Sharif Digital Repository

We introduce a new smooth, non-toxic, biocompatible method for cross-linking of gum tragacanth (GT), a polysaccharide of natural origin, in order to serve as a new supporting matrix for immobilization systems. The modified gum is used as a matrix for the catalysis of the conversion of benzyl penicillin to 6-aminopenicillanic acid (6-APA) by means of Escherichia coli ATCC11105 with penicillin G acylase (PGA) activity. The results show that GT beads can not only serve as a proper matrix for immobilization, but show enhanced hydrolysis rate and stability compared to other immobilization systems used for this reaction. This signifies the potential of GT as a biocompatible matrix for... 

Different techniques including toluene-ethanol, guanidine hydrochloride, guanidine hydrochloride-EDTA, lysozyme, lysozyme-EDTA and sonication treatments were used to extract penicillin G acylase from Escherichia coli ATCC 11105 cells. The obtained results show that penicillin G acylase extraction by guanidine-EDTA treatment is more specific in comparison to the other applied methods. The maximum specific activity of the enzyme (5.61 U/mg), i.e. the maximum purification was found when 1 M guanidine + 100 mM EDTA solution was used for penicillin G acylase extraction at culture condition including 0.50% (w/v) yeast extract as carbon source. In such a condition more than 95% of the enzyme was... 

Immobilization of enzymes on nonporous supports provides a suitable model for investigating the effect of external mass transfer limitation on the reaction rate in the absence of internal diffusional resistance. In this study, deacylation of penicillin G was investigated using penicillin acylase immobilized on ultrafine silica particles. Kinetic studies were performed within the low-substrate-concentration region, where the external mass transfer limitation becomes significant. To predict the apparent kinetic parameters and the overall effectiveness factor, knowledge of the external mass transfer coefficient, kLa, is necessary. Although various correlations exist for estimation of kLa, in... 

The kinetics of the enzymic reaction of penicillin G acylase from a mutant of Escherichia coli ATCC 11105 in forward and reverse directions were studied and the kinetic constants determined. Results show that the enzyme is inhibited by excess substrate, penicillin G (Pen G), and by both products. The non-competitive inhibition by 6-aminopenicillanic acid (6-APA) and competitive inhibition by phenylacetic acid were observed for the ordered uni bi deacylation reaction in the forward direction. The optimum pH value for the reverse acylation reaction was 5.7. The bi uni mechanism for the reverse reaction was investigated and the inhibitory effects of the substrates, 6-APA and phenyl acetic acid,... 

E.coli was immobilized by entrapment within calcium alginate beads using cell suspensions of different concentrations. The immobilization procedure resulted in beads with a homogeneous cell distribution, referred to as a Non-overlapping Cell (NC) configuration. If cells within the beads were allowed to grow, the NC configuration would transform into a Clustered Cell (CC) configuration as a, result of cell growth. Enzyme activity and substrate conversion were obtained for NC and CC configurations of different cell density, using penicillin G acylation by penicillin G acylase, to produce. 6-amino penicillanic acid. Enzyme activity and conversion were found to depend on both cell concentration... 

The partitioning of penicillin G acylase in aqueous two-phase systems (ATPS's) containing poly(ethylene glycol) (PEG) 20000 or 35000 and potassium dihydrogen phosphate (KH2PO4) or sodium citrate (C 6H5Na3O7 ·5H2O) has been measured at three temperatures, (301.2, 307.2, and 310.2) K. The effects of temperature, polymer molecular weight, and polymer and salt concentrations on the partitioning of penicillin G in the ATPS were studied. The experimental data showed that the composition of salt has a large effect on partitioning of penicillin G in ATPS, and the temperature of the system has a small effect on the partitioning. The UNIFAC-FV group contribution model (Pazuki et al., Ind. Eng. Chem.... 

Penicillin G is an active pharmaceutical ingredient of great importance in health sectors. Meanwhile, because of its huge quantity production and resistance to biodegradability, this antibiotic is ubiquitously presented in aquatic environment. In this study, the degradation of effluent wastewater from Penicillin G production plant by Photo- Fenton process and Ultrasound process (Sonolysis) was investigated, the effects of different process variables in both methods were evaluated and at last the degradation of Pen-G by these two processes in the optimum conditions was compared. Pen-G concentration and Chemical Oxygen Demand (COD) were selected as the environmental parameters to follow the... 

The synthesis of amoxicillin with immobilized penicillin G acylase (PGA) in aqueous medium was investigated. The parameters studied were: time course of amoxicillin production, concentration of substrates: hydroxyphenylglycine methyl ester (HPGM) and 6-aminopeicillanic acid (6-APA) and the. effect of enzyme (PGA) content and pH, under variable and constant conditions and temperature variations. In the study of two substrate concentration on amoxicillin production, impressive results were obtained for a 1/3 ratio of 6-amino penicillanic acid (6-APA) and hydroxyl-phenylglycine methyl ester (HPGM). The. synthesis of amoxicillin was preferable at constant pH rather than a variable one. Other...