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Showing 2 results for Ebrahimipour

Mohsen Shahriari Moghadam, Behrooz Abtahi, Gholamhossein Ebrahimipour,
Volume 6, Issue 2 (8-2019)
Abstract

Organisms in different environmental conditions express different genes, which result in different protein expressions. These changes result from the adaptation of the organism to environmental conditions such as the presence of toxic substances. This study aimed to investigate the changes in protein expression in Celeribacter persicus SBU1 isolated from Nayband Bay mangrove forests, cultured in the medium containing phenanthrene as the sole source of carbon and energy. For this purpose, C. persicus SBU1 was cultured on mineral salt medium containing phenanthrene and sodium acetate as treatment and control, respectively. After the extraction of total protein, changes in protein expression were evaluated by SDS-PAGE. Proteins were identified by MALDI-TOF-TOF MS. After evaluating changes in protein content, two bands which showed greater variation in comparison with the control treatment (increased protein expression) were detected. The identified proteins included one ligand-gated channel protein and one unknown protein. In general, the results of this study showed significant changes in the protein content of C. persicus SBU1 after using phenanthrene. The up-regulation of ligand-gated channel protein signified the role of this protein in phenanthrene molecules transport in and out of the cells.

Mahnaz Nasre Taheri, Gholamhossein Ebrahimipour, Hossein Sadeghi,
Volume 6, Issue 3 (10-2019)
Abstract

Proteases are important industrial enzymes used in different areas of industry, mainly detergent, food and leather industries. In this study, novel alkaline protease-producing bacterium was isolated from Geinarje hot spring and examined for maximum protease activity to be utilized in washing-powder. The isolated bacterium was cultured in mineral salt medium including 2% Skim Milk. Proteolytic activity of supernatant was measured by caseinolytic method. The effects of pH, temperature, SDS, Tween 80 and EDTA on protease stability and activity were investigated. The detergent compatibility of protease was assayed. On the basis of phylogenetic analysis and morphological as well as biochemical tests, the isolate was identified as a new strain of Brevibacillus borstelensis capable of generating extracellular alkaline protease. The generated protease was determined as alkaline metallo-protease having high activity at 60 oC and pH 9. Moreover, the alkaline protease was stable in the presence of SDS, Tween 80 and H2O2. It is compatible with commercial detergents. Finding proteases capable of degrading proteins in extreme environment (i.e. alkaline pH, high temperature and presence of surfactants) is valuable in biotechnological and industrial practices. Therefore, it can be utilized in detergent formulation in the future.

 



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