnetic particles (with diameters above ca 1 m) are used, simple magnetic separators can be employed. In case magnetic colloids (diameters ranging between tens and hundreds of nanometres) are used as affinity adsorbents, high-gradient magnetic separators have usually to be used to remove the magnetic particles from the system.

Alternatively magnetically stabilised fluidised beds (MSFB), which enable a continuous separation process, can be used. The use of MSFB is an alternative to conventional column operation, such as packed-bed or fluidised bed, especially for large-scale purification of biological products. Magnetic stabilisation enables the expansion of a packed bed without mixing of solid particles. High column efficiency, low pressure drop and elimination of clogging can be reached [21, 22].

Also non-magnetic chromatographic adsorbents can be stabilized in magnetically stabilized fluidized beds if sufficient amount of magnetically susceptible particles is also present. The minimum amount of magnetic particles necessary to stabilize the bed is a function of various parameters including the size and density of both particles, the magnetic field strength, and the fluidization velocity. A variety of commercially available affinity, ion-exchange, and adsorptive supports can be used in the bed for continuous separations [23].

Biocompatible two phase systems, composed for example from dextran and polyethylene glycol, are often used for isolation of biologically active compounds, subcellular organelles and cells. One of the disadvantages of this system is the slow separation of the phases when large amounts of proteins and cellular components are present. The separation of the phases can be accelerated by the addition of fine magnetic particles or ferrofluids to the system followed by the application of a magnetic field. This method seems to be useful when the two phases have very similar densities, the volumetric ratio between the phases is very high or low, or the systems are viscous. Magnetically enhanced phase separation usually increases the speed of phase separation by a factor of about 10 in well-behaved systems, but it may increase by a factor of many thousands in difficult systems. The addition of ferrofluids and/or iron oxide particles was shown to have usually no influence on enzyme partioning or enzyme activity [24, 25].

Proteins and peptides isolated using magnetic techniques have to be usually eluted from the magnetic separation materials. In most cases bound proteins and peptides can be submitted to standard elution methods such as the change of pH, change of ionic strength, use of polarity reducing agents (e.g., dioxane or ethyleneglycol) or the use of deforming eluents containing chaotropic salts. Affinity elution (e.g., elution of glycoproteins from lectin coated magnetic beads by the addition of free sugar) may be both a very efficient and gentle procedure.

Magnetic affinity and ion-exchange separations have been successfully used in various areas, such as molecular biology, biochemistry, immunochemistry, enzymology, analytical chemistry, environmental chemistry etc [2629]. Tables 1, 2, 3, 4, 5, 6, 7, 8, 9 show some selected applications of these techniques for proteins and peptides isolation.

In the case of proteins and peptides purifications, no simple strategy for magnetic affinity separations exists. Various affinity ligands have been immobilised on magnetic particles, or magnetic particles have been prepared from biopolymers exhibiting the affinity for target enzymes or lectins. Immunomagnetic particles, i.e. magnetic particles with immobilised specific antibodies against the target structures, have been used for the isolation of various antigens, both molecules and cells [5] and can thus be used for the separation of specific proteins.

Magnetic separation procedures can be employed in several ways. Preparative isolation of the target protein or peptide is usually necessary if further detailed study is intended. In other cases, however, the magnetic separation can be directly followed (after elution with an appropriate buffer) with SDS electrophoresis. Magnetically separated proteins and peptides can also be used for further mass spectroscopy characterization [30, 31]. The basic principles of magnetic separations can be used in the course of protein or peptide determination using various types of solid phase immunoassays. Usually immunomagnetic particles directly capture the target analyte, or magnetic particles with immobilised streptavidin are used to capture the complex of biotinylated primary antibody and the analyte. The separated analyte is then determined (usually without elution) using an appropriate method. A combination of magnetic separation with affinity capillary electrophoresis is also possible [32].

Genetic engineering enables the construction of gene fusions resulting in fusion proteins having the combined properties of the original gene products. To date, a large number of different gene fusion systems, involving fusion partners that range in size from one amino acid to whole proteins, capable of selective interaction with a ligand immobilized onto magnetic particles or chromatography matrices, have been described. In such systems, different types of interactions, such as enzyme-substrate, receptor-target protein, polyhistidines-metal ion, and antibody-antigen, have been utilized. The conditions for purification differ from system to system and the environment tolerated by the target protein is an important factor for deciding which affinity fusion partner to choose. In addition, other factors, including protein localization, costs for the affinity matrix and buffers, and the possibilities of removing the fusion partner by site-specific cleavage, should also be considered [33, 34]. As an example, isolation of recombinant oligohistidine-tagged proteins is based on the application of metal chelate magnetic adsorbents [35, 36]. This method has been used successfully for the purification of proteins expressed in bacterial, mammalian, and insect systems.

Antibodies from ascites, serum and tissue culture supernatants can be efficiently isolated using magnetic particles with immobilized Protein A, Protein G or anti-immunoglobulin antibodies. Protein A, isolated from Staphylococcus aureus, binds the Fc region of IgG of most mammalian species with high affinity, leaving antigen specific sites free. Protein G, isolated from Streptococcus sp., reacts with a larger number of IgG isotypes. It has a higher binding affinity to immunoglobulins than Protein A, however, it also interacts with the Fab regions of IgG, although the affinity is ten times lower than for the Fc region [37]. Antiphospholipid antibodies were successfully isolated using magnetoliposomes [15].

Aptamers are DNA or RNA molecules that have been selected from random pools based on their ability to bind other molecules. Aptamers binding proteins can be immobilised to magnetic particles and used for isolation of target proteins.

DNA/RNA binding proteins (e.g., promoters, gene regulatory proteins and transcription factors) are often short-lived and in low abundance. A rapid and sensitive method, based on the immobilization of biotinylated DNA/RNA fragments containing the specific binding sequence to the magnetic streptavidin particles, can be used. The bound DNA/RNA binding proteins are usually eluted with high salt buffer or change of pH [38].

Other types of proteins were isolated using specific affinity-based procedures. For example, plasminogen immobilized on magnetic particles was used to separate scrapie and bovine spongiform encephalopathy associated prion protein PrPSc from its conformer which is a cellular protein called PrPC. In fact, plasminogen represents the first endogenous factor discriminating between normal and pathological prion protein. This unexpected property may be exploited for diagnostic purposes [39, 40].

Magnetic separation was also successfully used for the recovery of proteins expressed in the form of inclusion bodies, involving at first chemical extraction from the host cells, then adsorptive capture of the target protein onto small magnetic adsorbents, followed by rapid collection of the product-loaded supports with the aid of high gradient magnetic fields [41].

A new approach for analytical ion-exchange separation of native proteins and proteins enzymatic digest products has been described recently [31]. Magnetite particles were covered with a gold layer and then stabilized with ionic agents. These charged stabilizers present at the surface of the gold particles are capable of attracting oppositely charged species from a sample solution through electrostatic interactions. [email protected] particles having negatively charged surfaces are suitable probes for selectively trapping positively charged proteins and peptides from aqueous solutions. The species trapped by the isolated particles were then characterized by matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) after a simple washing.

Magnetic solid phase extraction (MSPE) enables to preconcentrate target analytes from larger volumes of solutions or suspensions using relatively small amount of magnetic specific adsorbent. Up to now this procedure was used for preconcentration of low-molecular weight xenobiotics [42, 43] but using suitable magnetic adsorbents the MSPE could be used to preconcetrate target proteins and peptides as well.

Sometimes the removal of certain proteins will reveal functions involving the depleted proteins or will help in the course of subsequent protein isolation. As an example, Dynabeads have been used to remove involved proteins from Xenopus egg extracts for analyses of the cell mitosis mechanisms [44, 45]. Rapid removal of contaminating proteolytic enzymes from the crude samples could increase yields of sensitive proteins due to the limitation of their proteolysis [46].

A combination of mechanical cell disintegration and magnetic batch affinity adsorption was used to simplify the isolation of intracellular proteins. Magnetic glass beads were used because of their hardness and rigidity [1].

An example of quite different protein purification strategy can also be mentioned. Proteins associated with the endocytic vesicles of Dictyostelium discoideum were separated after magnetic isolation of the vesicles that was accomplished by feeding the amoebae with dextran-stabilized iron oxide particles. The cells were broken, the labelled vesicles were magnetically separated and then disrupted to release proteins which were resolved by SDS-PAGE. After in-gel digestion with endoproteinase Lys-C or Asp-N the generated peptides were used for amino acid sequencing. This strategy allowed the identification of the major protein constituents of the vesicles [47]. Analogous procedure was used for the separation and study of peroxisomes proteins when at first peroxisomes were separated using magnetic beads with immobilized specific antibodies and then the protein content of the separated peroxisomes was analysed [48].

Standard liquid column chromatography is currently the most often used technique for the isolation and purification of target proteins and peptides. Magnetic separation techniques are relatively new and still under development. Magnetic affinity particles are currently used mainly in molecular biology (especially for nucleic acids separation), cell biology and microbiology (separation of target cells) and as parts of the procedures for the determination of selected analytes using magnetic ELISA and related techniques (especially determination of clinical markers and environmental contaminants). Up to now separations in small scale prevail and thus the full potential of these techniques has not been fully exploited.

It can be expected that further development will be focused at least on two areas. The first one will be focused on the laboratory scale application of magnetic affinity separation techniques in biochemistry and related areas (rapid isolation of a variety of both low- and high-molecular weight substances of various origin directly from crude samples thus reducing the number of purification steps) and in biochemical analysis (application of immunomagnetic particles for separation of target proteins from the mixture followed by their detection using ELISA and related principles). Such a type of analysis will enable to construct portable assay systems enabling e.g. near-patient analysis of various protein disease markers. New methodologies, such as the application of chip and microfluidics technologies, may result in the development of magnetic separation processes capable of magnetic separation and detection of extremely small amount of target biologically active compounds [49].

In the second area, larger-scale (industrial) systems are believed to be developed and used for the isolation of biologically active compounds directly from crude culture media, wastes from food industry etc., integrating three classical steps (clarification, concentration and initial purification) into a single unit operation [50]. It is not expected that extremely large amounts of low cost products will be isolated using magnetic techniques, but the attention should be focused onto the isolation of minor, but highly valuable components present in raw materials. Of course, prices of magnetic carriers have to be lowered and special types of low-cost, biotechnology applicable magnetic carriers and adsorbents prepared by simple and cheap procedures have to become available. The existence of inexpensive and effective magnetic separators enabling large-scale operations is necessary, as well.

In the near future quite new separation strategies can appear. A novel magnetic separation method, which utilizes the magneto-Archimedes levitation, has been described recently and applied to separation of biological materials. By using the feature that the stable levitation position under a magnetic field depends on the density and magnetic susceptibility of materials, it was possible to separate biological materials such as haemoglobin, fibrinogen, cholesterol, and so on. So far, the difference of magnetic properties was not utilized for the separation of biological materials. Magneto-Archimedes separation may be another way for biological materials separation [51].

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The research is a part of ILE Research Intention No. AV0Z6087904. The work was supported by the Ministry of Education of the Czech Republic (Project No. ME 583) and Grant Agency of the Czech Academy of Sciences (Project No. IBS6087204).

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eclipse magnetics launches new products for industrial filtration - magnetics magazine

eclipse magnetics launches new products for industrial filtration - magnetics magazine

Eclipse Magnetics, a manufacturer of industrialworkholdingand separation systems based in the UK, has recently introduced several products in its lines of filtration equipment that demonstrate innovative new applications of magnetics technology for metals and food processing.

The company isnow offering a full range ofindustry standardsieve magnets, shown in the picture above,to ensure product purity in the food industry. Easy to install, the sieve magnet is a full stainless-steel design which is fully compatible with industry standard and leading manufacturers of vibratory sieves.

Typically positioned beneath the sieve screen in food processing applications including dry powders and granulates,the newsieve magnetsachieveexcellent separation, says Eclipse.Due to the high intensity magnetic field, even sub-micron sized ferrous metal and paramagnetic contamination can be successfully attracted and removed.

Ensuring product quality and purity is one of the greatest challenges faced by the processing industries. Our sieve magnets have a worldwide proven reputation in the food industry, ensuring protection against ferrous contamination, and maintaining efficiency and productivity within the productionprocess,saidMartyn Cotterill,generalsalesmanager. The sieve magnetsare available in 7,000 and 11,000 Gauss on product contact surface.

The companys newlylaunchedAutofiltrexrangeof automated filters, available inthreesizes with features including fully automated cleaning and a magnetic reclaim unit, isdesigned to be a high performance magnetic filtration device for handlingmost ferrous machining applications such asgrinding, honing, lapping, forming and quenching.It wasexhibitedin September at EMO Exhibition in Hannover,a trade fair for the metalworking industry.

We were delighted to see that theAutofiltrexwas a popular product at EMO, said Steve McAllorum, sales and marketing director. Not only did we receive plenty of enquiries and requests for more information, we also received a good amount of orders from manufacturers looking to improve efficiencies forprecision metal finishing processes. Thisis a great example of how an investment in magnetic technologies canimprove efficiency inautomotive and other metal finishing operations.

Thenewfilterscan be fitted in-line or off-line, ensuring 24/7 ultra-polished fluids and delivering considerable advantages over traditional filter media, said McAllorum.Themodular design allows additional units to be added to accommodate increased flow rates, depending on application needs. Offeringsub-micron filtration performance, thefiltersdeliver cleaner fluid to the machine, therefore improving surface finish and accuracy as well as reducing expenditure on filter media.

They are among an extensive line of filters manufactured by Eclipse. Itprovides a full range of coolant, oil, water, and industrial fluid filtration systems.Todays systems, the company notes,are massively advanced from traditional applications of magnets to remove ferrous particles.

The basic principle of magnetic filtration,also referred to as magnetic separation,is that fluid flows around a magnetic rod or core which attracts ferrous particles, removing them from the fluid and ensuring that clean fluids are returned to the contact area either on a machine tool or wash system. When the magnetic core becomes saturated with ferrous contamination it is then cleaned either manually or, in the case of theAutomag, automatically.

In the past magnetic systems were very basic, often consisting of randomly placing a low strength magnetic bar or rod in a settlement tank or a low strength magnetic roller, the results are largely ineffective. Whilst the basic principles are similar, there are huge differences in the product design and levels of performance betweenthe magnetic systems of the past anditsadvanced magnetic filters and the magnetic systemstoday.

Eclipseusesuse high strength neodymium magnets which attract virtually 100% of the ferrous particles including sub-micron size particles. The advanced magnetic core design creates a magnetic field pattern which ensures that the filters do not block even in high contamination applications.

In addition to magnetic performance, itsdesign and development team also researched fluid flow characteristics, henceitsfilters are designed to optimize the fluid flow, thereby maximizing contamination exposure to the magnet and ensuring almost 100% collection rateswithoutinterrupting or reducing the fluid rates.

Magnetic filters or magnetic separators are more effective at removing ferrous particles than virtually all other types of filtration, says Eclipse. Traditional barrier filters are constrained by the pore size in thebarrier. Make the pore too big and contamination continues to circulate, make the pore too small and it blocks.According to Eclipse, its patentedmagnetic design means that the filter will not block so there is no blinding or pressure build up.

Based in Sheffield, Eclipse makes a broad array of magnetic-based products includingworkholdingsystems, magnet assemblies, workshop tools, lifting and handling systems, industrial filters, foreign body removal and plumbing products.It also provides custom magnetic assembliesforOEMs inthe electronics, automotive, aerospace, pumps, audio equipment, sensors and security sectorsas well as servingresearch and developmentefforts and academic institutions.Part of the Spear & Jackson Group, Eclipse operates globally throughEclipse Tools North America based in Canada, and other operations in China and France.

Femtet, an integrated CAE software package for electromagnetic design and simulation, is now available from Murata Software, a part of Murata Mfg. Co., Ltd., based in Japan. A leading manufacturer of electronic components and devices, []

SpControl Technologies, startup developer of a new artificial-intelligence magnetic design platform known as Frenetic, has recently bolstered its go-to-market power with a fund raising backed by venture capitalinvestors in Spain, Portugal and Germany. We have []

Using two core magnetic technologies to compete with the precision of optical encoders yet withstand intense mechanical vibration, automation manufacturer Wachendorff continues to see its WDGA line of absolute encoders put to the test by []

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structure and working principle of wet permanent magnet drum-type ptms magnetic separator - news - foshan powtech technology company limited

structure and working principle of wet permanent magnet drum-type ptms magnetic separator - news - foshan powtech technology company limited

Wet permanent magnet drum-type PTMS magnetic separator is mainly composed of six parts: cylinder, roller, brush roller, magnetic system, tank and transmission. The cylinder is welded into a cylinder by a 2-3mm stainless steel plate coil. The end cover is cast aluminum or workpiece and connected to the cylinder with stainless steel screws. The motor drives the cylinder, the magnetic roller and the brush roller to rotate through the reducer or direct stepless speed regulating motor. The magnetic system is an open magnetic system, mounted in a cylinder and exposed to the full magnetic. The magnetic block is mounted on the bottom plate of the magnetic yoke with stainless steel bolts. The shaft of the magnetic yoke extends out of the cylinder, and the shaft end is fixed with a crank arm. Pull the arm to adjust the deflection Angle of the magnetic system, and fix it with the pull rod after proper adjustment. The working area of the tank is made of stainless steel plates, and the frame and other parts of the tank are welded with ordinary steel.

After the slurry flows into the tank through the feed tank, under the action of the water flow of the feed water pipe, the ore particles enter into the feed area of the tank in a loose state. Under the action of the magnetic field, the magnetic particles form a "magnetic mass" or "magnetic chain". The "magnetic mass" or "magnetic chain" in the slurry is affected by the magnetic force, moving towards the magnetic pole, and is adsorbed on the cylinder. Due to the polarity of the magnetic poles along the cylinder rotation direction are arranged alternately, and fixed at work, "magnetic group" or "magnetic chain" in the cylinder rotates, with alternating polarity magnetic stirring, was mixed in the "magnetic group" or "magnetic chain" of the gangue and other non-magnetic minerals in turn off, has finally been sucked on the surface of the cylinder, the "magnetic group" or "magnetic lotus" is to concentrate. The concentrate is transferred to the edge of the magnetic system with the cylinder, where the magnetic force is the weakest, and is discharged into the concentrate tank under the action of the flushing water gushing out of the discharge pipe. If it is a full magnetic roller, the discharge is carried out with a brush roller. Non-magnetic or weakly magnetic minerals are left in the slurry to be drained out of the tank, which is tailings.

basic principle of iron remover

basic principle of iron remover

magnetic separation equipment PTMS MAGNETIC SEPARATOR what is magnetic separation in chemistry The device that sorts iron minerals from raw materials by using the magnetic field's attractive properties to ferromagnetic materials is called a separator, also called a magnetic separator. The basic condition for achieving the sorting purpose is that the attraction force of the magnetic field to the ferromagnetic substance (F) is greater than the resultant force (Fc?, also called competitiveness) that prevents the magnetic particles from being separated. The Fc includes the gravity, centrifugal force, and inertial force of the ferromagnetic particles. And the resistance of fluid power and so on. When the slurry is de-ironed, the inertial force and fluid resistance are the main part of the competitiveness. At this time, the fluid resistance Fc=3dv Where: - mud viscosity D-mineral particle diameter V-mud flow rate According to the expression of Fc, the viscosity of the slurry, the size of the iron mineral particles and the flow velocity of the mud directly affect the magnitude of the competitiveness, that is, the effect of removing iron. Therefore, when using the iron remover, carefully grasp the "four degrees" (concentration, viscosity, speed and particle size) of the slurry. The particle size should be determined by the pore size selection of the vibrating screen; the speed is directly related to the flow rate; the viscosity is related to the concentration, properties and additives of the slurry; the concentration is related to the moisture ratio. A practical iron remover should have the following three conditions: 1 a sufficiently strong magnetic field source (F>Fc); 2 sufficient contact area to protect the opportunity and place to absorb prey; 3 Clean (separate) the ferromagnetic impurities that have been absorbed in a timely and effective manner. (Cleaning is the key to effective iron removal) Share to:

The device that sorts iron minerals from raw materials by using the magnetic field's attractive properties to ferromagnetic materials is called a separator, also called a magnetic separator. The basic condition for achieving the sorting purpose is that the attraction force of the magnetic field to the ferromagnetic substance (F) is greater than the resultant force (Fc?, also called competitiveness) that prevents the magnetic particles from being separated. The Fc includes the gravity, centrifugal force, and inertial force of the ferromagnetic particles. And the resistance of fluid power and so on.

According to the expression of Fc, the viscosity of the slurry, the size of the iron mineral particles and the flow velocity of the mud directly affect the magnitude of the competitiveness, that is, the effect of removing iron. Therefore, when using the iron remover, carefully grasp the "four degrees" (concentration, viscosity, speed and particle size) of the slurry. The particle size should be determined by the pore size selection of the vibrating screen; the speed is directly related to the flow rate; the viscosity is related to the concentration, properties and additives of the slurry; the concentration is related to the moisture ratio.

size fractionation of magnetic nanoparticles by magnetic chromatography - sciencedirect

size fractionation of magnetic nanoparticles by magnetic chromatography - sciencedirect

Comparison of different magnetic field sources and operation modes for magnetic chromatography.Fractionation of magnetic nanoparticles in the size range of 50400nm at more than 30CV/h.High separation sharpness factor of 0.62.

Magnetic chromatography is a promising method for fractionation of magnetic nanoparticles with respect to their size and/or magnetic properties. In this study, we investigate the effect of different magnetic field sources and operation modes on the retention of magnetic nanoparticles which pass through a chromatographic column filled with a fine magnetizable matrix. For nanoparticles in the size range between 50 and 400nm, both constant magnetic fields and square wave AC fields with amplitudes of around 2mT, result in retention factors of up to 2, while still showing good particle recoveries of more than 95%. In contrast, when using the on-off magnetic field operation reported previously, retention factors of only 1.4 could be achieved. We also demonstrate that single domain magnetic nanoparticles show retention factors of 1.21.4 even without the application of an external magnetic field, due to their spontaneous magnetization. By using a combination of online UV-measurement and sample collection followed by the determination of the particle size distribution (PSD) by dynamic light scattering, a quantification of the fractionation efficiency could be achieved. Despite the short column of only 12cm and the high specific throughput of more than 30 column volumes per hour a separation sharpness of 0.62 could be attained, demonstrating the high potential of the method for scalable nanoparticle fractionation.

application of electromagnetic (em) separation technology to metal refining processes: a review | springerlink

application of electromagnetic (em) separation technology to metal refining processes: a review | springerlink

Application of electromagnetic (EM) force to metal processing has been considered as an emerging technology for the production of clean metals and other advanced materials. In the current paper, the principle of EM separation was introduced and several schemes of imposing EM field, such as DC electric field with a crossed steady magnetic field, AC electric field, AC magnetic field, and traveling magnetic field were reviewed. The force around a single particle or multi-particles and their trajectories in the conductive liquid under EM field were discussed. Applications of EM technique to the purification of different liquid metals such as aluminum, zinc, magnesium, silicon, copper, and steel were summarized. Effects of EM processing parameters, such as the frequency of imposed field, imposed magnetic flux density, processing time, particle size, and the EM unit size on the EM purification efficiency were discussed. Experimental and theoretical investigations have showed that the separation efficiency of inclusions from the molten aluminum using EM purification could as high as over 90pct. Meanwhile, the EM purification was also applied to separate intermetallic compounds from metal melt, such as -AlFeMnSi-phase from the molten aluminum. And then the potential industrial application of EM technique was proposed.

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K. Li, J. Wang, D. Shu, T.X.Sun, B.D. Sun and Y.H. Zhou: Theoretical and Experimental Investigation of Aluminum Melt Cleaning using Alternating Electromagnetic Field, Materials Letters, 2002, vol. 56 (3), pp. 215-20.

D. Shu, B. Sun, K. Li and Y. Zhou: Particle Trajectories in Aluminum Melt flowing in A Square Channel under an Alternating Magnetic Field Generated by A Solenoid, Scripta Materialia, 2003, vol. 48, pp. 1385-90.

S. Makarov, R. Ludwig and D. Apelian: Electromagnetic Separation Techniques in Metal Casting. II. Separation with Superconduting Coils, IEEE Transactions on Magnetics, 2001, vol. 37 (2), pp. 1024-31.

A.P. Dong, D. Shu, J. Wang and B.D. Sun: Identification of Fe-Al-Zn Dross Phase in Galvanised Zinc Bath and Its Separation by Method of Alternating Magnetic Field, Ironmaking and Steelmaking, 2008, vol. 35 (8), pp. 633-37.

A.P. Dong, S. Da, J. Wang and B.D. Sun: Separation Behaviour of Zinc Dross from Hot dip Galvanising Melts of Different Aluminium Concentrations by Alternating Magnetic Field, Ironmaking and Steelmaking, 2009, vol. 36 (4), pp. 316-20.

M.R. Afshar, M.R. Aboutalebi, M. Isac and R.I.L. Guthrie: Mathematical Modeling of Electromagnetic Separation of Inclusions from Magnesium Melt in a Rectangular Channel, Materials Letters, 2007, vol. 61 (10), pp. 2045-49.

L.N.W. Damoah and L. Zhang: 3rd International Symposium on High-Temperature Metallurgical ProcessingTMS 2012 Annual Meeting and Exhibition, Orlando, FL, Minerals, Metals and Materials Society, 2012, pp. 27178.

L. Zhang, E. vrelid, S. Senanu, B. Agyei-Tuffour and A.N. Femi: REWAS2008: 2008 Global Symposium on Recycling, Waste Treatment and Clean Technology, CANCUN, MEXICO, TMS, Warrendale, PA, 2008, pp. 101126.

M. Kadkhodabeigi, J. Safarian, H. Tveit, M. Tangstad and S.T. Johansen: Removal of SiC Particles from Solar Grade Silicon Melts by Imposition of High Frequency Magnetic Field, Trans. Nonferr. Met. Soc. China, 2012, vol. 22 (11), pp. 2813-21.

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The authors wish to acknowledge the authors of the literatures cited in the current paper and publishers for their permission to reproduce figures from their publications and are grateful for the support from the National Science Foundation China (Grant Nos. 51274034, 51334002, U1360201, and 51204110), Beijing Key Laboratory of Green Recycling and Extraction of Metals (GREM), the Laboratory of Green Process Metallurgy and Modeling (GPM2) and the High Quality steel Consortium (HQSC) at the School of Metallurgical and Ecological Engineering at University of Science and Technology Beijing (USTB), China.

Zhang, L., Wang, S., Dong, A. et al. Application of Electromagnetic (EM) Separation Technology to Metal Refining Processes: A Review. Metall Mater Trans B 45, 21532185 (2014). https://doi.org/10.1007/s11663-014-0123-y

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