This study was designed to evaluate the ability of Saccharomyce buolardi as effective probiotic against Shiegella flexneri. Mice treated with S. boulardii and infected with Sh. flexneri, then serum levels of Aspartate aminotransferase (AST) and Alanine aminotransferase (ALT) of treated mice were measured and histological sections were made from liver to evaluate protective effect. Results showed that mice treated with S. boulardii exhibited no significant p≤0.05 differences in serum level of AST and ALT 131,67 respectively U/L in comparison with their levels in serum of control group 113.2, 72.86 U/L. Mice infected with Sh. flexneri showed a significant increase in serum level of AST and ALT 198, 101 U/L in comparison with their levels 113,72 U/L in control group. Mice treated with S. boulardii and infected with Sh. flexneri showed a significant decrease in serum level of AST and ALT in comparison with their levels in mice infected with Sh. flexneri 80.13,78.26 U/L vs. 198 and 101 U/L respectively. Histopathological study showed that infection with Sh. flexneri caused a necrosis, degenerative changes and inflammatory cells infiltration as compared with control, while treatment with S. boulardii prevented the histopathological effect of Sh. flexneri.

Optimum conditions for glutaminase production by Serratia marcescens N1 in glutamine broth medium were studied. Results showed that maximum glutaminase production was achieved when S.marcescens was cultured in production medium supplemented with starch as a sole source for carbon and energy at a concentration of 0.5%, meat extract as a nitrogen source at a concentration of 0.5%, pH8 and inoculated with a count of 2×10 4 CFU/ml of fresh bacterial culture, then incubated in a shaker incubator (150 rpm) at 30 o C for 18 hrs. Under these conditions, specific activity of crude glutaminase produced in culture filtrate was 5.8U/mg protein.

Through the development of advanced, stimulus-responsive pharmacological systems, protein engineering has the potential to alter the metabolic drug landscapes. Protein therapies are a fast growing category of FDA-approved medications that have the potential to improve clinical consequences in the long run. Protein therapeutics engineering is still in its preliminary phase; however recent advancements in protein engineering skills are being used to gain direct monitoring over pharmacodynamics. Drugs that are intended to be metabolized under specific conditions are known as stimulus-responsive protein medicines. Protein engineering is being used to create biochemically based smart therapies that are personalized to the patient's needs. Protein engineering brings a new features and functionality to the bio-chemical and bio-physical modification of proteins to meet the necessities of therapeutic applications. Provided the enormous capability of protein engineering approaches to modify the activity of bio-catalysts, this review summarizes the current studies are showing the advancements and limitations in using these methods to therapeutic enzyme engineering. The current review will concentrate mainly on three types of therapeutic based enzymes: Diagnostic enzymes,  Fibrinolytic enzymes, and pharmaceutical enzymes, in which the protein is the restorative agent, prodrug-activating enzymes, provokes a therapeutic effects, and diagnostic enzymes, in which the remarkable specificity and selectivity  of a protein offer advantages compared to conventional analytical techniques.

L-glutaminase has recently attracted much attention due to its medicinal and industrial potential. It's an antileukemic drug with flavor-enhancing properties when used in fermented foods manufacturing. The enzyme purification was determined by ammonium sulfate precipitation, Ion exchange chromatography and gel filtration chromatography with estimating glutaminase activity and characterization of purified glutaminase in several parameters such as substrate concentration and reaction time pH, and temperature influence in this study. As a result, glutaminase is purified in three steps: ammonium sulfate precipitation with 30% saturation, DEAE-Cellulose and Sephacryl S-200. The specific activity increased to 85 U/mg protein with 4 folds of purification and 18% enzyme recovery. When glutaminase was incubated in the presence of 150 millimolar glutamine at thirty-five centigrade for thirty minutes, the enzyme reached its maximal activity of 1.8 u/ml, in the presence of a 0.05 Molar potassium phosphate buffer solution, at pH 8. Keywords: Capsicum annum, glutaminase, enzyme activity, glutaminase purification

The aim of this research is to evaluate the effect of glucose and sodium chloride on biofilm formation by bacteria causing wound infection. For this purpose, 1% and 2% concentration of each of glucose and sodium chloride were used to test the biofilm formation potential of Staphylococcus aureus and Pseudomonas aeruginosa, which were the most common abundant bacteria that cause infection by biofilm. Each of the concentrations was kept in contact with the pathogenic bacteria for 24 hours. After the period of incubation, the concentration of 1% of glucose enhanced moderate biofilm formation capacity for (66% and 80%) on both bacteria respectively. The concentration of 2% glucose, on the other hand, led to a weak biofilm for 33% and 20% on both bacteria isolates respectively. In respect to the effect of sodium chloride, no isolate was able to form neither moderate nor strong biofilms. Nonetheless, all isolates succeeded in forming weak biofilms at 2% sodium chloride, while treatment with a concentration of 1% sodium chloride led to inhibited biofilm formation for 43% of isolates. Besides, Pseudomonas aeruginosa isolates were able to form moderate biofilms in the presence of 1% concentration of glucose, and weak producers in the presence of 2% glucose concentration. The isolates succeeded in forming strong biofilms at both 1% and 2% sodium chloride.