Are babies of vaccinated Pregnant and lactating mothers with ChAdOx1 AstraZeneca covid vaccine more risk for zinc deficiency and SCID disease.

AstraZeneca's covid-19 vaccine demonstrates some concerns regarding its excipients, such as polysorbate 80, which serves as a stabilizer, and EDTA, which serves as a binding agent. 7 ADA is a critical purine metabolic enzyme required for adequate immunological competence. The current study examines the effect of Zn2+ on the maintenance of ADA. After eliminating Zn2+, the protein's crystallographic structure has retained a high degree of order and similarity to the original one, with some alterations limited to the areas surrounding the pocket. However, the protein's stability has been dramatically reduced. EDTA is a highly effective zinc-chelating agent employed in the investigations of protein interactions. The potential damage of the structure and interactions of zinc-binding proteins by EDTA treatment must be considered. Excess Zn2+ has not returned C/H1 to its normal structure, highlighting the irreversible denaturation induced by the EDTA. Around 30% of proteins in cells form complexes with metals. Metal ions are essential not just for regulating biological functions but also for stabilizing proteins. (ADA, EC 3.5.4.4) has a molecular mass of 40 kDa and contains a firmly attached zinc ion essential for its activity. The lack of its enzymatic activity leads to malfunction B and T cells, and SCID development

Modalities of Protein Denaturation and Nature of Denaturants

Denaturation of protein is a biological phenomenon in which a protein loses its native shape due to the breaking or disruption of weak chemical bonds and interactions which makes the protein biologically inactive. It is the process where properly folded proteins formed under physiological conditions is transformed to an unfolded protein under non-physiological conditions. The process of denaturation of proteins can occur under different physiological and chemical conditions. Denaturation can be reversible or irreversible. Denaturation mostly takes places when the protein is subjected under external elements like inorganic solutes, organic solvents, acids or bases, and by heat or irradiations. The denaturing agents or denaturants widely used in protein folding or unfolding experiments are urea and guanidinium chloride (GdmCl). In denaturation, the alpha-helix structure and beta sheets structure of the native protein are disrupted and unfolds it into any random shape. We can also say that denaturation occurs due to the disruption of bonding interactions which are responsible for secondary structure and the tertiary structure of the proteins.

Kinetic and Thermodynamic Characterization of the Protease from Bacillus licheniformis (ATCC 12759)

In this study, the kinetic of a thermo-stable extracellular protease produced by Bacillus licheniformis (ATCC 12759) cultured in skim latex serum fortified media was investigated. The enzyme was stable up to 65 oC after incubation for 60 min at pH 8. The Lineweaver-Burk exhibited vmax (maximum rate) of 37.037 U/mg min-1 and KM (Michaelis-Menten constant) of 8.519 mg/mL. The activation energy (Ea) of casein hydrolysis and temperature quotient (Q10) were found to be 4.098 kJ/mol and 1.038 - 1.034, respectively, at a temperature ranging from 35 oC to 65 oC. The results of the residual activity test allowed estimating activation energy for irreversible inactivation of the protease (denaturation) which was approximately Ea(d) = 62.097 kJ/mol. The thermodynamic parameters for the enzyme irreversible denaturation were as follow enthalpy (59.286 ≤ΔH*d≥ 59.535 kJ/mol), Gibbs free energy (97.375 ≤ ΔG*d≥ 93.774kJ/mol), and entropy (-122.797 ≤ ΔS*d≥ -101.992 kJ/mol). These thermodynamic parameters inferred that the thermo-stable proteases could be potentially important for industrial application, for example, in the detergent industries.Abstrak: Pada penelitian ini, kinetika protease ekstraseluler termo-stabil yang diproduksi oleh Bacillus licheniformis (ATCC 12759), yang dikultur dalam media yang diperkaya serum lateks skim diselidiki. Enzim stabil hingga 65 oC setelah diinkubasi selama 60 menit pada pH 8. Lineweaver-Burk menunjukkan vmax (laju maksimum) adalah 37.037 U/mg min-1 dan KM (konstanta Michaelis-Menten) 8.519 mg/mL. Energi aktivasi (Ea) dari hidrolisis kasein dan suhu quotient (Q10) ditemukan masing-masing sebesar 4.098 kJ/mol dan 1.038 - 1.034, pada suhu yang berkisar dari 35 oC hingga 65 oC. Hasil uji aktivitas residu memungkinkan estimasi energi aktivasi untuk inaktivasi ireversibel dari protease (denaturasi) yang kira-kira Ea (d) = 62.097 kJ/mol. Parameter termodinamika untuk denaturasi enzim ireversibel adalah sebagai berikut entalpi (59.286 ≤ΔH * d≥ 59.535 kJ / mol), energi bebas Gibbs (97.375 ≤ ΔG * d≥ 93.774kJ / mol) dan entropi (-122.797 ≤ ΔS * d≥ -101.992 kJ / mol). Parameter termodinamika pada penelitian ini menyimpulkan bahwa protease termo-stabil dapat berpotensi penting untuk aplikasi industry seperti dalam industri deterjen.

Peculiarities of thermal denaturation of OmpF porin from Yersinia ruckeri

Irreversible denaturation of membrane proteins in detergent solutions is similar to unfolding of water-soluble multidomain proteins and represents a complex, multistage process.

Biochemical Characterization, Thermal Stability, and Partial Sequence of a Novel Exo-Polygalacturonase from the Thermophilic Fungus Rhizomucor pusillus A13.36 Obtained by Submerged Cultivation

This work reports the production of an exo-polygalacturonase (exo-PG) by Rhizomucor pusillus A13.36 in submerged cultivation (SmC) in a shaker at 45°C for 96 h. A single pectinase was found and purified in order to analyze its thermal stability, by salt precipitation and hydrophobic interaction chromatography. The pectinase has an estimated Mw of approximately 43.5–47 kDa and optimum pH of 4.0 but is stable in pH ranging from 3.5 to 9.5 and has an optimum temperature of 61°C. It presents thermal stability between 30 and 60°C, has 70% activation in the presence of Ca2+, and was tested using citrus pectin with a degree of methyl esterification (DE) of 26%. Ea(d) for irreversible denaturation was 125.5 kJ/mol with positive variations of entropy and enthalpy for that and ΔG(d) values were around 50 kJ/mol. The hydrolysis of polygalacturonate was analyzed by capillary electrophoresis which displayed a pattern of sequential hydrolysis (exo). The partial identification of the primary sequence was done by MS MALDI-TOF and a comparison with data banks showed the highest identity of the sequenced fragments of exo-PG from R. pusillus with an exo-pectinase from Aspergillus fumigatus. Pectin hydrolysis showed a sigmoidal curve for the Michaelis-Menten plot.