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Showing 3 results for Stability

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.

 


Ali Bahrami, Bita Jenabzadeh, Hamid Mosmeri, Mohammad Davoud Ghafari,
Volume 7, Issue 1 (4-2020)
Abstract

Phenazine 1-corboxylic acid (PCA) is an antibiotic, which inhibits the growth of a vast number of micro-organisms. PCA has has been applied in fields such as pharmaceutical, agricultural, marine and chemical industries. In this study, the antibiotic properties of PCA (produced by pseudomonas aeruginosa MUT.3, which is kept at the Microbial Collection of Malek Ashtar University of Technology) was studied. The impacts of temperature and light conditions on the activity of PCA was investigated within a 230-day period. To investigate the rate of PCA destruction in the experiment, high performance liquid chromatography (HPLC) was utilized. Moreover, the antibacterial activity of PCA under various conditions was studied by minimum inhibitory (MIC) and minimum biocidal concentration (MBC) methods against E. coli DH5α. The results showed that PCA could be active up to 210 days in darkness (at 25oC). Meanwhile, the antibacterial activity of PCA was reduced to 100 and 50 days by increasing the temperature to 35 and 45oC, respectively. In addition, PCA could be active up to 120 and 10 days in visible and ultraviolet light condition, respectively. The MIC and MBC data were consistent with the HPLC results. Detailed data on the activity and stability of phenazine 1-corboxylic acid under various environmental conditions, as presented in this study, could be helpful in industries and healthcare services.
 
 


Faezeh Ranjbar, Dr Nikoo Nasoohi, Dr Khosro Khajeh,
Volume 12, Issue 2 (9-2025)
Abstract

Basic fibroblast growth factor (bFGF), also known as FGF-2, is a crucial member of the fibroblast growth factor family, involved in a variety of biological functions including cellular proliferation, wound healing, angiogenesis, intercellular signalling, and cell differentiation, In contemporary stem cell research, serum-free media enriched with various additives and growth factors are employed, and among these, bFGF being particularly significant. Despite its extensive potential applications, the clinical utilization of bFGF is limited due to its instability, especially in aqueous environment. Therefore, a thorough investigation of the protein's structural integrity and stability is essential. This study focuses on the expression, purification, and characterization of bFGF for structural and stability analysis through biophysical methods. Intrinsic fluorescence measurement indicated a structural alteration surrounding the tryptophan residue, while circular dichroism (CD) analysis showed a decrease in the protein’s secondary structure. The differential scanning calorimetry (DSC) used for stability analysis. Furthermore, the study aims to evaluate the biological activity of the protein in cellular context. For this purpose, gold nanoparticles were synthesized. The results from the Cell Migration Assay indicated that the proliferation of HT29 cells was enhanced following treatment with bFGF in conjunction with gold nanoparticles. Also, a MTT assay was conducted.

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