Details

Autor(en) / Beteiligte

• Satari Faghihi, Leila
• Seyedalipour, Bagher
• Riazi, Gholamhossein
• Ahmady-Asbchin, Salman

Titel

Introduction of Two Halo-Alkali-thermo-stable Biocatalysts: Purification and Characterization

Ist Teil von

• Catalysis letters, 2018-03, Vol.148 (3), p.831-842

Ort / Verlag

New York: Springer US

Erscheinungsjahr

2018

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Halophilic bacterium, producing two extracellular proteases, was isolated from Badab-Sourt, Iran. 16S rDNA analysis shown high similarity with the genera Idiomarina . Maximum secretion of enzymes was observed during the early-stationary phase of bacterial growth. Both extracellular proteases were purified by three purification steps; ammonium sulfate precipitation, Q-Sepharose, and Sephadex G-200 chromatography columns. The molecular weight of purified enzymes was determined by SDS-PAGE gel electrophoresis with approximate masses of 48 and 51 kDa (45.57 and 80.30 U/mg specific activity). Proteases synthesized by strain S-18 were affected by medium compositions. Optimum concentration of substrate, pH, and temperature for both enzymes activity were 0.5% casein, 9.0, and 50 °C. However, purified proteases showed different activity at various salt concentrations, which their maximum activity was determined in the presence of 7.5 and 5% NaCl. The activity of enzymes increased in the presence of metal ions such as Mn 2+ and Cu 2+ and decreased by the presence of Hg 2+ and Fe 2+ . Both proteases were strongly inhibited by SDS, while DDT, EDTA, and 2-Mercaptoethanol could stimulate their activity. The results of present research might be interesting issue for industrial applications and biotechnological processes. Graphical Abstract