Sharif Digital Repository

Penicillin G Acylase is the key enzyme in producing semi-synthetic antibiotics such as Ampicillin and Amoxicillin. In this study, we used E.coli ATCC 11105 in order to produce it. This enzyme was an intracellular one which was produced under suitable conditions. Crude enzyme was released after cell disruption by ultrasonic waves (sonication method) and was partially purified by ammonium sulphate precipitation. Immobilization is investigated at different pHs around the iso-electric pH of Penicillin G Asylase enzyme. Therefore, optimum pH and optimum concentration of ammonium sulphate cuts were determined. Also immobilization process of this enzyme was studied on chitosan polymer, activated by... 

In this study, Pseudomonas aeruginosa BBRC-10036 was used for lipase production. The organism secreted the enzyme extracellulary. First of all, effect of initial pH of the culture broth on lipase activity was studied in order to determine the optimum condition for lipase production. After production, this enzyme must be separated from culture and after that the enzyme must be purified for using in analysis and industry. Different methods are used for purification of the enzyme. In this research, first precipitation was used and then this lipase has been purified by Ion exchange Chromatography leading to 2.33- fold purification and 11.47% recovery. In precipitation by acetone, maximum... 

This thesisconsiders new fundamental approaches to yield heterogeneous catalysts in to three sections. The first section described the immobilization of the molybdenum-Schiff base complexes in pores of SBA-15 in two different methodologies depending on the actual structure of the complexes., (i) stepwise formation of the complex by initial covalent anchoring of one of the components and consecutive solid phase synthesis consisting of the condensation of the other components of the salen complex (iii) one-step complex immobilization by covalent binding through the ligand.Based on the first methodology, we report the preparation of ordered mesoporous silica SBA-15 containing a molybdenum... 

The enzyme L-asparaginase (L-asparagine amidohydroxylase , EC 3.5.1.1) is utilizable in the treatment of acute childhood lymphoblastic leukaemia. L-asparaginase catalyses the hydrolysis of the amino acid L- asparagines to L-aspartic acid and ammonia. Unlike normal cells,malignant cells which can only slowly synthesize L-asparagine , are killed by lacking exogenous supply. In contrast, normal cells are protected from Asn-starvation due to their ability to produce this amino acid.
In this study , L- asparaginase from E.coli, was immobilized onto a polymeric compound, poly(vinyl alcohol)(PVA) with cross-linking agent glutaraldehyde and calcium alginate beads .. Herein ,with the use of the... 

Ion exchange resins are widely used in nuclear industries. These spent resins result in the production of a large amount of low and intermediate level radioactive wastes, therefore, the treatment and immobilization of spent ion exchange resins are the major problems in the development of nuclear power plants.In this research, in a laboratory scale, we tried to find the suitable procedure and formulation to immobilize a specific group of cation-exchange resins which is used in Bushehr nuclear power plant (AMBERLITE IRN-97H) in the cement matrix. The solidification matrix consists of five constituents: anti sulfate slag type portland cement, cation-exchange resins, diatomite, sodium hydroxide... 

Nowadays , application of enzymes as biocatalysts in wastewater treatment processes is increasing. It is economically important to reuse enzymes and increase their stability in these types of processes. Therefore, was immobilization of enzymes and using them in wastewater treatment have a great importance.In this project, Horseradish peroxidase enzyme, whose effect on phenol removal reactions in other studies has been proven before, was immobilized on the alginate-coated magnetic nanoparticles, to investigate the effect of immobilization on the stability and function of this enzyme for phenol removal. The enzyme was immobilized at the temperature of 25 ° C and pH = 8, according to the data... 

In this research, immobilization method was employed to increase the thermal stability of Chondroitinase ABC I (cABC I) enzyme. In first step, magnetite nanoparticle (Fe3O4) was selected as a support and cABC I enzyme was attached via the adsorption method. The results showed that pH=6.5, temperature 15 ˚C, enzyme-to-support mass ratio 0.75, and incubation time 4.5 hr were the appropriate conditions for immobilizing cABC I enzyme on Fe3O4 nanoparticle. It was also found that the optimum pH for free and immobilized enzymes was 7.6 and 8.0, respectively. The maximum activity of free enzyme was obtained at 25 ˚C, whereas the activity of immobilized enzyme was almost constant in the temperature...