Properties Of Bovine Serum Albumin Research Articles

Changes in Secondary Structure and Properties of Bovine Serum Albumin as a Result of Interactions with a Gold Surface.

The front cover artwork is provided by Prof. Barbara Jachimska's group at the Jerzy Haber Institute of Catalysis and Surface Chemistry, PAS. The image represents the process of changes in the secondary structure of Bovine Serum Albumin (BSA) as a result of its interactions with a gold surface. Read the full text of the Research Article at 10.1002/cphc.202300505.

Front Cover: Changes in Secondary Structure and Properties of Bovine Serum Albumin as a Result of Interactions with Gold Surface (ChemPhysChem 2/2024)

Front Cover: Changes in Secondary Structure and Properties of Bovine Serum Albumin as a Result of Interactions with Gold Surface (ChemPhysChem 2/2024)

Changes in Secondary Structure and Properties of Bovine Serum Albumin as a Result of Interactions with Gold Surface.

Proteins can alter their shape when interacting with a surface. This study explores how bovine serum albumin (BSA) modifies structurally when it adheres to a gold surface, depending on the protein concentration and pH. We verified that the gold surface induces significant structural modifications to the BSA molecule using circular dichroism, infrared spectroscopy, and atomic force microscopy. Specifically, adsorbed molecules displayed increased levels of disordered structures and β-turns, with fewer α-helices than the native structure. MP-SPR spectroscopy demonstrated that the protein molecules preferred a planar orientation during adsorption. Molecular dynamics simulations revealed that the interaction between cysteines exposed to the outside of the molecule and the gold surface was vital, especially at pH=3.5. The macroscopic properties of the protein film observed by AFM and contact angles confirm the flexible nature of the protein itself. Notably, structural transformation is joined with the degree of hydration of protein layers.

Pulsed electric field enhances glucose glycation and emulsifying properties of bovine serum albumin: Focus on polarization and ionization effects at a high reaction temperature

Previous studies demonstrated that the non-thermal effects of pulsed electric fields can promote protein glycation below 40 °C, but it does not always enhance the emulsifying properties of proteins, such as in the bovine serum albumin/glucose model. Therefore, the aim of this study was to investigate the impact of non-thermal effects on the glucose glycation and emulsification properties of bovine serum albumin at 90 °C. The results of circular dichroism, surface hydrophobicity, and molecular dynamics simulations showed that the polarization effect increased the degree of glycation of bovine serum albumin-glucose conjugates from 12.82 % to 21.10 % by unfolding protein molecule, while the emulsifying stability index was increased from 79.17 to 100.73 compared with the control. Furthermore, the results of principal component analysis and Pearson correlation analysis indicated that the ionization effect and the free radicals generated by pulsed electric fields significantly (p < 0.05) inhibited browning and reduced free sulfhydryl content. This study demonstrated that pulsed electric fields combined with heating can prepare glycated proteins with good emulsifying properties in a short period of time and at temperatures lower than conventional heating while reducing energy consumption. This processing strategy has potential applications in improving the emulsifying performance of highly stable proteins.

Foaming properties of the complex of chitooligosaccharides and bovine serum albumin and its application in angel cake

The complex of chitooligosaccharides (COS) and protein is worthy of investigation, as COS is an important functional ingredient and the functional properties of protein might be improved after complexation. Using bovine serum albumin (BSA) as the model protein, this work explored the foaming properties and interfacial behavior of COS-BSA complex, as well as its application as a substitute for egg whites in angel cake. The effects of pH and mixing ratio ( r ) on the foam properties and interfacial behavior of COS-BSA complex were studied using dilute solution. And the effects of the COS-BSA substitution rate on the physical properties and microbial storability of the cake were studied. Compared with BSA, the foaming capacity and foam stability of COS-BSA complexes were significantly improved in the pH range of 3.0–10.0, and both the foaming capacity and foam stability of COS-BSA complexes at pH 7.0 were in the order of r 0.5 ≥ r 0.25 ≥ r 1.0 > r 2.0 > BSA > COS. Angel cake with the COS-BSA substitution rate of 25% had the best physical properties, in which COS and BSA had a synergistic effect on the specific volume and texture of the cake. The substitute of COS-BSA complex for egg white in angel cake significantly inhibited microbial growth during storage. This work provided COS-BSA complex as a substitute for egg white in cake making, and COS-BSA complex improved the physical properties of cake and inhibited microbial growth. • Chitooligosaccharides improved foaming properties of bovine serum albumin. • Good foaming of complexes was related with their surface dilatational rheology. • Cake with complex substitution rate of 25% exhibited the best physical properties. • Complex addition in cake significantly inhibited microbial growth during storage.

СПЕКТРОМЕТРИЯ РАСТВОРА АЛЬБУМИНА В ЭЛЕКТРОХИМИЧЕСКИ АКТИВИРОВАННОЙ ВОДЕ

Electrochemical activation of water (ECAW) is a topical method of reagent-free regulation of physicochemical parameters of aquatic food environments. The properties of solutions of macronutrients based in ECAW may differ from similar solutions on untreated water. In this work, the regularities of the interaction of the anodic and cathodic fractions of ECAW with protein molecules have been investigated. ECAW state and solutions are defined by anomalous physical chemical features (pH, redox potential) that provide ther biological activity. Solutions both low molecular and high molecular compounds prepared on the basis of ECAW can be distinguished from solutions prepared with non activated water. Applying spectral approaches (UV spectrometry, ToF – SIMS), it was shown that the analyzed mono product of protein nature (bovine serum albumin) and the complex food proteins (gelatin, casein) were modified in ECAW fractions. A number of data obtained allows us to suggest that funded effects may be provided with changes of structure in the protein and/ or its fragmentation. The shown results of the anolyte and catholyte impact on properties of bovine serum albumin confirm the perspective of the direct use of ECAW approach in the food industry for aim to improve the parameters of technological process. In the other words, electrochemical activation is the efficacious way to get acidic and alkalic solutions for replacing NaCl acid and sodium hydroxide in the industry of foodstuffs.

Properties of serum albumin in electrolyzed water

Introduction. Electrochemical activation of water controls the physicochemical parameters of aquatic food environment without any reagents. Electrolyzed water affects the properties of macronutrient solutions. The present research studied the effect of anodic and cathodic fractions of electrochemically activated water on protein molecules and their interaction patterns.&#x0D; Study objects and methods. The study featured bovine serum albumin and its properties in electrochemically activated water with nonstandard redox and acidity values. The aqueous solution of bovine serum albumin was studied by viscometry, UV spectrometry, time-of-flight secondary ion mass spectrometry, and electrophoresis.&#x0D; Results and discussion. By knowing the interaction patterns of electrochemically activated water and protein molecules, food producers can control the properties of biological raw materials. Bovine serum albumin was studied in metastable fractions of electrochemically activated water obtained in the anode or cathode chamber of an electrochemical reactor. Both fractions of electrochemically activated water appeared to modify the properties of bovine serum albumin. The oxidized fraction of electrochemically activated water (anolyte) converted the protein solution into a more homogeneous molecular composition. The solution of bovine serum albumin in the reduced fraction of electrochemically activated water (catholyte) had an abnormally negative redox potential (–800 mV). The aqueous solution of bovine serum albumin in catholyte retained its initial viscosity for a long time, and its level was lower than in the control sample. This effect was consistent with other physicochemical characteristics of the solution.&#x0D; Conclusion. The research revealed some patterns that make it possible to apply reagent-free viscosity regulation to protein media in the food industry.

Advancement of Fluorescent and Structural Properties of Bovine Serum Albumin-Gold Bioconjugates in Normal and Heavy Water with pH Conditioning and Ageing

The red-emitting fluorescent properties of bovine serum albumin (BSA)–gold conjugates are commonly attributed to gold nanoclusters formed by metallic and ionized gold atoms, stabilized by the protein. Others argue that red fluorescence originates from gold cation–protein complexes instead, not gold nanoclusters. Our fluorescence and infrared spectroscopy, neutron, and X-ray small-angle scattering measurements show that the fluorescence and structural behavior of BSA–Au conjugates are different in normal and heavy water, strengthening the argument for the existence of loose ionic gold–protein complexes. The quantum yield for red-emitting luminescence is higher in heavy water (3.5%) than normal water (2.4%), emphasizing the impact of hydration effects. Changes in red luminescence are associated with the perturbations of BSA conformations and alterations to interatomic gold–sulfur and gold–oxygen interactions. The relative alignment of domains I and II, II and III, III and IV of BSA, determined from small-angle scattering measurements, indicate a loose (“expanded-like”) structure at pH 12 (pD ~12); by contrast, at pH 7 (pD ~7), a more regular formation appears with an increased distance between the I and II domains, suggesting the localization of gold atoms in these regions.

Fluorescent Gold Nanoclusters for In Vivo Shortwave-Infrared Imaging

Gold nanoclusters (Au-NCs) are unique fluorescent nanomaterials that can be used for in vitro and in vivo bioimaging. Au-NCs are less toxic, and their size is much smaller than that of other fluorescent nanomaterials such as quantum dots. The emission wavelengths of Au-NCs depend on the nanocluster size, which can be controlled by the reaction conditions. Recently, shortwave-infrared (SWIR) emitting Au-NCs have attracted much attention for bioimaging. SWIR fluorescence (900–1400 nm) enables deep tissue imaging due to the weak absorption and scattering of the SWIR fluorescence by tissues. Since the autofluorescence of tissues is almost zero in the SWIR region, SWIR fluorescence imaging results in high contrast images compared to visible and near-infrared imaging. For the SWIR fluorescence imaging, the development of biocompatible SWIR fluorescent probes is crucial. Although several types of SWIR fluorescent probes based on quantum dots, rare-earth-doped nanoparticles, and organic dyes have been appeared, there are very few examples of SWIR probe which cytotoxicity is low enough to use in biomedical fields. Herein, we present the synthesis, and optical properties of bovine serum albumin (BSA) capped Au-NCs (Au-NCs@BSA), which emit at the SWIR region. We demonstrate the efficacy of Au-NCs@BSA for in vivo SWIR fluorescence imaging of brain vasculatures, blood vessels, lymph nodes and tumors in mice.

A comparative study of structural and dynamical properties of bovine serum albumin in the presence of spermine

Bovine Serum Albumin (BSA) has many functions in plasma. Serum albumins function as a carrier for fatty acids, thyroid hormones, and steroids in the blood and are involved in stabilizing the volume of extracellular fluid. BSA is a polypeptide with 583 amino acids and a molecular weight of 66,463 Da. Polyamines have several roles in cell physiology; Such as protection against oxidative damage, gene expression, and protein synthesis. Spermine (as a polyamine) is present in all eukaryotic cells. Using the methods of spectroscopic, thermal denaturation, molecular docking, and molecular dynamics simulation, we were able to investigate the effect of spermine binding to BSA in Tris-HCl buffer with pH 7.4. By binding spermine to the BSA, the absorbance changed significantly at 280 nm. The addition of spermine alters the folding of BSA and regularly decreases intrinsic fluorescence intensity at temperatures 298 K and 308 K. The formation of the BSA-spermine complex was mainly by electrostatic interactions. According to the results, fluorescence quenching (Ksv) was static and revealed one binding site for spermine. Also, molecular dynamics simulation results demonstrated that spermine binds to BSA and due to the decrease in RMSD and RMSF and the increase in Tm, it can be said that spermine has a stabilizing effect on BSA.

Facile synthesis of a three-dimensional hydroxyapatite monolith for protein adsorption.

Hydroxyapatite (HA) shows promising applications in the clinical treatment of bone defects owing to its excellent physicochemical properties, such as biocompatibility, bioactivity, and osteoconductivity. However, it is difficult to maintain a porous structure in HA materials because of processing difficulties. In this study, a hard template method was developed to prepare a porous HA monolith with a hierarchical pore structure and high porosity. The cellulose monolith template was prepared from cellulose acetate using a thermally induced phase separation method. The cellulose monoliths were then immersed into the HA slurry to form a cellulose_HA composite monolith, which was converted to an HA monolith by burning in air to remove the cellulose monolith. Owing to the hierarchically porous structure of the cellulose monolith template, the obtained HA monolith demonstrated a hierarchically porous structure. Furthermore, the HA monolith was explored to study the adsorption and release properties of bovine serum albumin (BSA), which indicated that the HA monolith had a high adsorption capacity (388.6 mg g-1) and sustained release from the BSA-loaded HA monolith. Thus, HA monoliths have potential applications in the field of protein purification and biomaterials.

Self-assembled bovine serum albumin nanoparticles as pesticide delivery vectors for controlling trunk-boring pests

BackgroundTrunk-boring pests (TBPs) are an important type of forest pest, TBPs not only feed on the branches and trunks of trees, but also spread quarantine diseases in forests. However, because the larvae of TBPs live inside the trunk and are well concealed, prevention and control are difficult. The lack of effective control methods leads to the death of many trees in forests. In this study, a novel nanopesticide featuring high bioactivity and slow-release properties was developed to control TBPs. Thiacloprid (THI), which is commonly used to control Coleoptera species, was used as a model pesticide.ResultsThe oleophobic properties of bovine serum albumin (BSA) were exploited to encapsulate the hydrophobic pesticide THI by self-assembly, and the size of the obtained nanoparticles, THI@BSA·NPs, was approximately 23 nm. The loading efficiency reached 70.4%, and THI@BSA·NPs could be released continuously for over 15 days, with the cumulative release reaching 93.5%. The fluorescein isothiocyanate (FITC)-labeled nanoparticles were evenly distributed in the digestive tract and body surface of a typical TBPs, M. alternatus, and the stomach and contact toxicities increased by 33.7% and 25.9%, respectively, compared with those of free THI. Furthermore, the results showed that the transport efficiency of THI@BSA·NPs was highest at a concentration of 50 μg/mL, and the THI@BSA·NPs content in the trunk, from to lower to higher layers, was 8.8, 8.2, 7.6, and 5.8 μg/g. At the same time, THI@BSA·NPs also exhibited high transport efficiency in dead trees.ConclusionThe transport efficiency and toxicity of the active ingredients are the key factors for the control of TBPs. This work provided idea for the application of biological delivery system encapsulated hydrophobic pesticides. The novel self-assembled THI@BSA·NPs have promising potential for sustainable control of TBPs.

The Role of Surface Properties on Protein Aggregation Behavior in Aqueous Solution of Different pH Values.

This study aimed to investigate the effect of pH-mediated surface properties of bovine serum albumin (BSA) on protein aggregation and the changes of protein structure and colloidal stability at different solution pH levels. The hydrophobicity of BSA surface was characterized by endogenous fluorescence spectroscopy, fluorescence quenching of acrylamide, and fluorescence probe. The results showed that the hydrophobicity of BSA surface was similar at pH5, 6, 7.4, followed by pH4, 8, 9, 10, and finally by pH3 and 11 with strong acidity and alkalinity. The positive charge on the BSA surface was increased gradually with the decrease of solution pH, while the negative charge on protein surface was increased gradually with the increase of solution pH. The degree of protein aggregation was examined by turbidimetry, flow cytometry, and SDS-PAGE. The results showed that the oscillating aggregation of BSA did not change with the solution pH, but was partially dependent on the relative contribution of electrostatic and hydrophobic interactions between the protein molecules. In addition, the secondary structure, conformational stability, unfolding degree, and colloidal stability of proteins were investigated by circular dichroism, fluorescence spectroscopy, protein pulse hydrolysis, and dynamic light scattering, respectively. The results suggested that the solution pH could change the structure and stability of the protein at different levels. Solution pH has distinct effects on the structural stability of protein at different levels. The change of protein surface properties mediated by solution pH is related to protein aggregation.

The effect of putrescine on stability and structural properties of bovine serum albumin

Serum albumins are the abounding proteins in plasma. Their most important characteristic is that they act as carriers for a type of compound, for example, different drugs. Bovine Serum Albumin (BSA) is a single-chain polypeptide with 583 amino acids. Polyamines such as putrescine can interact with negatively charged molecules. The effect of putrescine on the structure of bovine serum albumin has been surveyed utilizing the method of UV-Vis spectroscopy, Thermal stability, fluorescence spectroscopy, and molecular docking at temperature 298 K and 308 K at pH 7.4 using Tris-HCl as a buffer. The complex formation between putrescine and bovine serum albumin was discovered as alter in the absorbance at 280 nm. The amount of absorption increases with the addition of putrescine. The adding of putrescine alters the bovine serum albumin and decrements the hydrophobicity of the micro-environment of the Trp residues in the inner hydrophobic zone. The static kind of quenching process was chiefly contained within the quenching of intrinsic emission of the protein. The fluorescence quenching details (Ksv) for complex bovine serum albumin-putrescine revealed one binding site for putrescine. The negative amount of Gibbs free energy change (ΔG°) suggested the binding operation was spontaneous.Communicated by Ramaswamy H. Sarma

Effect of dielectric barrier discharge (DBD) plasma on the structure and antioxidant activity of bovine serum albumin (BSA)

AbstractThis study was aimed to determine the influence of dielectric barrier discharge (DBD) plasma with a plasma intensity (20 and 40 kV) and treatment times (0, 2, 4, 6 and 8 min) on the physicochemical, structural and antioxidant properties of bovine serum albumin (BSA) solution. In results, the free sulphydryl content, pH and free amino group contents, while carbonyl groups and surface hydrophobicity were increased after the plasma treatment. After plasma treatment, there is also an increase in the DPPH and FRAP assay that was associated with the changes in the structure of the peptides chain. The complementary techniques were employed to identify the protein structural modifications by plasma treatment. These changes were more severe at the most extended treatment duration and plasma intensity. The high energetic and oxidising species carried by plasma may have significant associations on the structural and physical properties of BSA.

RETRACTED: Thermal investigation of montmorillonite/BSA by Fourier Transform InfraRed Spectroscopy measurements

&lt;abstract&gt; &lt;p&gt;This paper reports the analysis of the intramolecular OH stretching band obtained by Fourier Transform Infrared (FTIR) spectroscopy measurements. In order to characterize the effect of montmorillonite on the properties of Bovine Serum Albumin (BSA) the two-state model is adopted for the analysis of the OH stretching band. We assume that the OH stretching can be divided into two different states of inter-molecular bonding. The results of this experimental work confirm that the montmorillonite leads to a stabilization of the BSA structure. Also, the analysis of the spectra temperature dependence shows a montmorillonite-induced higher thermal stability of the BSA in respect to pristine BSA. Thus, this paper allows to highlight the importance of montmorillonite as thermal bio-protector: this is also evidenced by the theory widely discussed in the following introduction regarding the birth of the first life forms on earth in montmorillonite clay, in which the protective role of the montmorillonite interlayer space is also highlighted. A FTIR analysis was carried out to investigate the interaction of montmorillonite with BSA. Two different approaches, i.e. Spectral Distance and Wavelet analyses, constitute two effective and innovative approaches for the characterization of the thermal properties of pristine BSA and of BSA in the presence of montmorillonite. The results allowed us to consider as BSA in the presence of montmorillonite has a lower spectral sensitivity when the temperature changes and, therefore, the role of montmorillonite as a thermal bio-protector is motivated.&lt;/p&gt; &lt;/abstract&gt;

Thermal investigation of montmorillonite/BSA by fourier transform infrared spectroscopy measurements&lt;xref ref-type="fn" rid="fn1"&gt;&lt;sup&gt;1&lt;/sup&gt;&lt;/xref&gt;

&lt;abstract&gt; &lt;p&gt;This paper reports the analysis of the intramolecular OH stretching band obtained by Fourier Transform Infrared (FTIR) spectroscopy measurements. In order to characterize the effect of montmorillonite on the properties of Bovine Serum Albumin (BSA) the two-state model is adopted for the analysis of the OH stretching band. We assume that the OH stretching can be divided into two different states of inter-molecular bonding. The results of this experimental work confirm that the montmorillonite leads to a stabilization of the BSA structure. Also, the analysis of the spectra temperature dependence shows a montmorillonite-induced higher thermal stability of the BSA in respect to pristine BSA. Thus, this paper highlights the effectiveness of montmorillonite as thermal bio-protector. A FTIR analysis was carried out to investigate the interaction of Montmorillonite with BSA. Two different approaches, i.e. Spectral Distance and Wavelet analyses, constitute two effective and innovative approaches for the characterization of the thermal properties of pristine BSA and of BSA in the presence of Montmorillonite. The results allowed us to consider as BSA in the presence of Montmorillonite has a lower spectral sensitivity when the temperature changes and, therefore, the role of Montmorillonite as a thermal bio-protector is motivated.&lt;/p&gt; &lt;/abstract&gt;

Effect of layered graphene oxide on the structure and properties of bovine serum albumin grafted polyacrylonitrile hybrid bionanocomposites

Herein, one‐pot synthetic protocol is utilized to synthesize graphene oxide (GO) reinforced bovine serum albumin grafted polyacrylonitrile (BSA‐g‐PAN) microspheres through emulsifier‐free in situ emulsion polymerization route by using potassium persulfate (KPS) as initiator. The surface morphologies of pure PAN, BSA‐g‐PAN hybrid polymer, and BSA‐g‐PAN/GO hybrid bionanocomposites are observed through scanning electron microscope. Pure PAN shows the self‐assembled cauliflower like morphology which is found to be structurally interfered due to grafting between BSA and PAN. Moreover, the growth of cauliflower like morphology is influenced by the incorporation of GO platelets within BSA‐g‐PAN matrix, due to strong interfacial adhesion between GO and PAN. Transmission electron microscopy, X‐ray diffraction, and atomic force microscopy techniques are used to evaluate structural distributions of layered GOs within BSA‐g‐PAN chains. Due to filling up of microvoids of BSA‐g‐PAN structure by the GO layers, the oxygen permeability of the hybrid bionanocomposite is reduced by 22 folds with incorporation of only 3 wt% of GO. Moreover, the BSA‐g‐PAN/GO hybrid bionanocomposite shows significant antibacterial activities against bacteria such as S. aureus and E. coli. Primarily, thermal, gas barrier, biodegradability, antimicrobial, and mechanical properties of the synthesized hybrid bionanocomposites are studied to explore the hybrid bionanocomposite in packaging applications. POLYM. COMPOS., 40:3989–4003, 2019. © 2019 Society of Plastics Engineers

Ultrasonic dispersion temperature- and pH-tuned spectral and electrochemical properties of bovine serum albumin on carbon nanotubes and its conformational transition

In this paper, we first report the ultrasonic dispersion temperature- and pH-tuned spectral and electrochemical properties of bovine serum albumin (BSA) on single-walled carbon nanotubes (SWCNTs) and its configurational transition. The BSA-SWCNTs exhibit an irreversible oxidation peak at 0.793 V (vs. SCE) and a couple of tryptophan (Trp)-based surface-confined redox peaks at the formal potential of 0.154 V. The decrease of the dispersion temperature down to 283 K from 313 K at pH 7.2 leads to an increase in the surface activity coefficient (γs) and exothermic reaction rate constant (kf). The loop (L)-shaped BSA-SWCNTs with slight β-sheet prepared by controlling the dispersion temperature at 298 K (pH 7.2) show the maximum emission and minimum absorbance. The L-form of BSA-SWCNTs is transformed into basic (B)-form and fast migration (F)-form while controlling the dispersion temperature at 283 K and 313 K, respectively. The dispersion temperature and pH have a synergistic influence on the spectral and electrochemical properties of BSA-SWCNTs via the unfolding/refolding processes of β-sheet driven by ultrasonic/thermal motion and surface adsorption. The present study provides an effective approach for the preparation and evaluation of serum protein-based nanomaterials with spectral and electrochemical properties tuned by dispersion pH or temperature, as well as opens the way for optoelectronic and electrochemical applications.

Immobilization kinetics and mechanism of bovine serum albumin on diatomite clay from aqueous solutions

In this research, adsorption properties of bovine serum albumin (BSA) on diatomite clay, which is an oxide mineral, were studied as a function of BSA, sodium phosphate buffer and protein concentration and pH and the thermodynamic parameters of adsorption process were investigated. The BSA adsorption experiment onto diatomite clay indicated that the BSA solution reached the maximum adsorption value at pH 5.5. It was observed that the maximum adsorption capacity (qm) of the data obtained from the adsorption studies showed a great dependence on pH. The maximum amount of adsorption in adsorption experiments can be considered as points where the electrostatic interaction for pH is appropriate. Both structural and electrostatic interaction in regions outside of the isoelectric point may have caused a decrease in BSA absorbance. The structural influences were associated with different conformational states that while BSA molecules accept changes with pH, electrostatic effects can be observed in BSA molecules behaved like soft particles. In this case, it is not possible to explain the independence of the qm–pH curves of the amount of adsorption. The protein molecules at this point are very stable. Because this value is close to the isoelectric point of serum albumin. The surface structural change of BSA and diatomite clay was studied. For this, Fourier transform infrared spectroscopy (FTIR) spectroscopy values were compared before and after the experiment. The diatomite samples used as support material were characterized by FTIR, scanning electron microscopy, thermogravimetric analysis and Brunauer Emmett–Teller surface area analysis. The thermodynamic functions such as enthalpy, entropy, Gibbs free energy and activation energy were investigated in their experimental work. The thermodynamic parameters such as Gibbs free energy (ΔG*), Ea, ΔH* and ΔS* were calculated as − 67.45, 15.41, − 12.84 kJ mol−1 and − 183.28 J mol−1 K−1 for BSA adsorption, respectively. We can deduce that the adsorption process from the data obtained from the thermodynamic parameters is spontaneous and exothermic. The adsorption of the process was investigated using Eyring and Arrhenius equations, and its adsorption kinetic found to be coherent with the pseudo-second-order model. As a result, we reached that the diatomite clay is a suitable adsorbent for the BSA. Experimental results showed that diatomite clay has the potency to be used for rapid pretreatment in the process of identifying proteins.