Barely three months into the new year and we are happy to announce a monumental milestone reached - 150 million downloads.
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This achievement solidifies IntechOpen’s place as a pioneer in Open Access publishing and the home to some of the most relevant scientific research available through Open Access.
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We are so proud to have worked with so many bright minds throughout the years who have helped us spread knowledge through the power of Open Access and we look forward to continuing to support some of the greatest thinkers of our day.
\n\n
Thank you for making IntechOpen your place of learning, sharing, and discovery, and here’s to 150 million more!
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1. Introduction
1.1. Formation of the protein-polyelectrolyte complex
Polyelectrolytes are flexible-chain polymers containing subunits with negative or positive charges. These compounds form soluble or insoluble complexes with proteins with opposite electrical charge.
The different equilibriums present in a solution of protein and polyelectrolyte are shown in figure 1.
Figure 1.
Formation of the protein- polyelectrolyte complex (binary complex).
As can be seen, when a protein interacts with a polyelectrolyte, a soluble complex is formed containing few molecules of the protein. As more molecules of protein interact with the polyelectrolyte, the complex becomes insoluble. Finally, the particles of insoluble complex start to interact with each other to form the macroscopic insoluble complex.
Besides this model of formation of the insoluble complex, there is another model in which the formation of the insoluble complex requires the presence of an inorganic polyion (figure 2).
Figure 2.
Formation of polyelectrolyte-ion-protein complex (ternary complex).
First, the polyelectrolyte interacts with the polyion and forms a soluble complex with charges oppose to those in the protein. Then, the protein interacts with the complex to form the insoluble complex.
In both cases, the formation and solubility of the complex depends on the pH and the ionic strength of the medium [1], the density of charges in the protein and the polyelectrolyte, the molecular weight and the concentration of the polyelectrolyte [2,3]. Various studies have been directed to understand the formation of these complexes in aqueous medium [4-6]. Equation 1 shows how the density of charges (σ) on the surface of the protein and the polyelectrolyte is affected by the pH and the ionic strength of the medium.
σ=∂σ∂pH(pH−pI)E1
Mattison et. al. postulated an equation that correlates the density of charges in the protein (σ) and the polyelectrolyte (ξ) with the Debye-Hückel constant (κ) that is highly dependent on ionic strength (a is a constant that depends on the protein-polyelectrolyte system) [7].
ξσ≅a⋅κE2
The conditions of the medium determine whether the soluble or the insoluble complex is formed, or if the complex is dissociated.
1.2. Stoichiometry of the protein-polyelectrolyte formation
When studying the interaction of a protein and a polyelectrolyte, it is interesting to know the minimum quantity of protein requires forming the maximum quantity of complex per polyelectrolyte unit. This value is called stoichiometry of the complex (e) and it is usually represented as the moles of polyelectrolyte per mol of protein, mass of polyelectrolyte per mass unit of protein, etc.
The stoichiometry of a protein-polyelectrolyte complex might be over or below 1 as shown in figure 3.
A complex with a stoichiometry below 1 contains more protein molecules than polyelectrolyte molecules. Usually, this kind of complex is insoluble, while a complex with a stoichiometry over 1 might be soluble or insoluble. As can be seen in figure 3, a complex with a stoichiometry below 1 can be turned into one with stoichiometry over 1 by adding polyelectrolyte to the medium. Of course, the effect can be reverted by adding protein.
Figure 3.
Stoichiometry (e) of a protein-polyelectrolyte complex.
1.3. Biotechnological applications of the protein-polyelectrolyte complex
In biotechnology, it is interesting to use insoluble protein-polyelectrolyte complexes with e < 1 since they can be used to purificate and concentrate industrial-interest enzymes [8], to immobilized enzymes in bioreactors or scarefolds.
1.3.1. Bioseparation of proteins from a complex mixture
The development of Biotechnology has allowed the used of enzymes in the production of food, drugs and in many others industries. At the same time, Genetic Engineering and Molecular Biology has allowed the expression of proteins in bacteria and superior microorganisms; however, some proteins must still being isolated from its natural sources due to complex post-traductional modifications that occur during the synthesis of the proteins. In both cases, the protein of interest is in a media containing many other biomolecules and inorganic compounds that need to be separated from the protein before applied it to any industrial process.
Most purification protocols consist on many steps: the first ones have the aim to concentrate the protein of interest and to obtain a high recovery; while the last steps of the protocol are expected to yield a high purification factor.
Precipitation of enzyme-polyelectrolyte insoluble complexes is a very useful technique to apply at the beginning of purification protocols since it requires simple equipment and so is very easy to scale up; needs low concentrations of the polyelectrolyte since it interacts with high affinity with the proteins; and can be based on a wide variety of polyelectrolytes, both natural and synthetic, positively or negatively charged. An important aspect of this technique is that the enzyme usually retains its tertiary structure and its catalytic activity. Even more, usually it is more stable in the presence of the polyelectrolyte [9,10].
1.3.2. Enzyme immobilization
The immobilization of enzymes is a process by which the protein is attached to a solid matrix, synthesized using a polyelectrolyte, in order to enhance the stability of the structure of the protein and to reuse enzyme [11]. Enzymes immobilized, in comparison with enzymes in solution, are more robust and resistant to environmental changes.
Immobilization can be performed by physical or chemical methods. The first results in weak interactions between the enzyme and the solid support and includes adsorption on a water-insoluble matrix and gel entrapment or micelles [12,13]. Chemical methods generate covalent bonds or electrostatic interactions between the enzyme and a water-insoluble support forming reticulated or single-chain particles. Insoluble complexes allow to immobilized enzymes by entrapment in polyelectrolyte solid particles, micelles or by covalent linkage to the support using carboimide as coupling.
The protein-matrix systems are widely used in bio-reactors for industrial process mainly because of the possibility of recycle the enzyme. Bio-reactors are very useful for the synthesis of organic compounds; since immobilized enzymes reduced the steps of the process, enhance the purity of the final products and allow stereo-selective synthesis. These systems also can be applied on the production of micro/nanocapsules for the delivery of proteins (or drugs). In this case, the use of polyelectrolytes sensitive to environmental conditions allows the releasing of the enzyme (or drug) molecules in different parts of the body [14].
1.4. Characterization of the protein-polyelectrolyte complex
The formation of the protein-polyelectrolyte complex can be studied by spectroscopic and calorimetric techniques.
Spectroscopy assays based on turbidimetric measurements allow knowing the effect of pH, ionic strength, time and temperature on the amount of insoluble complex formed. Phase diagrams, turbidimetric titrations and kinetic assays must be performed in order to evaluate the best conditions to obtain the maximum quantity of insoluble protein-polyelectrolyte complex [15;16].
Study the stability of the enzyme when it is part of the complex is also important to understand how the polyelectrolyte affects its catalytic activity since it is expected to use the enzyme in an industrial process. Fluorescence, UV-visible and circular dichroism spectroscopy are very useful techniques to analyze the structure of the protein but also must be performed experiments to study the enzymatic activity.
Although these techniques are helpful, they do not give an idea of the nature of the interaction between the protein and the polyelectrolyte. Calorimetric techniques such as differential scanning calorimetry and isothermal titration calorimetry allow studying the thermal stability of the enzyme in the presence of the polyelectrolyte and the nature of the interaction between the enzyme and polyelectrolyte, respectively.
2. Research course and methodology
In order to study the formation of insoluble complexes between proteins and polyelectrolytes it is necessary to carry out different methodologies in a sequential way.
2.1. Titration curves at different pH in binary systems
The formation of the insoluble polyelectrolyte-protein complexes can be followed by means of turbidimetric titration of the protein with the polyelectrolyte, or vice versa. Taking into account the isoelectric point of the protein and the pK value of the polyelectrolyte, the pH of the medium should be selected so that they have opposite net charge.
Figure 4. shows the turbidimetric titration curve obtained for two systems with different behavior: hyperbolic and sigmoid. Turbidity is usually measured as the absorbance (Abs) at 420 nm.
Figure 4.
Determination of the polyelectrolyter/protein mass ratio when saturation is reached in a A- sigmoid and B- hyperbolic graph
These graphs demonstrate a saturation behavior with different mechanism of complex formation, and allow us to determine the stoichiometric polyelectrolyte/protein ratio “e”, which is defined as the minimal ratio in which the protein precipitates as an insoluble complex. The value “e” is calculated from the plot at the lowest concentration of polyelectrolyte necessary to get the saturation. This value is important because it allows us to determine the minimal amount of polymer needed to fully precipitate the protein, and can be expressed as the number of moles of protein bounded per mol of polyelectrolyte.
2.2. Titration curves at different pH in ternary systems
In ternary systems, the polyelectrolyte forms an insoluble complex with an anion, which associates proteins with opposite net charge. The mixture polyelectrolyte-anion behaves as a pseudo polyampholyte with a characteristic isoelectric point.
The formation of insoluble complexes between the polymer and the anion can be examined by turbidimetric titration of the anion with the polyelectrolyte. When these curves reach the saturation it suggests a complete precipitation of the complex.
The precipitation of polyampholyte -protein complexes is driven by coulombic forces, which are highly dependent on protein and polyampholitic isoelectric pH values [5;17;18]. So, precipitation begins at a critical pH where the attractive forces have just overcome electrostatic repulsion.
2.3. Phase diagrams in binary systems
Phase diagrams, also called solubility curves, show the range of pH in which the complexes are soluble or insoluble. It means that they provide information about the pH of higher interaction between the components and the optimum pH for precipitation and dissolution of the complexes.
To obtain these diagrams, a polyelectrolyte/protein mixture at a ratio close to “e” is titrated with acid or alkali and the turbidity of the medium is measured after pH variation.
Figure 5. shows an schematic phase diagram in a binary system.
2.4. Phase diagrams in ternary systems
Classical polyampholytes have both anionic and cationic groups in their molecules. However, the aqueous solution of any polyelectrolyte may behave as a polyampholyte provided there is a small ion with multiple electrical charges (two or more) in the medium which interacts with the opposite charge of the polyelectrolyte to form a pseudo polyampholyte. Under these conditions, it is possible to find a pH interval where the pseudo complex behaves as an ampholyte.
To obtain the phase diagrams, a mixture with fixed polyelectrolyte/anion ratio is titrated with alkali or acid, and the turbidity of the medium is measured as the absorbance at 420 nm after pH variation.
Figure 5.
Phase diagram, turbidity vs. pH, for protein (—), polyelectrolyte (—) and binary system (—).
Figure 6 shows a schematic phase diagram between a cationic polyelectrolyte and an anion, in different polymer/anion ratios. Figure 6 A shows a pH range where the turbidity of the medium drastically increases. Each curve has a trapezoidal shape with a plateau, and the height of the trapezium depends on the polyelectrolyte concentration. The pHs that correspond to the edges of the trapezium are the critical pH values, at which the transition from complete dissolution to precipitation occurs. The lower critical pH is usually called acidic, and the higher one is called basic. It is remarkable that the transitions from complete solubility to precipitation occur at the same critical pHs independently of the polyelectrolyte concentration.
Also, phase diagrams can be represented as in figure 6.B. This diagram represents the behavior of the polyelectrolyte-anion complex by filled and open circles: filled circles are drawn at the pH of non-zero absorbance whereas the open circles at the zero absorbance values of the solution.
As mentioned above, insoluble polyelectrolyte-anion complexes behave as an ampholyte. This can be used to precipitate cationic or anionic proteins depending on the pH of work, as indicated in figure 6.B.
2.5. Effect of ionic strength
The coulombic component in the interaction between proteins and polyelectrolytes is closely related with the presence of charges. So, the ionic strength of the medium can alter the forces involved in the interaction and eventually leads to dissociation of the complexes.
In ternary systems, high ionic strength can also inhibit polymer-anion interaction.
Whatever the system, this inhibition of the formation of the precipitates may be directly proportional to salt concentration. So, the effect of the presence of salt in the systems can be evaluated by turbidimetric titration in the presence of different concentrations of NaCl in the medium.
Figure 6.
Phase diagram in polyelectrolyte-anion systems. Each color represents a different polyelectrolyte/anion ratio.
2.6. Complex formation kinetics
The interaction between polyelectrolytes and proteins requires time to achieve the maximum quantity of complex (maximum turbidity). Thus, it is necessary a kinetic study by which the turbidity of a mixture polyelectrolyte-protein is measured over time. So, a solution of the polyelectrolyte is added to a solution of the protein, at the pH of precipitation and in an appropriate ratio, and absorbance at 420 nm is measured over time. Finally, a plot of turbidity vs. time is made and the time required to reach the maximum quantity of turbidity is obtained [19].
2.7. Conformational and enzymatic evaluation of the protein in the complex
Several investigations have reported that polymers stabilize the catalytic activity in a variety of enzymes. Besides, it has been suggested that electrostatic interactions between the enzyme and polyelectrolytes play a primary role, also in conformational stabilization [20;21].
2.7.1. Effect of the polyelectrolytes on the far-UV circular dichroism (CD) of proteins
Circular dichroism spectroscopy is a very frequently used technique to evaluate protein conformation in solution. This method is sufficiently simple and allows a rapid determination of protein structure or conformational changes.
In the far-UV region (between 180 and 250 nm) the circular dichroism spectrum provides information one the secondary structure of proteins, due to asymmetrical packing of intrinsically achiral (planar) peptide groups [22].
The effect of polymers on the structure of proteins can be analyzed in terms of its secondary elements. So, far-UV circular dichroism spectra of proteins are recorded in different polymer/protein ratios, with a fixed concentration of protein and varying the amount of polymer. The pH of the medium must be the pH of higher interaction between the protein and the polyelectrolyte.
2.7.2. Effect of the polyelectrolytes on the enzymatic activity of proteins
In order to evaluate the effect of the polyelectrolyte on the enzymatic activity of the protein, enzyme assays are performed at constant protein concentration in the presence of different amounts of polymer. Polyelectrolyte/protein ratios are usually close to the stoichiometry of the complex (“e”) or in excess of polymer respect this value.
The stability of the enzyme in the presence of the polyelectrolyte can also be monitored by incubating the mixture polyelectrolyte/enzyme and recording the enzymatic activity over time.
2.8. Precipitation and redissolution of the complexes
After analyzing the conditions of complex formation or dissolution and evaluating the effects of the different variables, we are able to design a methodology of precipitation of the protein with the polyelectrolyte by following the steps shown in figure 7.:
According to this precipitation scheme, an aliquot of the polyelectrolyte is mixed with a solution of the protein, both prepared at the pH of precipitation, to reach a proper polymer/protein ratio. This mixture is incubated the time necessary to form the maximum quantity of insoluble complex and centrifuged to obtain a solid precipitate. Then, the supernatant is separated and the precipitate redissolved in buffer at the pH of dissolution of the complex. Finally, in order to evaluate the effectiveness of the total process, enzymatic activity is measured in both fractions.
This scheme is successfully applied in many systems [15-20] and allows to obtain a protein with a high recovery and catalytically conserved.
2.9. Calorimetric measurements for polymer-protein complex
2.9.1. Differential scanning calorimetry
Thermal desnaturation of proteins was monitored with a high sensitivity differential scanning calorimeter model VP-DSC from MicroCal Inc. Thermograms were obtained between 20-85°C, at scan rate 25-30ºC/h and at constant pressure of 28 psi. All result were averages of, at least, three independent measurements. Buffer versus buffer baseline scans were determined and subtracted from transition scans prior to normalization and analysis of protein denaturation. Finally, the values of the excess heat capacity were obtained after subtraction of the baseline. The calorimetric data were analysed by using the software ORIGIN 7.0, MicroCal Inc., following the methodology recommended by IUPAC. The parameters obtained from this analysis were: temperature at which maximum heat exchange occurs (Tm), the area under the peak, which represents the enthalpy of transition for reversible process (ΔHcal) and the van´t Hoff enthalpy (ΔHVH).
Figure 7.
Scheme of precipitation of polyelectrolyte/protein complexes
The evaluation of ΔHVH gives an idea of the mechanism of the unfolding process [23]:
ΔHVH = ΔHcal: a two-state process is carried out under equilibrium condition.
ΔHVH > ΔHcal: intermolecular cooperation is taking place which may require some degree of molecular association.
ΔHVH < ΔHcal: one or more intermediate states of significance in the overall process.
However, in some cases this calorimetric criterion may lead to erroneous conclusion.
2.9.2. Isothermal titration calorimetry
Measurements of the examples presented were performed at 20-25 ºC by using a VP-ITC titration calorimeter (MicroCal Inc. USA). The sample cell was loaded with 1.436 mL of protein solution and the reference cell contained Milli-Q grade water. Titration was carried out using a 300 µL syringe filled with polyelectrolyte solutions. The experiments were performed by adding aliquots of 3-5µL of polyelectrolyte solutions 0.175 % (w/w) to the cell containing the protein solution.
The mathematical model equation selected to fit the ITC data was derived from a model that assumes the polyelectrolyte molecule binding to several protein molecules, all with the same intensity; in other words, the polyelectrolyte was considered as a macromolecule having n independent and equivalent sites, all of which have the same affinity constant, K, for the ligand (protein) [24].
The heat associated with the interaction polyelectrolyte-protein (ΔHb) was calculated by subtraction using the equation 3:
ΔHb=ΔHt−ΔHd−ΔHdissolE3
Where ΔHt is the total heat associated to each polymer addition, ΔHd is the heat of dilution of the polyelectrolyte in the buffer in the absence of the protein and ΔHdissol is the heat of polymer dissolution. The heat associated to the dilution of the protein in buffer was negligible. Then ΔHb was plotted vs polyelectrolyte/protein molar ratio and, by non-linear fitting of these calorimetric curve, the affinity constant (K) for the polyelectrolyte binding to the protein and the number of polymer molecules (n) bound per protein molecule was calculated using the software provided by the instrument.
The resulting data set was fitted using MicroCal ORIGIN 7.0 software supplied with the instrument and the intrinsic molar enthalpy change for the binding, ΔHb, the binding stoichiometry, n, and the intrinsic binding constant, K, were thus obtained. The equation for determining the heat associated to each injection is:
Q=nMt∆HbVo21+1nkMt+XtnMt-1+1nkMt+XtnMt2-4XtnMtE4
\n\t\t\t\t\t
where Vo is the active volume cell, Xt is the bulk concentration of ligand and Mt is the bulk concentration of the macromolecule in V0 [25].
The intrinsic molar free energy change, ΔGº, and the intrinsic molar entropy change, ΔSº, for the binding reaction were calculated by the fundamental thermodynamic equations 5 and 6:
∆G°=-RTlnKE5
∆S°=∆H°-∆G°TE6
3. Results
3.1. Turbidimetric titration curves
Figure 8 shows typical hyperbolic titration curves of a protein with a polyelectrolyte. In this case, trypsin (TRP) with poly vinyl sulfonate (PVS) [26]. As can be seen, two important characteristics were observed: at low polymer/protein ratios, absorbance increases with an increase in the polyelectrolyte total concentration and, at high polyelectrolyte/protein ratio, there is a plateau which depends on the medium pH.
The protein/polyelectrolyte molar ratio which corresponds to the situation where the protein has been precipitated as an insoluble complex was calculated from the intersection of a straight line which corresponds to the prolongation of the linear zone of the curve (at low polymer concentration) with a line which gives a plateau.
Trypsin is a serin-protease found in the digestive system. It is used for numerous biotechnological processes. Its isoelectric point is between 11.0 and 11.4 [27]. The pHs selected in the curves were chosen in the range where TRP and PVS have opposite charges.
Figure 8.
Turbidimetric titration curves of TRP (70µM) solution with PVS (0.25 % w/w) in a medium with phosphate buffer 50mM, pH 3.0 (●), 5.5 (▲) and 7.0 (■). T=20 ºC, [21].
Table 1 shows the molar protein-polyelectrolyte ratio which corresponds to the stoichiometry of the complex formation calculated from the titration curves for the different experiments. These values are important because they allow us to calculate the minimal polymer amount necessary to precipitate the protein in a complete form. The data have been expressed as the number of TRP moles bound per polyelectrolyte mol. Despite the fact that these values were similar, turbidity is much higher at pH 3.00 which suggest a major size of the precipitate particle.
pH
Protein/polyelectrolyte molar ratio
3.00
136 ± 3
5.50
228 ± 21
7.00
147 ± 12
Table 1.
TRP/PVS molar ratios at different pHs.
Figure 9 shows titration curves of lysozyme (LYZ) with the polyelectrolyte PVS. LYZ is a basic protein with 19 amino residues, an isoelectrical pH between 11.0 and 11.4 and a molecular mass of 14.3 kDa [28], therefore at the pHs where the turbidimetry titration were assayed the protein has a net positive electrical charge. Formation of LYZ-PVS complex was observed to be influenced by the medium pH, however, at pH 3.1, a minor absorbance maximum value was observed than at pH 5.5, which can be assigned to the loss of the native structure of this protein by influence of the acid medium [26].
Table 2 shows the molar protein-polymer ratios which correspond to the stoichiometry of the complex formation calculate from the titration curves for the different experiments. These values are important because allow to estimate the minimal polyelectrolyte amount needed to precipitate the protein, the data have been expressed as the number of LYZ molecules bound per polyelectrolyte molecule.
Figure 9.
Turbidimetric titration curves of LYZ (0.3mg/mL) solution with PVS in a medium with 50 mM phosphate buffer. pH 5.5 (▲), 7.0 (●), and acetic acid/acetate buffer pH 3.1 (■). T= 20 ºC.
LYZ- PVS
Protein/polyelectrolyte molar ratio
pH 3.1
66
pH 5.5
47
pH 7.0
23
Table 2.
Lys/PVS molar ratios at different pHs.
3.2. Turbidimetric titration of ternary complex:
Figure 10 shows turbidimetric titration curves when phosphate (500mM) or citrate (50mM) was titrated by adding a concentrated solution of the polyelectrolyte poly ethylene imine (PEI). Both curves reached a plateau at high polyelectrolyte anion ratios, which suggests a complete precipitation of the complex. It could be seen that the plateau was obtained at a polymer/anion ratio 10 times higher for citrate than for phosphate, suggesting that citrate has a greater precipitation capacity than phosphate. These ternary systems have the capability to precipitate in the absence of protein. Only is required the presence in the medium of the cationic polyelectrolyte (PEI) and a polyanion like phosphate (Pi) or citrate (Cit).
3.3. Phase diagrams of binary systems
Figures 11 show the absorbance dependence (at 420 nm) vs. the pH change by the system LYS with poly acrylate (PAA). These complexes were soluble at basic pH values. At pH lower than 6.50 a significant increase in the turbidity was observed that corresponding to the insoluble complex formation. Similar behavior was reported for the serum albumin titration with anionic polyelectrolyte [7].
The relevance of these phase diagrams are in the possibility to know the insolubility and solubility complex conditions.
Figure 10.
Turbidimetric titration of phosphate (▲) and citrate (●) with PEI. pH 5.5. T= 20º C [6].
Figure 11.
Dependence of the absorbance at 420 nm vs the medium pH at a constant protein-polyelectrolyte molar ratio of LYZ-PAA: (●) 0.0027, (■) 0.0065, (▲) 0.0010. T= 20ºC [25].
3.4. Phase diagrams of ternary systems
Figure 12 shows the pH variation effect on the insoluble complex formation obtained for ternary systems PEI/Pi at different PEI/Pi molar ratios [6]. As can be seen, in all curves there is an increase in the turbidity of the medium, reaching a maximum value and then decreasing in the pH interval 3.5-7. Each curve has a trapezoidal shape and the pH values corresponding to the edges of the trapezium are the critical pHs at which the transition from complete dissolution to precipitation occurs.
In this figure it can be identify both critical pHs: 3.5 and 7. At pH=3.5 the net charge of the complex is positive whereas at pH= 7 is negative. On the other hand, transitions from complete solubility of the insoluble complex are independent of the polyelectrolyte concentration.
Figure 12.
Phase diagram of PEI/Pi systems at different molar ratios.
3.5. Effect of ionic strength
In general, protein/polyelectrolyte insoluble complexes are greatly affected by ionic strength because the molecular mechanism of the interaction is mainly electrostatic in nature. Turbidimetric titrations at pH 7.00 were performed in medium of different ionic strength such as shown Figure. 13. In this case, only 0.1 M of NaCl is enough to avoid formation the insoluble protein-polyelectrolyte complex [26]. This finding may be interesting in the design of an isolation method of protein, allowing in a first step the precipitation by the polyelectrolyte and then the precipitate may be dissolved by NaCl solution addition at low concentration.
Ternary systems like PEI-citrate was dramatically affected by 0.5 for higher ionic strength; in this case, no formation of the insoluble complex was found while the PEI-phosphate system showed to be slightly affected by the NaCl increased concentration. The inhibition of the precipitate formation in both systems was directly proportional to the salt concentration, in agreement with the presence of an important coulombic component in the insoluble complex formation [19].
3.6. Kinetics of the complex formation
In general, the kinetics of complex formation is fast (around 2-10 minutes) [15;17;19]. Figure 14 shows the kinetic studies of different molar ratios of the systems TRP/Eudragit®L100 (EL100). It required less than 2 minutes of incubation to achieve the maximum quantity of complexes. In addition, by increasing the polyelectrolyte concentration increases the turbidity of the system, however the time required achieving the maximum turbidity is independent of the concentration of the molar ratio.
Figure 13.
NaCl concentration effect on the turbidity of LYZ-PAA, pH 7.0, NaCl concentration: (O) 0M, (■) 0.1 M and (▲) 0.5M. T= 20ºC.
Figure 14.
Formation of complex TRP-EL100 through time at three protein/polyelectrolyte molar ratio of TRP/EL100: (──) 32.41, (─ ─) 16.18, ( ) 8.08. [15].
4. Calorimetric techniques of protein-polyelectrolyte complex
4.1. Differential scanning calorimetry by polymer-protein complex
DSC is a useful tool for studying the protein unfolding in which values of excess specific heat capacity (Cp) are obtained as a function of temperature. Two enzymes having different behavior towards charged flexible chain polyelectrolytes are analyzed below.
Lysozyme is a basic protein with 19 amino residues, an isoelectrical pH between 11.0 to 11.4 and a molecular mass of 14.3 kDa. Because LYZ is one of the four proteins whose thermal denaturation is thermodynamically reversible, the equations for systems in thermodynamic equilibrium can be applied to obtain the thermodynamic functions (entropy and enthalpy of unfolding) directly from the thermograms, as described by Privalov [29].
Thermograms of LYS enzyme with PAA and PVS are presented as examples in figure 15 and Table 3 shows the thermodynamics functions and Tm obtained in each case. In these systems DSC measurements demonstrated that the Tm of LYS was not modified by the polyelectrolytes presence only a decrease in the denaturalization heat (ΔHcal) was observed.
Figure 15.
DSC Thermograms of the LYZ in the absence (—) and presence of: PVS (----) and PAA (….) pH 7.00.
LYZ
LYZ-PVS
LYZ -PAA
ΔHcal (kcal/ mol)
89.4 ± 0.3
72.0 ± 0.3
66.7 ± 0.4
ΔHVH (kcal/ mol)
139.0 ± 0.6
141 ± 0.8
151 ± 1.0
ΔH VH / ΔH cal
1.55 ± 0.05
1.96 ± 0.01
2.26 ± 0.03
Tm (ºC)
75.01 ± 0.01
75.33 ± 0.02
75.2 ± 0.1
ΔS (e.u.)
399 ± 3
405 ± 4
405 ± 5
Table 3.
Thermodynamic functions obtained for the thermal LYZ unfolding determined by DSC in the absence and presence of the studied polyelectrolytes.
A Tm constant value is a proof that the protein retains its thermodynamic stability in the presence of both polyelectrolytes. However the polymer presence induced a decrease in the area under the curves, in agreement with a diminution of the heat associated to the denaturation process. The unfolding entropic change showed to be not affected by the polyelectrolyte presence, in accordance with the protein retaining its tertiary structure and no important conformational protein change is occurring.
LYZ is a protein which has only one domain with low molecular mass, its thermal unfolding have been describe as reversible, however the capacity of LYZ to associate in aqueous solution it is well known. ΔHVH/ΔHcal ratio greater than 1 is an indication of the intermolecular cooperation presence during the thermal unfolding. The increase of this ratio in the polyelectrolytes presence, suggests more cooperative intermolecular process.
Furthermore, the unfolding entropy was not affected in the protein-polymer complexes (LYZ-PVS and LYS-PAA). It indicates that LYZ in complex follows in the same conformational state that LYZ alone.
Trypsin is a serin-protease found in the digestive system. It is used for numerous biotechnological processes. It is a globular protein which has two domains with similar structures [27]. DSC experimental results for enzyme trypsin are demonstrated a two-state transition model at pH 3.00 [30]. Figure 16.A shows DSC thermograms of TRP. Although the ratio ΔHVH/ ΔHcal is close to 1, however the thermogram clearly shows 3 transitions.
TRP-EL100 complex has a very interesting behavior. As can be seen in Figure 16.B protein thermogram was significantly modified by the polyelectrolyte presence.
Figure 16.
A) DSC Thermogram of the TRP: (—) experimental data; (---) fit data; (∙∙ ─) first transition; (- - -) second transition; (─ ─) third transition. (B) DSC Thermogram of the TRP in the presence of EL100: (—) experimental data; (---) fit data.
Tm (K)
ΔHcal (kcal/mol)
ΔHVH (kcal/mol)
ΔHVH/ ΔHcal
TRP
320.6 ± 0.1
38.7 ± 0.6
42.2 ± 0.8
1.09
TRP (transitions)
316.1 ± 0.1 324.4 ± 0.3 336.4 ± 0.3
13.9 ± 0.1 22.2 ± 0.2 1.8 ± 0.5
8.3 ± 3 53.1 ± 3 -
-
TRP-EL100
327.8 ± 0.1
82.0± 0.1
81.6± 0.1
0.99
Table 4.
Thermodynamics functions obtained for the thermal TRP unfolding determined by DSC in the absence and presence of the EL100.
The comparison of the two figures and table evidences two main differences
Tm of the TRP curve is 320.6 K (47.5°C), whereas for the TRP-EL100 complex the same parameter is 327.8 K (54.6°C). The shift of the Tm of TRP in the presence of the polymer means that the EL100 stabilizes the structure of the enzyme against thermal denaturation.
The different unfolding model in the absence (3 transitions of independent domains) and in the presence of polymer (two-state model)
4.2. Isothermal titration calorimetry
ITC technique gives the direct heat associated to the complex formation (ΔH), a number of protein molecules bounded to polyelectrolyte molecule (n), the affinity constant (K). Before performed ITC experiment is important to known which is the number “e“ obtained by turbidimetric titration because is a good estimation of n.
Figure 17 shows the ITC measurements of the LYS titration with PVS and Table 5 summarizes the parameters obtained by two anionic polyelectrolytes (PVS and PAA).
Figure 17.
ITC measurements of LYZ with PVS [26].
System
LYZ-PVS
LYZ -PAA
n (protein /polyelectrolyte)
21.2 ± 0.2
294 ± 8
K (M-1)
2.7 103
5.1 104
ΔHº (kcal/mol)
- 15.2
- 10.0
ΔSº (e.u. )
1103
1033
Table 5.
Thermodynamic and binding parameters of the interaction LYZ-polyelectrolyte from ITC experiments.
The interaction LYZ-PVS and LYZ-PAA is exothermic. The mechanism of bond is carried out between the electrically charged groups of both. The differences found between complexes were the affinity (K) and the number of molecules of protein bonded to polymer molecule. Because the size of the polyelectrolytes are 10-fold larger than the protein, the number of protein molecules bound per polymer molecule is high.
The heat associated to the complex formation were extremely high, but when they are normalized per protein molecule bound to the polyelectrolyte the heat associate yielded 10-15 kcal/mol which is a normal heat amount for a coulombic interaction between two charge groups in solution. These low interaction heats are in agreement with the low NaCl concentration needed to induces the dissolution of the insoluble complex (around 0.1 M) Other important parameters to know are the thermodynamically stability of the protein in the polyelectrolyte presence. It is desirable that the protein retains its tertiary structure.
TRP- EL100 complex is an interesting example. Although the polymer and protein present opposite electrical charge, however the interaction is endothermic.
Figure 18 shows the binding isotherm obtained when consecutive aliquots of EL100 were added to a solution of trypsin [15]. The parameters calculated are summarized in Table 6.
Figure 18.
ITC measurements of TRP with EL100.
Binding parameter
Value
n ( molar ratio) [mol TRP/mol EL-100]
15.22 ± 0.05
K (affinity constant) [M-1]
9.8 106 ± 7. 105
ΔH° (kcal/mol)
62.1 ± 0.3
ΔS°(e.u.)
240 ± 10
ΔG° (kcal/mol)
- 9.59 ± 0.05
Table 6.
Binding parameters of the TRP- EL100 interaction from ITC experiments.T= 25°C.
A value of 15 mol of protein per mol of polyelectrolyte was found for the complex EL100-TRP formation. The high value of the affinity constant demonstrated that both molecules interact strongly with each other. The ΔH was normalized per mol of protein; therefore, heat value of 62.14 Kcal/mol of protein is yielded. The positive value of ΔH indicates that the interaction between EL100 and TRP requires consuming of heat form de medium. The ΔS° value obtained was positive as a result of the increase of the disorder of the system due to release of structured water molecules.
EL100 is a charged polymer which also contains a hydrophobic framework in its linear chain. For such a complicated system it is not clear to what extent non-electrostatic forces contribute to the observed complexation behavior. Besides, the value of ΔS° was positive indicating that the disorder of the system increased.
ITC experiment performed in presence of NaCl confirmed the results obtained by turbidimetry (data not shown). The values of heat measured during the experiment of titration are similar that obtained when studying the dilution of the polyelectrolyte. This result is indicating that the TRP and the EL100 are not interacting when NaCl 1.00 M is added to the buffer.
Thermodynamic parameters were according to hydrophobic interactions between TRP and EL100. However, ITC and turbidimetric titrations experiments were altered in salt presence. It would demonstrate that the mechanism of interaction between these two molecules involves both hydrophobic and electrostatic interactions.
5. Conclusions
Experimental conditions of charged polyelectrolyte-protein complex formation may be determined by turbidimetric measurements, but are necessary to complement it for calorimetric techniques.
DSC measurements show that the Tm and denaturalization heat of some proteins may increase or not change in the polymer presence and the complex unfolded according to a two-state model.
In general, ΔH° and ΔS° of complex formation obtained by ITC have negative when protein and polyelectrolyte are oppositely charged (electrostatic interaction). Nevertheless, the thermodynamic functions can be positive as a result of the interaction between hydrophobic backbone of polymers and aromatic amino acids. Moreover, if ionic strength modifies this insoluble complex formation, a mechanism of interaction may involve both hydrophobic and electrostatic interactions.
The calorimetric techniques (ITC and DSC), turbidimetry and enzymatic activity studies provide useful quantitative information about the interaction of proteins and charged polyelectrolytes in aqueous solution. The knowledge of the nature of this interaction is essential for the application of the complex formation in protocols as proteins isolation strategy, immobilization or in purification of a target protein.
Acknowledgement
We thank Prof Watson Loh, Institute of Chemistry, State University of Campinas (UNICAMP), Campinas, SP, BRAZIL for performing DSC and ITC measurements. We also thank Prof. G. Picó, Prof. B. Nerli and Prof. B. Farruggia for useful discussions.
\n',keywords:null,chapterPDFUrl:"https://cdn.intechopen.com/pdfs/42253.pdf",chapterXML:"https://mts.intechopen.com/source/xml/42253.xml",downloadPdfUrl:"/chapter/pdf-download/42253",previewPdfUrl:"/chapter/pdf-preview/42253",totalDownloads:2981,totalViews:399,totalCrossrefCites:1,totalDimensionsCites:5,totalAltmetricsMentions:0,impactScore:2,impactScorePercentile:77,impactScoreQuartile:4,hasAltmetrics:0,dateSubmitted:"November 21st 2011",dateReviewed:"October 11th 2012",datePrePublished:null,datePublished:"January 23rd 2013",dateFinished:"January 23rd 2013",readingETA:"0",abstract:null,reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/42253",risUrl:"/chapter/ris/42253",book:{id:"2519",slug:"applications-of-calorimetry-in-a-wide-context-differential-scanning-calorimetry-isothermal-titration-calorimetry-and-microcalorimetry"},signatures:"Diana Romanini, Mauricio Javier Braia and María Cecilia Porfiri",authors:[{id:"141993",title:"Dr.",name:"Diana",middleName:null,surname:"Romanini",fullName:"Diana Romanini",slug:"diana-romanini",email:"dianaromanini@hotmail.com",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:null},{id:"143343",title:"Mr.",name:"Mauricio",middleName:null,surname:"Braia",fullName:"Mauricio Braia",slug:"mauricio-braia",email:"mauriciobraia@conicet.gov.ar",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:null},{id:"143344",title:"Ms.",name:"María",middleName:null,surname:"Porfiri",fullName:"María Porfiri",slug:"maria-porfiri",email:"ceciliaporfiri@conicet.gov.ar",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",institution:null}],sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_1_2",title:"1.1. Formation of the protein-polyelectrolyte complex",level:"2"},{id:"sec_2_2",title:"1.2. Stoichiometry of the protein-polyelectrolyte formation",level:"2"},{id:"sec_3_2",title:"1.3. Biotechnological applications of the protein-polyelectrolyte complex",level:"2"},{id:"sec_3_3",title:"1.3.1. Bioseparation of proteins from a complex mixture",level:"3"},{id:"sec_4_3",title:"1.3.2. Enzyme immobilization",level:"3"},{id:"sec_6_2",title:"1.4. Characterization of the protein-polyelectrolyte complex",level:"2"},{id:"sec_8",title:"2. Research course and methodology",level:"1"},{id:"sec_8_2",title:"2.1. Titration curves at different pH in binary systems",level:"2"},{id:"sec_9_2",title:"2.2. Titration curves at different pH in ternary systems",level:"2"},{id:"sec_10_2",title:"2.3. Phase diagrams in binary systems",level:"2"},{id:"sec_11_2",title:"2.4. Phase diagrams in ternary systems",level:"2"},{id:"sec_12_2",title:"2.5. Effect of ionic strength ",level:"2"},{id:"sec_13_2",title:"2.6. Complex formation kinetics",level:"2"},{id:"sec_14_2",title:"2.7. Conformational and enzymatic evaluation of the protein in the complex",level:"2"},{id:"sec_14_3",title:"2.7.1. Effect of the polyelectrolytes on the far-UV circular dichroism (CD) of proteins",level:"3"},{id:"sec_15_3",title:"2.7.2. Effect of the polyelectrolytes on the enzymatic activity of proteins",level:"3"},{id:"sec_17_2",title:"2.8. Precipitation and redissolution of the complexes",level:"2"},{id:"sec_18_2",title:"2.9. Calorimetric measurements for polymer-protein complex",level:"2"},{id:"sec_18_3",title:"2.9.1. Differential scanning calorimetry",level:"3"},{id:"sec_19_3",title:"2.9.2. Isothermal titration calorimetry",level:"3"},{id:"sec_22",title:"3. Results",level:"1"},{id:"sec_22_2",title:"3.1. Turbidimetric titration curves ",level:"2"},{id:"sec_23_2",title:"3.2. Turbidimetric titration of ternary complex: ",level:"2"},{id:"sec_24_2",title:"3.3. Phase diagrams of binary systems",level:"2"},{id:"sec_25_2",title:"3.4. Phase diagrams of ternary systems ",level:"2"},{id:"sec_26_2",title:"3.5. Effect of ionic strength",level:"2"},{id:"sec_27_2",title:"3.6. Kinetics of the complex formation ",level:"2"},{id:"sec_29",title:"4. Calorimetric techniques of protein-polyelectrolyte complex",level:"1"},{id:"sec_29_2",title:"4.1. Differential scanning calorimetry by polymer-protein complex",level:"2"},{id:"sec_30_2",title:"4.2. Isothermal titration calorimetry ",level:"2"},{id:"sec_32",title:"5. Conclusions",level:"1"},{id:"sec_32_2",title:"Acknowledgement",level:"2"}],chapterReferences:[{id:"B1",body:'KumaraA Srivastavaa A, Yu Galaevb I, Mattiasson B, (2007Smart polymers: Physical forms and bioengineering applications. Progress in Polymer Science 3212051237\n\t\t\t'},{id:"B2",body:'WangYGaoYDubinP1999Protein Separation via Polyelectrolyte Coacervation: Selectivity and EfficiencyBiotechnology Progress12356362'},{id:"B3",body:'ArvindLArunaNRoshnnieJDevikaT2000Reversible precipitation of proteins on carboxymethyl cellulosePoocess Biochemistry 35777785'},{id:"B4",body:'WeinbreckFDe VriesRSchrooyenPDe KruifC. G2003Complex Coacervation of Whey Proteins and Gum Arabic,Biomacromolecules4293303'},{id:"B5",body:'GuptaVNathSChandS2002Estimation of proteins in the presence of polyethylenimineBiotechnol. Lett., 22: 927 EOF929 EOF'},{id:"B6",body:'ManzurASpelziniDFarruggiaBRomaniniDPicóG2007Polyethyleneimine phosphate and citrate systems act like pseudo polyampholytes as a starting method to isolate pepsinJournal of Chromatography B8606368'},{id:"B7",body:'MattisonK. WDubinP. LBrittainI. J1998Complex Formation between Bovine Serum Albumin and Strong Polielectrolytes: Effect of Polymer Charge Density, Journal of Physical Chemistry B, 10238303836'},{id:"B8",body:'CooperCDubinPKayitmazerATurksenSCurrent, (2005Polyelectrolyte-protein complexes Opinion in Colloid & Interface Science 105278'},{id:"B9",body:'Pessoa JrA.; Vahan Kilikian, B.;Purificação de Produtos Biotecnológicos, Ed. Manole Ltda., cap. 2. (2005'},{id:"B10",body:'HilbrigFFreitagR2003Protein purification by affinity precipitation,J Chrom B 7907990'},{id:"B11",body:'ArroyoM1998Inmobilized enzymes: Theory, methods of study and applications. Ars Pharmaceutica, 392339'},{id:"B12",body:'KrajewskaB2004Application of chitin- and chitosan-based materials for enzyme immobilizations: a review Enzyme Microb Tech 35126139'},{id:"B13",body:'Saskia Lindhoud2009Polyelectrolyte Complex Micelles as Wrapping for enzymesTesis, 206 p.\n\t\t\t'},{id:"B14",body:'EspositoECervellatiFMenegattiENastruzziCCortesiR2002Spray dried Eudragit microparticles as encapsulation devices for vitamin C,Int J Pharm 242329334'},{id:"B15",body:'BraiaM Tubio, G Nerli, B Loh W, Romanini, D., (2012Analysis of the interactions between eudragit® l100 and porcine pancreatic trypsin by calorimetric techniques. Int J Biol Macromol 50180186'},{id:"B16",body:'PorfiriM. CPicóGFarruggiaBRomaniniD2010Insoluble complex formation between alpha-amylase from Aspergillus oryzae and polyacrylic acid of different molecular weightProc. Biochem. 4517531756'},{id:"B17",body:'TsuboiAIzumiTHirataMJXiaPDublinEKokufuta1999Complexation of Proteins with a Strong Polyanion in an Aqueous Salt-free System Langmuir 1262956303'},{id:"B18",body:'FornasieroFUlrichJPrausnitzJ1999Molecular thermodynamics of precipitationChem. Eng. Process 38463475'},{id:"B19",body:'PatrickiosCSharmaLArmesSBillinghamN1999Precipitation of a Water-Soluble ABC Triblock Methacrylic Polyampholyte: Effects of Time, pH, Polymer Concentration, Salt Type and Concentration, and Presence of a Protein. Langmuir 1516131620'},{id:"B20",body:'ForemanTKhalilMMeierPBrainardJVanderbergLSauerN2001Effects of charged water-soluble polymers on the stability and activity of yeast alcohol dehydrogenase and subtilisin carlsberg.Biotechnol Bioeng 76241246'},{id:"B21",body:'BraiaMPorfiriM. CFarruggiaBPicóGRomaniniD2008Complex formation between protein and poly vinyl sulfonate as a strategy of proteins isolation. Journal of Chromatography B, 873139143'},{id:"B22",body:'FasmanG. D1996Circular dichroism and the conformational analysis of biomoleculesPlenum press 738p.'},{id:"B23",body:'SturtevantJ2001Biochemical applications of differential scanning calorimetryAnnu. Rev. Phys. Chem. 38463'},{id:"B24",body:'JhaNKishoreN2009Binding of streptomycin with bovine serum albumin: Energetics and conformational aspects.Thermochim. Acta 4822129'},{id:"B25",body:'KimWYamasakiYKataokaK2006Development of a Fitting Model Suitable for the Isothermal Titration Calorimetric Curve of DNA with Cationic Ligands.J. Phys. Chem. B 1101091910925'},{id:"B26",body:'RomaniniDBraiaMGiatte Angarten R, Loh W, Picó G, (2007Interaction of lysozyme with negatively charged flexible chain polymersJ Chrom B, 8572531'},{id:"B27",body:'BeynonRBondJ. SProteolytic Enzymes, Practical Approach, Oxford University Press, 2001'},{id:"B28",body:'AschaffenburgRBlakeCDickieHGayenSKeeganRSenA1980The crystal structure of tortoise egg-white lysozyme at 6 Å resolution.Biochim Biophys Acta 6256471'},{id:"B29",body:'PrivalovP. L1979Stability of Proteins Small Globular Proteins.Adv. Protein Chem. 33167241'},{id:"B30",body:'SantosASantanaMGomideaFMirandaAOliveiraJVilas Boas F., Vasconcelos, A., Bemquerer M.,Santoro M., (2008Physical-chemical characterization and stability study of alpha-trypsin at pH 3.0 by by differential scanning calorimetry Int. J. Biol.Macromol. 42278284'}],footnotes:[],contributors:[{corresp:null,contributorFullName:"Diana Romanini",address:null,affiliation:'
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Hybrids",slug:"effects-of-morphometric-indicators-on-incubation-values-of-eggs-and-sex-of-the-chicks-of-the-light-h",abstract:"The aim of this study was to establish incubation values of eggs (egg fertilization, absolute and relative embryo mortality, and hatchability of male and female chicks), morphometric indicators (preincubation egg mass; length, width, and egg shape index; hatched female and male chicken mass and their relative share in the egg mass before incubation), and the phenotype correlation between some traits in the younger parent flock (YF33—33 weeks) and the older flock (OF49—49 weeks) of the light Institut de Sélection Animale (ISA) Brown hybrid. With regard to incubation values, the younger flock (YF33) demonstrated better incubation results than the older flock (OF49). The egg fertilization rate was 95.24 and 94.22%, respectively, chick hatchability as the percentage of the total of incubated eggs was 86.51 and 84.89%, respectively, and chick hatchability as the percentage of the total of fertilized eggs was 90.83 and 90.09%, respectively. Embryo mortality rate was 8.73 and 9.17% (YF33), and 9.33 and 9.91% (OF49). Regardless of the parent flock age, eggs that hatched female chicks had lower values of observed morphometric traits than those that hatched male chicks, except for the egg shape index (77.49–77.47%, respectively) which was higher by 0.02% in eggs which hatched female chicks, but this difference was not statistically significant (P > 0.05). Contrary to effects of the chick sex, the parent flock age had considerably larger effect on observed morphometric traits, as all morphometric indicators of eggs and hatched chicks of both sexes in the older flock (OF59) had statistically significantly higher values (P < 0.001) than in the younger flock (YF33). The only exception is the relative share of the chicken in the egg mass where the measured difference (−0.03%) was not statistically significant (P > 0.05). The phenotype correlation coefficients determined (rp) between the egg mass before the incubation period and the egg shape index were statistically significant (P < 0.01; P < 0001), except between the egg mass of eggs which hatched female chicks and the egg shape index in the young flock (YF33), whereby the calculated coefficient (rxy = 0.107) was not statistically confirmed (P > 0.05). Furthermore, the egg mass and hatched chicken mass of both sexes increased with the age of the parent flock, and statistically significant absolute phenotype correlation (P < 0.001) was determined between these two indicators.",signatures:"Milena Milojević, Živan Jokić and Sreten Mitrović",authors:[{id:"304335",title:"Dr.",name:"Milena",surname:"Milojević",fullName:"Milena Milojević",slug:"milena-milojevic",email:"milojevic.milena23@gmail.com"},{id:"305032",title:"Prof.",name:"Sreten",surname:"Mitrović",fullName:"Sreten Mitrović",slug:"sreten-mitrovic",email:"mitrovic@agrif.bg.ac.rs"},{id:"309958",title:"Prof.",name:"Živan",surname:"Jokić",fullName:"Živan Jokić",slug:"zivan-jokic",email:"zivjokic@agrif.bg.ac.rs"}],book:{id:"8699",title:"Animal Models in Medicine and Biology",slug:"animal-models-in-medicine-and-biology",productType:{id:"1",title:"Edited Volume"}}}],collaborators:[{id:"179622",title:"Dr.",name:"Georg",surname:"Schmolzer",slug:"georg-schmolzer",fullName:"Georg Schmolzer",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/179622/images/system/179622.jpeg",biography:"Dr. Schmölzer is the inaugural Heart and Stroke Foundation/University of Alberta Professor of Neonatal Resuscitation and the Director of the Center for the Studies on Asphyxia and Resuscitation (CSAR) in Edmonton. He also works as a Neonatologist at the Royal Alexandra Hospital. Dr. Schmölzer obtained his MD, Ph.D. and clinical training in Austria and Australia. In 2014 he completed a Banting Postdoctoral Fellowship at the University of Alberta. \r\nDr. Schmölzer’s research focuses to i) understand physiological changes during fetal to neonatal transition, ii) improve diagnoses, mitigate risk and improve survival and quality of life for newborns, iii) use of emerging technologies during neonatal resuscitation, and iv) examine how these physiological changes can be used to improve short- and long-term outcomes of newborn babies.",institutionString:"University of Alberta",institution:{name:"University of Alberta",institutionURL:null,country:{name:"Canada"}}},{id:"179805",title:"Dr.",name:"Po-Yin",surname:"Cheung",slug:"po-yin-cheung",fullName:"Po-Yin Cheung",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Alberta",institutionURL:null,country:{name:"Canada"}}},{id:"179806",title:"Dr.",name:"Megan",surname:"O'Reilly",slug:"megan-o'reilly",fullName:"Megan O'Reilly",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Alberta",institutionURL:null,country:{name:"Canada"}}},{id:"300121",title:"Prof.",name:"Marcela",surname:"Capcarova",slug:"marcela-capcarova",fullName:"Marcela Capcarova",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Slovak University of Agriculture",institutionURL:null,country:{name:"Slovakia"}}},{id:"301719",title:"Dr.",name:"Marie Noelle",surname:"Giraud",slug:"marie-noelle-giraud",fullName:"Marie Noelle Giraud",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Fribourg",institutionURL:null,country:{name:"Switzerland"}}},{id:"301720",title:"MSc.",name:"Aurélien",surname:"Frobert",slug:"aurelien-frobert",fullName:"Aurélien Frobert",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Fribourg",institutionURL:null,country:{name:"Switzerland"}}},{id:"301721",title:"Prof.",name:"Stéphane",surname:"Cook",slug:"stephane-cook",fullName:"Stéphane Cook",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Fribourg",institutionURL:null,country:{name:"Switzerland"}}},{id:"301723",title:"BSc.",name:"Guillaume",surname:"Ajalbert",slug:"guillaume-ajalbert",fullName:"Guillaume Ajalbert",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Fribourg",institutionURL:null,country:{name:"Switzerland"}}},{id:"301724",title:"BSc.",name:"Jeremy",surname:"Valentin",slug:"jeremy-valentin",fullName:"Jeremy Valentin",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Fribourg",institutionURL:null,country:{name:"Switzerland"}}},{id:"306704",title:"Dr.",name:"Tze-Fun",surname:"Lee",slug:"tze-fun-lee",fullName:"Tze-Fun Lee",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Alberta",institutionURL:null,country:{name:"Canada"}}}]},generic:{page:{slug:"authorship-policy",title:"Authorship Policy",intro:'
',metaTitle:"Authorship Policy",metaDescription:"IN TECH's Authorship Policy is based on ICMJE criteria for authorship. In order to be identified as an Author, one must:",metaKeywords:null,canonicalURL:"/page/authorship-policy",contentRaw:'[{"type":"htmlEditorComponent","content":"
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Substantially contribute to the conception or design of the work; or the acquisition, analysis, or interpretation of data for the work
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Participate in drafting or revising the work
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Approve the final version of the work to be published.
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All contributors who meet these criteria are listed as Authors. Their exact contributions should be described in the manuscript at the time of submission.
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Conversely, all contributors who do not meet these criteria should be listed in the Acknowledgments section of the manuscript, along with a short description of their specific contributions.
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CHANGES IN AUTHORSHIP
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If it is felt necessary to make changes to the list of Authors after a manuscript has been submitted or published, it is the responsibility of the Author concerned to provide a valid reason to amend the published list. Additionally, all listed Authors must verify and approve the proposed changes in order for any amendments to be made.
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AFFILIATION
\\n\\n
Authors are responsible for ensuring all addresses and emails provided are correct. Under affiliation(s) all Authors should indicate where the research was conducted. Please note that no changes to the affiliation(s) can be made after the chapter has been published.
Substantially contribute to the conception or design of the work; or the acquisition, analysis, or interpretation of data for the work
\n\t
Participate in drafting or revising the work
\n\t
Approve the final version of the work to be published.
\n
\n\n
All contributors who meet these criteria are listed as Authors. Their exact contributions should be described in the manuscript at the time of submission.
\n\n
Conversely, all contributors who do not meet these criteria should be listed in the Acknowledgments section of the manuscript, along with a short description of their specific contributions.
\n\n
CHANGES IN AUTHORSHIP
\n\n
If it is felt necessary to make changes to the list of Authors after a manuscript has been submitted or published, it is the responsibility of the Author concerned to provide a valid reason to amend the published list. Additionally, all listed Authors must verify and approve the proposed changes in order for any amendments to be made.
\n\n
AFFILIATION
\n\n
Authors are responsible for ensuring all addresses and emails provided are correct. Under affiliation(s) all Authors should indicate where the research was conducted. Please note that no changes to the affiliation(s) can be made after the chapter has been published.
\n\n
Policy last updated: 2017-05-29
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On September, 29th 2006 he has won a post PhD fellowship from the university of Bologna (from October 2006 to October 2008), at the competitive examination he was ranked first in the industrial engineering area. He extensively served as referee for several international journals. He is author/coauthor of more than 100 research papers. He has been involved in some projects supported by MURST and European Community. 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From 1985 to 1986, he was a Research Fellow in the Research Institute for Electronic Equipment, ZZU AD, Plovdiv, Bulgaria. In 1986, he joined the Department of Control Systems, Technical University of Sofia at the Plovdiv campus, where he is presently a Full Professor. He has held long-term visiting Professor/Scholar positions at various institutions in South Korea, Turkey, Mexico, Greece, Belgium, UK, and Germany. And he has coauthored one book and authored or coauthored more than 80 research papers in conference proceedings and journals. 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Aalborg University has Two Satellite Campuses, one in Copenhagen (Aalborg University Copenhagen) and the other in Esbjerg (Aalborg University Esbjerg).\n· He is a member of prestigious IEEE (Institute of Electrical and Electronics Engineers), and IAENG (International Association of Engineers) organizations. \n· He is the chief Editor of the Journal of Software Engineering.\n· He is the member of the Editorial Board of International Journal of Computer Science and Software Technology (IJCSST) and International Journal of Computer Engineering and Information Technology. \n· He is also the Editor of Communication in Computer and Information Science CCIS-20 by Springer.\n· Reviewer For Many Conferences\nHe is the lead person in making collaboration agreements between Aalborg University and many universities of Pakistan, for which the MOU’s (Memorandum of Understanding) have been signed.\nProfessor Akbar is working in Academia since 1990, he started his career as a Lab demonstrator/TA at the University of Sussex. After finishing his P. hD degree in 1992, he served in the Industry as a Scientific Officer and continued his academic career as a visiting scholar for a number of educational institutions. In 1996 he joined National University of Science & Technology Pakistan (NUST) as an Associate Professor; NUST is one of the top few universities in Pakistan. In 1999 he joined an International Company Lineo Inc, Canada as Manager Compiler Group, where he headed the group for developing Compiler Tool Chain and Porting of Operating Systems for the BLACKfin processor. The processor development was a joint venture by Intel and Analog Devices. In 2002 Lineo Inc., was taken over by another company, so he joined Aalborg University Denmark as an Assistant Professor.\nProfessor Akbar has truly a multi-disciplined career and he continued his legacy and making progress in many areas of his interests both in teaching and research. He has contributed in stochastic estimation of control area especially, in the Multiple Target Tracking and Interactive Multiple Model (IMM) research, Ball & Beam Control Problem, Robotics, Levitation Control. He has contributed in developing Algorithms for Fingerprint Matching, Computer Vision and Face Recognition. He has been supervising Pattern Recognition, Formal Languages and Distributed Processing projects for several years. He has reviewed many books on Management, Computer Science. Currently, he is an active and permanent reviewer for many international conferences and symposia and the program committee member for many international conferences.\nIn teaching he has taught the core computer science subjects like, Digital Design, Real Time Embedded System Programming, Operating Systems, Software Engineering, Data Structures, Databases, Compiler Construction. 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Thus, the sustainability of the cocoa economy is under threat as diseases of various statuses now constitute the most serious constraint to production. Most important among these is the black pod disease caused by Phytophthora genus with annual losses of 30–90% of the crop. This economically important pathogen is very diverse in nature and varied across growing countries including species such as palmivora, megakarya, capsici and citrophthora distinguished based on chromosome number, sporangial characteristics and pedicel length. World losses of 20–25% in cacao production are due to black pod disease, an estimate of 700,000 metric tons on global scale reducing global cocoa production. High cacao loss to diseases is a prime factor limiting production; consequently, significant effort is required to deal with problems associated with disease control to ensure a sustainable cacao. The effective and sustainable management of black pod disease requires integrated approach encompassing different control measures.",book:{id:"7005",slug:"theobroma-cacao-deploying-science-for-sustainability-of-global-cocoa-economy",title:"Theobroma Cacao",fullTitle:"Theobroma Cacao - Deploying Science for Sustainability of Global Cocoa Economy"},signatures:"Dele Adeniyi",authors:null},{id:"67634",title:"Cacao Growth and Development Under Different Nursery and Field Conditions",slug:"cacao-growth-and-development-under-different-nursery-and-field-conditions",totalDownloads:1248,totalCrossrefCites:2,totalDimensionsCites:2,abstract:"Experiments were conducted between 2004 and 2018 to examine cacao growth, development, establishment and yield under varying experimental conditions comprised of seed mucilage handling before sowing, sowing methods and its effects on seedling growth and development, timing of mycorrhizal inoculation on root and shoot growth and development and effects of shade and dry season drip irrigation on growth and yield of field-grown cacao. Results show that cleaning cacao seed mucilage before sowing enhanced sprouting rate and percent germination. The use of manure mixed with sawdust and loamy soil aided excellent seed germination, seedling vigor and root development. Inoculating cacao seeds with arbuscular mycorrhizal fungi (AMF) at point of sowing and early stages in the nursery aided root development and enhanced field establishment and survival during the dry season. Dense shade retarded cacao growth and development during the rainy season, while no shade enhances optimum growth and canopy development. The use of drip irrigation strategies in young cacao plantations increased seedling survival from less than 45% under no irrigation to above 95% at the end of the second dry season. This showed that irrigation during dry season can significantly enhance cacao establishment and survival.",book:{id:"7005",slug:"theobroma-cacao-deploying-science-for-sustainability-of-global-cocoa-economy",title:"Theobroma Cacao",fullTitle:"Theobroma Cacao - Deploying Science for Sustainability of Global Cocoa Economy"},signatures:"Idowu Babadele Famuwagun and Samuel Ohi Agele",authors:null},{id:"68383",title:"Major Natural Vegetation in Coastal and Marine Wetlands: Edible Seaweeds",slug:"major-natural-vegetation-in-coastal-and-marine-wetlands-edible-seaweeds",totalDownloads:754,totalCrossrefCites:0,totalDimensionsCites:1,abstract:"For thousands of years, seaweeds grown in coastal and marine have been used as food, materials and medicines by the people. Edible seaweeds directly consumed, especially in Asian, are used for preparing food due to the their components containing minerals, essential trace elements, and various natural compounds. At the last decades, they have been getting more and more attention in food and pharmaceutical industries because of their biological activities such as anti-cancer, anti-obesity, anti-diabetes, anti-microbial, and anti-oxidant activity. Therefore, in the present study, we have worked on to understand the structure of edible seaweeds. It is worthy to mention that they can be considered as source of some proteins, polyunsaturated fatty acids, minerals, vitamins, dietary fibers, antioxidants, and phytochemicals.",book:{id:"8667",slug:"plant-communities-and-their-environment",title:"Plant Communities and Their Environment",fullTitle:"Plant Communities and Their Environment"},signatures:"Ilknur Babahan, Birsen Kirim and Hamideh Mehr",authors:null},{id:"67540",title:"Aphid-Plant Interactions: Implications for Pest Management",slug:"aphid-plant-interactions-implications-for-pest-management",totalDownloads:1072,totalCrossrefCites:2,totalDimensionsCites:4,abstract:"Aphids are important herbivores and important pest of many field and forest crops. They have specialized long and flexible stylets which are adapted to feeding on phloem sap. To establish successful feeding on host plant, they need to counter a range of both physical and chemical defenses. The defenses employed by plants can have direct effect on the aphid species through difficulty in establishing successful feeding due to the presence of trichomes, thick cell wall, etc. or effect on their biology with lethal consequences in extreme cases (direct defenses). In contrast to this, plants can attract natural enemies of aphids through the release of volatile compounds (the so-called “cry or call for help”) (indirect defense). The information on different defense strategies employed by plants can be utilized to enhance the level of resistance (R) to develop sustainable pest management strategies.",book:{id:"8667",slug:"plant-communities-and-their-environment",title:"Plant Communities and Their Environment",fullTitle:"Plant Communities and Their Environment"},signatures:"Sarwan Kumar",authors:null},{id:"72336",title:"Plant Phenology and An Assessment of the Effects Regarding Heavy Metals, Nanoparticles, and Nanotubes on Plant Development: Runner Bean, Artichoke, and Chickpea Seedlings",slug:"plant-phenology-and-an-assessment-of-the-effects-regarding-heavy-metals-nanoparticles-and-nanotubes-",totalDownloads:654,totalCrossrefCites:0,totalDimensionsCites:0,abstract:"The relationship between environmental pollution and nutrition in particular, which forms the basis of health, is fundamentally important for protecting human health. Therefore, the data obtained from the examination of how plants and animals consumed as food are affected by environmental pollution can be seen as an indicator of their effects on humans. On the other hand, the role of technology and nanotechnology in life has been increasing in this century, and a considerable amount of heavy metals, nanoparticles (NPs), and nanotubes (NTs) are released to the environment. The results of morphological or anatomical examination of runner bean (Phaseolus coccineus L) and artichoke (Cynara scolymus L.) plants subjected to copper (Cu) and lead (Pb) heavy metals and chickpea (Cicer arietinum L) plants subjected to Au nanoparticles and C70 single-walled carbon nanotubes (SWNTs) are presented with this study in the point of their phenological development process. The three taxa belonging to Fabaceae and Asteraceae families with high economic status and having flowers with characteristic features were chosen deliberately as representatives. 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\r\n\tTransforming our World: the 2030 Agenda for Sustainable Development endorsed by United Nations and 193 Member States, came into effect on Jan 1, 2016, to guide decision making and actions to the year 2030 and beyond. Central to this Agenda are 17 Goals, 169 associated targets and over 230 indicators that are reviewed annually. The vision envisaged in the implementation of the SDGs is centered on the five Ps: People, Planet, Prosperity, Peace and Partnership. This call for renewed focused efforts ensure we have a safe and healthy planet for current and future generations.
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\r\n
\r\n\tThis Series focuses on covering research and applied research involving the five Ps through the following topics:
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\r\n\t1. Sustainable Economy and Fair Society that relates to SDG 1 on No Poverty, SDG 2 on Zero Hunger, SDG 8 on Decent Work and Economic Growth, SDG 10 on Reduced Inequalities, SDG 12 on Responsible Consumption and Production, and SDG 17 Partnership for the Goals
\r\n
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\r\n\t2. Health and Wellbeing focusing on SDG 3 on Good Health and Wellbeing and SDG 6 on Clean Water and Sanitation
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\r\n\t3. Inclusivity and Social Equality involving SDG 4 on Quality Education, SDG 5 on Gender Equality, and SDG 16 on Peace, Justice and Strong Institutions
\r\n
\r\n\t
\r\n
\r\n\t4. Climate Change and Environmental Sustainability comprising SDG 13 on Climate Action, SDG 14 on Life Below Water, and SDG 15 on Life on Land
\r\n
\r\n\t
\r\n
\r\n\t5. Urban Planning and Environmental Management embracing SDG 7 on Affordable Clean Energy, SDG 9 on Industry, Innovation and Infrastructure, and SDG 11 on Sustainable Cities and Communities.
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\r\n\tThe series also seeks to support the use of cross cutting SDGs, as many of the goals listed above, targets and indicators are all interconnected to impact our lives and the decisions we make on a daily basis, making them impossible to tie to a single topic.
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He also obtained an MSc in Molecular and Genetic Medicine, and a Ph.D. in Clinical Immunology and Human Genetics from the University of Sheffield, UK. He also completed a short-term fellowship in Pediatric Clinical Immunology and Bone Marrow Transplantation at Newcastle General Hospital, England. Dr. Rezaei is a Full Professor of Immunology and Vice Dean of International Affairs and Research, at the School of Medicine, Tehran University of Medical Sciences, and the co-founder and head of the Research Center for Immunodeficiencies. He is also the founding president of the Universal Scientific Education and Research Network (USERN). Dr. Rezaei has directed more than 100 research projects and has designed and participated in several international collaborative projects. He is an editor, editorial assistant, or editorial board member of more than forty international journals. He has edited more than 50 international books, presented more than 500 lectures/posters in congresses/meetings, and published more than 1,100 scientific papers in international journals.",institutionString:"Tehran University of Medical Sciences",institution:{name:"Tehran University of Medical Sciences",country:{name:"Iran"}}},{id:"180733",title:"Dr.",name:"Jean",middleName:null,surname:"Engohang-Ndong",slug:"jean-engohang-ndong",fullName:"Jean Engohang-Ndong",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/180733/images/system/180733.png",biography:"Dr. Jean Engohang-Ndong was born and raised in Gabon. After obtaining his Associate Degree of Science at the University of Science and Technology of Masuku, Gabon, he continued his education in France where he obtained his BS, MS, and Ph.D. in Medical Microbiology. He worked as a post-doctoral fellow at the Public Health Research Institute (PHRI), Newark, NJ for four years before accepting a three-year faculty position at Brigham Young University-Hawaii. Dr. Engohang-Ndong is a tenured faculty member with the academic rank of Full Professor at Kent State University, Ohio, where he teaches a wide range of biological science courses and pursues his research in medical and environmental microbiology. Recently, he expanded his research interest to epidemiology and biostatistics of chronic diseases in Gabon.",institutionString:"Kent State University",institution:{name:"Kent State University",country:{name:"United States of America"}}},{id:"188773",title:"Prof.",name:"Emmanuel",middleName:null,surname:"Drouet",slug:"emmanuel-drouet",fullName:"Emmanuel Drouet",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/188773/images/system/188773.png",biography:"Emmanuel Drouet, PharmD, is a Professor of Virology at the Faculty of Pharmacy, the University Grenoble-Alpes, France. As a head scientist at the Institute of Structural Biology in Grenoble, Dr. Drouet’s research investigates persisting viruses in humans (RNA and DNA viruses) and the balance with our host immune system. He focuses on these viruses’ effects on humans (both their impact on pathology and their symbiotic relationships in humans). He has an excellent track record in the herpesvirus field, and his group is engaged in clinical research in the field of Epstein-Barr virus diseases. He is the editor of the online Encyclopedia of Environment and he coordinates the Universal Health Coverage education program for the BioHealth Computing Schools of the European Institute of Science.",institutionString:null,institution:{name:"Grenoble Alpes University",country:{name:"France"}}},{id:"131400",title:"Prof.",name:"Alfonso J.",middleName:null,surname:"Rodriguez-Morales",slug:"alfonso-j.-rodriguez-morales",fullName:"Alfonso J. Rodriguez-Morales",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/131400/images/system/131400.png",biography:"Dr. Rodriguez-Morales is an expert in tropical and emerging diseases, particularly zoonotic and vector-borne diseases (especially arboviral diseases). He is the president of the Travel Medicine Committee of the Pan-American Infectious Diseases Association (API), as well as the president of the Colombian Association of Infectious Diseases (ACIN). He is a member of the Committee on Tropical Medicine, Zoonoses, and Travel Medicine of ACIN. He is a vice-president of the Latin American Society for Travel Medicine (SLAMVI) and a Member of the Council of the International Society for Infectious Diseases (ISID). Since 2014, he has been recognized as a Senior Researcher, at the Ministry of Science of Colombia. He is a professor at the Faculty of Medicine of the Fundacion Universitaria Autonoma de las Americas, in Pereira, Risaralda, Colombia. He is an External Professor, Master in Research on Tropical Medicine and International Health, Universitat de Barcelona, Spain. He is also a professor at the Master in Clinical Epidemiology and Biostatistics, Universidad Científica del Sur, Lima, Peru. In 2021 he has been awarded the “Raul Isturiz Award” Medal of the API. Also, in 2021, he was awarded with the “Jose Felix Patiño” Asclepius Staff Medal of the Colombian Medical College, due to his scientific contributions to COVID-19 during the pandemic. He is currently the Editor in Chief of the journal Travel Medicine and Infectious Diseases. His Scopus H index is 47 (Google Scholar H index, 68).",institutionString:"Institución Universitaria Visión de las Américas, Colombia",institution:null},{id:"332819",title:"Dr.",name:"Chukwudi Michael",middleName:"Michael",surname:"Egbuche",slug:"chukwudi-michael-egbuche",fullName:"Chukwudi Michael Egbuche",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/332819/images/14624_n.jpg",biography:"I an Dr. Chukwudi Michael Egbuche. I am a Senior Lecturer in the Department of Parasitology and Entomology, Nnamdi Azikiwe University, Awka.",institutionString:null,institution:{name:"Nnamdi Azikiwe University",country:{name:"Nigeria"}}},{id:"284232",title:"Mr.",name:"Nikunj",middleName:"U",surname:"Tandel",slug:"nikunj-tandel",fullName:"Nikunj Tandel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/284232/images/8275_n.jpg",biography:'Mr. Nikunj Tandel has completed his Master\'s degree in Biotechnology from VIT University, India in the year of 2012. He is having 8 years of research experience especially in the field of malaria epidemiology, immunology, and nanoparticle-based drug delivery system against the infectious diseases, autoimmune disorders and cancer. He has worked for the NIH funded-International Center of Excellence in Malaria Research project "Center for the study of complex malaria in India (CSCMi)" in collaboration with New York University. The preliminary objectives of the study are to understand and develop the evidence-based tools and interventions for the control and prevention of malaria in different sites of the INDIA. Alongside, with the help of next-generation genomics study, the team has studied the antimalarial drug resistance in India. Further, he has extended his research in the development of Humanized mice for the study of liver-stage malaria and identification of molecular marker(s) for the Artemisinin resistance. At present, his research focuses on understanding the role of B cells in the activation of CD8+ T cells in malaria. Received the CSIR-SRF (Senior Research Fellow) award-2018, FIMSA (Federation of Immunological Societies of Asia-Oceania) Travel Bursary award to attend the IUIS-IIS-FIMSA Immunology course-2019',institutionString:"Nirma University",institution:{name:"Nirma University",country:{name:"India"}}},{id:"334383",title:"Ph.D.",name:"Simone",middleName:"Ulrich",surname:"Ulrich Picoli",slug:"simone-ulrich-picoli",fullName:"Simone Ulrich Picoli",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/334383/images/15919_n.jpg",biography:"Graduated in Pharmacy from Universidade Luterana do Brasil (1999), Master in Agricultural and Environmental Microbiology from Federal University of Rio Grande do Sul (2002), Specialization in Clinical Microbiology from Universidade de São Paulo, USP (2007) and PhD in Sciences in Gastroenterology and Hepatology (2012). She is currently an Adjunct Professor at Feevale University in Medicine and Biomedicine courses and a permanent professor of the Academic Master\\'s Degree in Virology. She has experience in the field of Microbiology, with an emphasis on Bacteriology, working mainly on the following topics: bacteriophages, bacterial resistance, clinical microbiology and food microbiology.",institutionString:null,institution:{name:"Universidade Feevale",country:{name:"Brazil"}}},{id:"229220",title:"Dr.",name:"Amjad",middleName:"Islam",surname:"Aqib",slug:"amjad-aqib",fullName:"Amjad Aqib",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/229220/images/system/229220.png",biography:"Dr. Amjad Islam Aqib obtained a DVM and MSc (Hons) from University of Agriculture Faisalabad (UAF), Pakistan, and a PhD from the University of Veterinary and Animal Sciences Lahore, Pakistan. Dr. Aqib joined the Department of Clinical Medicine and Surgery at UAF for one year as an assistant professor where he developed a research laboratory designated for pathogenic bacteria. Since 2018, he has been Assistant Professor/Officer in-charge, Department of Medicine, Manager Research Operations and Development-ORIC, and President One Health Club at Cholistan University of Veterinary and Animal Sciences, Bahawalpur, Pakistan. He has nearly 100 publications to his credit. His research interests include epidemiological patterns and molecular analysis of antimicrobial resistance and modulation and vaccine development against animal pathogens of public health concern.",institutionString:"Cholistan University of Veterinary and Animal Sciences",institution:null},{id:"62900",title:"Prof.",name:"Fethi",middleName:null,surname:"Derbel",slug:"fethi-derbel",fullName:"Fethi Derbel",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/62900/images/system/62900.jpeg",biography:"Professor Fethi Derbel was born in 1960 in Tunisia. He received his medical degree from the Sousse Faculty of Medicine at Sousse, University of Sousse, Tunisia. He completed his surgical residency in General Surgery at the University Hospital Farhat Hached of Sousse and was a member of the Unit of Liver Transplantation in the University of Rennes, France. He then worked in the Department of Surgery at the Sahloul University Hospital in Sousse. Professor Derbel is presently working at the Clinique les Oliviers, Sousse, Tunisia. His hospital activities are mostly concerned with laparoscopic, colorectal, pancreatic, hepatobiliary, and gastric surgery. He is also very interested in hernia surgery and performs ventral hernia repairs and inguinal hernia repairs. He has been a member of the GREPA and Tunisian Hernia Society (THS). During his residency, he managed patients suffering from diabetic foot, and he was very interested in this pathology. For this reason, he decided to coordinate a book project dealing with the diabetic foot. Professor Derbel has published many articles in journals and collaborates intensively with IntechOpen Access Publisher as an editor.",institutionString:"Clinique les Oliviers",institution:null},{id:"300144",title:"Dr.",name:"Meriem",middleName:null,surname:"Braiki",slug:"meriem-braiki",fullName:"Meriem Braiki",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/300144/images/system/300144.jpg",biography:"Dr. Meriem Braiki is a specialist in pediatric surgeon from Tunisia. She was born in 1985. She received her medical degree from the University of Medicine at Sousse, Tunisia. She achieved her surgical residency training periods in Pediatric Surgery departments at University Hospitals in Monastir, Tunis and France.\r\nShe is currently working at the Pediatric surgery department, Sidi Bouzid Hospital, Tunisia. Her hospital activities are mostly concerned with laparoscopic, parietal, urological and digestive surgery. She has published several articles in diffrent journals.",institutionString:"Sidi Bouzid Regional Hospital",institution:null},{id:"229481",title:"Dr.",name:"Erika M.",middleName:"Martins",surname:"de Carvalho",slug:"erika-m.-de-carvalho",fullName:"Erika M. de Carvalho",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/229481/images/6397_n.jpg",biography:null,institutionString:null,institution:{name:"Oswaldo Cruz Foundation",country:{name:"Brazil"}}},{id:"186537",title:"Prof.",name:"Tonay",middleName:null,surname:"Inceboz",slug:"tonay-inceboz",fullName:"Tonay Inceboz",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/186537/images/system/186537.jfif",biography:"I was graduated from Ege University of Medical Faculty (Turkey) in 1988 and completed his Med. PhD degree in Medical Parasitology at the same university. I became an Associate Professor in 2008 and Professor in 2014. I am currently working as a Professor at the Department of Medical Parasitology at Dokuz Eylul University, Izmir, Turkey.\n\nI have given many lectures, presentations in different academic meetings. I have more than 60 articles in peer-reviewed journals, 18 book chapters, 1 book editorship.\n\nMy research interests are Echinococcus granulosus, Echinococcus multilocularis (diagnosis, life cycle, in vitro and in vivo cultivation), and Trichomonas vaginalis (diagnosis, PCR, and in vitro cultivation).",institutionString:"Dokuz Eylül University",institution:{name:"Dokuz Eylül University",country:{name:"Turkey"}}},{id:"71812",title:"Prof.",name:"Hanem Fathy",middleName:"Fathy",surname:"Khater",slug:"hanem-fathy-khater",fullName:"Hanem Fathy Khater",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/71812/images/1167_n.jpg",biography:"Prof. Khater is a Professor of Parasitology at Benha University, Egypt. She studied for her doctoral degree, at the Department of Entomology, College of Agriculture, Food and Natural Resources, University of Missouri, Columbia, USA. She has completed her Ph.D. degrees in Parasitology in Egypt, from where she got the award for “the best scientific Ph.D. dissertation”. She worked at the School of Biological Sciences, Bristol, England, the UK in controlling insects of medical and veterinary importance as a grant from Newton Mosharafa, the British Council. Her research is focused on searching of pesticides against mosquitoes, house flies, lice, green bottle fly, camel nasal botfly, soft and hard ticks, mites, and the diamondback moth as well as control of several parasites using safe and natural materials to avoid drug resistances and environmental contamination.",institutionString:null,institution:{name:"Banha University",country:{name:"Egypt"}}},{id:"99780",title:"Prof.",name:"Omolade",middleName:"Olayinka",surname:"Okwa",slug:"omolade-okwa",fullName:"Omolade Okwa",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/99780/images/system/99780.jpg",biography:"Omolade Olayinka Okwa is presently a Professor of Parasitology at Lagos State University, Nigeria. She has a PhD in Parasitology (1997), an MSc in Cellular Parasitology (1992), and a BSc (Hons) Zoology (1990) all from the University of Ibadan, Nigeria. She teaches parasitology at the undergraduate and postgraduate levels. She was a recipient of a Commonwealth fellowship supported by British Council tenable at the Centre for Entomology and Parasitology (CAEP), Keele University, United Kingdom between 2004 and 2005. She was awarded an Honorary Visiting Research Fellow at the same university from 2005 to 2007. \nShe has been an external examiner to the Department of Veterinary Microbiology and Parasitology, University of Ibadan, MSc programme between 2010 and 2012. She is a member of the Nigerian Society of Experimental Biology (NISEB), Parasitology and Public Health Society of Nigeria (PPSN), Science Association of Nigeria (SAN), Zoological Society of Nigeria (ZSN), and is Vice Chairperson of the Organisation of Women in Science (OWSG), LASU chapter. She served as Head of Department of Zoology and Environmental Biology, Lagos State University from 2007 to 2010 and 2014 to 2016. She is a reviewer for several local and international journals such as Unilag Journal of Science, Libyan Journal of Medicine, Journal of Medicine and Medical Sciences, and Annual Research and Review in Science. \nShe has authored 45 scientific research publications in local and international journals, 8 scientific reviews, 4 books, and 3 book chapters, which includes the books “Malaria Parasites” and “Malaria” which are IntechOpen access publications.",institutionString:"Lagos State University",institution:{name:"Lagos State University",country:{name:"Nigeria"}}},{id:"273100",title:"Dr.",name:"Vijay",middleName:null,surname:"Gayam",slug:"vijay-gayam",fullName:"Vijay Gayam",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/273100/images/system/273100.jpeg",biography:"Dr. Vijay Bhaskar Reddy Gayam is currently practicing as an internist at Interfaith Medical Center in Brooklyn, New York, USA. 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Thus proteomics, an area of research that detects all protein forms expressed in an organism, including splice isoforms and post-translational modifications, is more suitable than genomics for a comprehensive understanding of the biochemical processes that govern life. The most common proteomics applications are currently in the clinical field for the identification, in a variety of biological matrices, of biomarkers for diagnosis and therapeutic intervention of disorders. From the comparison of proteomic profiles of control and disease or different physiological states, which may emerge, changes in protein expression can provide new insights into the roles played by some proteins in human pathologies. Understanding how proteins function and interact with each other is another goal of proteomics that makes this approach even more intriguing. Specialized technology and expertise are required to assess the proteome of any biological sample. Currently, proteomics relies mainly on mass spectrometry (MS) combined with electrophoretic (1 or 2-DE-MS) and/or chromatographic techniques (LC-MS/MS). MS is an excellent tool that has gained popularity in proteomics because of its ability to gather a complex body of information such as cataloging protein expression, identifying protein modification sites, and defining protein interactions. 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