Papers by Abdollah Ghasemian
Cloning, purification and enzymatic assay of streptokinase gene from Streptococcus pyogenes in Escherichia coli
Minerva Biotechnology and Biomolecular Research, 2016
Streptokinase is an important therapeutic enzyme that acts as a fibrinolytic agent and use in the... more Streptokinase is an important therapeutic enzyme that acts as a fibrinolytic agent and use in the treatment of multi serious and life threatening diseases such as pulmonary embolism and acute myocardial infarction. Cloning and extracellular expression of recombinant streptokinase from Streptococcus pyogenes was done by fusing the gene coding for streptokinase to an efficient vector (pET15b) with NdeI and BamHI as restriction enzymes and T4 DNA ligase. Streptokinase activity was determined using synthetic chromogenic substrate S-2251, and measuring the absorbance at 405 nm in a UV-spectrophotometer; and purification done under N-terminal 6× histidine tag complementation using affinity chromatography. A 1323-bp of the structural streptokinase gene was amplified. The DNA and amino acid sequence alignments resulting from the BLAST search of streptokinase showed high sequence identity with the other strains of S. pyogenes. The recombinant enzyme had the same molecular weight as other reported streptokinase and the E. coli transformants showed high streptokinase activity. Comparative clinical trials and cost-effectiveness considerations between several major available thrombolytic agents suggest that streptokinase is the drug of choice for thrombolytic therapy particularly in the poorer economies.
International Journal of Health Sciences (IJHS), Oct 16, 2022
Urate oxidase is a peroxisomal enzyme with four equal subunits that convert uric acid to allantoi... more Urate oxidase is a peroxisomal enzyme with four equal subunits that convert uric acid to allantoin, a more soluble metabolite for excretion. The usage of uricase as a drug in medicine is to treat hyperuricemia. Many microorganisms have been used for uricase production such as Streptomyces exfoliates, Pseudomonas aeruginosa, and Aspergillus flavus. In this study, soil samples were collected and then cultured in a screening medium including uric acid as the sole carbon source. Samples with the higher ability of uricase production were selected for enzyme assay. Enzyme activity was measured by spectrophotometry and the sample with the maximal uricase activity was identified as Aspergillus niger and selected for further studies. According to the results of experiments, the optimized temperature for enzyme production by Aspergillus niger was determined to be 35±2°C. 47963 The best carbon and nitrogen source was glucose and NH4NO3, and the highest enzyme activity was observed in the presence of Cu 2+ ion.
Antibiofilm activity of a natural bacteriophage against multi-drug resistant Pseudomonas aeruginosa
MDPI, Apr 26, 2021
The human RECQ1 helicase is highly expressed in glioblastoma and plays an important role in tumor... more The human RECQ1 helicase is highly expressed in glioblastoma and plays an important role in tumor cell proliferation
The human RECQ1 helicase is highly expressed in glioblastoma and plays an important role in tumor... more The human RECQ1 helicase is highly expressed in glioblastoma and plays an important role in tumor cell proliferation
Production of Recombinant Microbial Thermostable Lipases
New and Future Developments in Microbial Biotechnology and Bioengineering, 2019
Microbial thermostable lipases are biotechnologically valuable biocatalysts. They perform a diver... more Microbial thermostable lipases are biotechnologically valuable biocatalysts. They perform a diverse range of reactions, including hydrolysis, esterification, interesterification transesterification, alcoholysis, acidolysis, and aminolysis. They are used in a broad spectrum of industrial applications ranging from the formulation of biological laundry detergents, flavor improvement in food and food additives, chemical synthesis in the oleochemical industry, mitigation of environmental pollution, resolving the pitch problem in the pulp and paper industry, biosensors in medical diagnosis, and as the active ingredient in pharmaceiticals. The expression of thermostable lipases in the heterologous recombinant hosts is the most appropriate, and in some cases the sole, approach to improving the production of these enzymes. In this chapter, the most common strategies for the expression of thermostable lipases in prokaryotic (Escherichia coli) and eukaryotic hosts (Saccharomyces cerevisiae and...
Iranian Journal of Basic Medical Sciences, 2020
Objective(s): Bacteriophages are infectious replicating entities that are under consideration as ... more Objective(s): Bacteriophages are infectious replicating entities that are under consideration as antimicrobial bioagents to control bacterial infections. As an alternative or supplement to antibiotics, bacteriophages can be used to circumvent the resistance to existing antibiotics. The aim of this study was to assess the synergistic effect of a naturally isolated phage and ampicillin against Escherichia coli O157. Materials and Methods: In the present study, a natural phage against E. coli O157 was isolated, the morphology and molecular characteristics of the phage were identified, and the combination of bacteriophage and antibiotic to combat clinically isolated drug-resistant E. coli O157 was evaluated. Results: The results showed the synergistic action between a naturally isolated phage and ampicillin in solid (disk diffusion test) and liquid culture media. Addition of the isolated phage, gT0E.co-MGY2, to the microbial lawn of bacteria in modified antibiotic disk diffusion test, a...
Phage therapy: Current development and future prospects
New and Future Developments in Microbial Biotechnology and Bioengineering, 2020
Abstract Phage therapy is the application of bacteriophages (phages) or bacterial viruses as anti... more Abstract Phage therapy is the application of bacteriophages (phages) or bacterial viruses as antibacterial agents. Prior to the discovery of penicillin by Fleming in 1929, phages have been used for control or eradication of bacterial infection in Eastern countries. However, the synthesis of broad-spectrum antibiotics repressed the research on phage therapy. Rediscovery of phage therapy, especially in Western countries, was induced by developing multidrug-resistance bacteria. Phages, with their pros and cons, show great potential as alternative or synergistic agents to chemical antibiotics to treat bacterial infection in situations where antibiotic therapy is ineffective. In this chapter, we describe the current development and future prospects of phage therapy, discuss the concerns about phage therapy, and suggest some solutions to avoid or circumvent the problems.
Microbial Products and Biotechnological Applications Thereof: Proteins, Enzymes, Secondary Metabolites, and Valuable Chemicals
Microbial Interventions in Agriculture and Environment, 2019
Microbial species are among prominent producers of useful natural products, which are a very dive... more Microbial species are among prominent producers of useful natural products, which are a very diverse collection of molecules. These natural products or better defined as specialized metabolites occur in various structural and functional classes and have been used by humans historically for different purposes: pharmaceuticals, chemical industry, agriculture, food and feed sector, etc. To the best of our knowledge, only a small fraction of microbial products is exploited and yet remains a larger chest to be reached. The most advantageous microbial products not only are restricted to useful proteins and enzymes, antibiotics, antitumor agents, immunosuppressants but also include antivirals, anthelmintics, nutraceuticals, polymers, enzyme inhibitors, surfactants, bioherbicides, biopesticides, and many more agricultural and industrial products.
N-Acetyl Cysteine and Metal Nanoparticles Internalization: A Critical Methodological Aspect
Journal of Bionanoscience, 2018
Journal of Applied Pharmaceutical Science, 2017
Escherichia coli O157 is one of the common and problematic pathogens, particularly in developing ... more Escherichia coli O157 is one of the common and problematic pathogens, particularly in developing countries. To isolate a phage against this pathogen, a total of 32 water samples were enriched for phage and two of these samples were found to contain lytic phages that grow on and kill enterohaemorrhagic E. coli serotype O157. Following the primary evaluation, the most efficient phage was chosen for further characterization. The multiplicity of infection, morphology, killing efficiency and bacterial host range were determined under controlled conditions in the laboratory. Isolated phage was designated gBSN-MGB13. According to transmission electron microscopy, this lytic phage morphologically belonged to the myoviridae family. Based on phage efficiency test, a multiplicity of infection of 5 logs of gBSN-MGB13 resulted in 50% reduction in viable bacterial cell count after 20 min incubation in 37 °C without shaking. Since gBSN-MGB13 is a broadhost range phage and effective against several pathogenic species, E. coli O157 as well as Proteus vulgaris and Pseudomonas aeruginosa, its applications could be investigated in complex infections as combinatory therapy. This is an exciting aspect of phage therapy.
Research in Pharmaceutical Sciences, Aug 30, 2012
Background and Aims: Streptokinase is an important therapeutic enzyme that acts as a fibrinolytic... more Background and Aims: Streptokinase is an important therapeutic enzyme that acts as a fibrinolytic agent and use in the treatment of multi serious and life threatening diseases such as pulmonary embolism and acute myocardial infarction. Cloning and extracellular expression of recombinant streptokinase from Streptococcus pyogenes was done by fusing the gene coding for streptokinase to an efficient vector (pET15b) with NdeI and BamHI as restriction enzymes and T4 DNA ligase. Streptokinase activity was determined using synthetic chromogenic substrate S-2251, and measuring the absorbance at 405 nm in a UV-spectrophotometer; and purification done under N-terminal 6× histidine tag complementation using affinity chromatography. A 1323-bp of the structural streptokinase gene was amplified. The DNA and amino acid sequence alignments resulting from the BLAST search of streptokinase showed high sequence identity with the other strains of S. pyogenes. The recombinant enzyme had the same molecular weight as other reported streptokinase and the E. coli transformants showed high streptokinase activity. Comparative clinical trials and cost-effectiveness considerations between several major available thrombolytic agents suggest that streptokinase is the drug of choice for thrombolytic therapy particularly in the poorer economies.
World Journal of Microbiology and Biotechnology, 2005
The bioconversion of hydrocortisone by a locally isolated strain of cyanobacterium Fischerella am... more The bioconversion of hydrocortisone by a locally isolated strain of cyanobacterium Fischerella ambigua PTCC 1635 was investigated. Fischerella ambigua had not been previously examined for this potential. The fermentation led to production of 11b,17a, 20b, 21-tetrahydroxypregn-4-en-3-one and 11b-hydroxyandrost-4-en-3,17-dione. The metabolites were isolated and purified by chromatographic methods and identified using instrumental analyses.
Algal transformation of hydrocortisone by the cyanobacterium Nostoc ellipsosporum
Chemistry of Natural Compounds, 2006
Abstract The potential of Nostoc ellipsosporum for biotransformation of hydrocortisone was studie... more Abstract The potential of Nostoc ellipsosporum for biotransformation of hydrocortisone was studied. The microorganism was isolated during a screening program from soil samples collected from the paddy fields in the north of Iran and had not been previously examined for this purpose. The biotransformation yielded 11β, 17α, 20β, 21-tetrahydroxypregn-4-en-3-one and 11β-hydroxyandrost-4-ene-3, 17-dione. Both of the metabolites were purified chromatographically and characterized using instrumental analyses.
14. Cyanobacteria: biotechnological and environmental applications
Microbial Applications, 2016
Purification and Characterization of ExtraCellular Cholesterol Oxidase From Rhodococcus sp. PTCC 1633
Biotechnology(faisalabad), 2008
J Biotechnol, 2010
The animal by-products industry is a vital part of the world food production chain, providing val... more The animal by-products industry is a vital part of the world food production chain, providing valuable new products, while reducing pollution load. Bones and meat trimmings can contain up to 10% of a valuable and easily accessible proteins. Although their mechanical separation is inefficient, solubilisation by enzymatic proteolysis provides almost quantitative extraction of proteins/peptides to the liquid phase, whereby the biologically valuable compounds are preserved because of the mild treatment conditions.
Protein engineering of microbial cholesterol oxidases: a molecular approach toward development of new enzymes with new properties
Applied Microbiology and Biotechnology, 2016
Cholesterol oxidase, a flavoenzyme, catalyzes two reactions in one active site: oxidation and iso... more Cholesterol oxidase, a flavoenzyme, catalyzes two reactions in one active site: oxidation and isomerization. This enzyme has been isolated from a variety of microorganisms, mostly from actinomycetes. This enzyme has been widely used in clinical laboratories for cholesterol assays and was subsequently determined to have other potential applications. Engineering of cholesterol oxidase have enabled the identification of critical residues, and the information derived could lead to the rational development of improved types of the enzyme with increased stability and better functional properties. This review is the first that exclusively summarizes the reported results on the engineering of bacterial cholesterol oxidases aimed at improving their thermal and chemical stability, catalytic activity, and substrate specificity.
Phylogeny of urate oxidase producing bacteria: on the basis of gene sequences of 16S rRNA and uricase protein
Iranian Journal of Pharmaceutical Sciences, Mar 1, 2012
Increased expression of recombinant cholesterol oxidase in Escherichia coli by optimization of culture condition using response surface methodology
Minerva Biotecnologica
Increased expression of recombinant cholesterol oxidase in Escherichia coli by optimization of cu... more Increased expression of recombinant cholesterol oxidase in Escherichia coli by optimization of culture condition using response surface methodology Moradpour Z. 1, Ghasemian A. 1, 2, Nouri F. 1, 2, Ghasemi Y. 1, 2 1 Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Urmia University of Medical Sciences, Urmia, Iran; 2 Pharmaceutical Sciences Research Center, Faculty of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran AIM: The FAD-containing enzyme, cholesterol oxidase (EC 1.1.3.6) is an enzyme that catalyses sequential reactions which convert cholesterol (5-cholesten-3-b-ol) to 4-cholesten-3-one with concomitant reduction of oxygen to hydrogen peroxide. In fact, this enzyme catalyzes two reactions in one active site: oxidation and isomerization. Cholesterol oxidase is an industrially and commercially important enzyme. METHODS: Response surface methodology that uses quantitative data from appropriate experiments was applied to optimize the culture condition...
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Papers by Abdollah Ghasemian