Journal Article

Purification and biochemical characterization of a novel thermostable serine alkaline protease from Aeribacillus pallidus C10: a potential additive for detergents

Yildirim, Vildan, Adiguzel, Ahmet, Ozgencli, Ilknur, Sisecioglu, Melda, Adiguzel, Gulsah, Mustafa Ozkan Baltaci

2017

Overview

An extracellular thermostable alkaline serine protease enzyme from Aeribacillus pallidus C10 (GenBank No: KC333049), was purified 4.85 and 17. 32-fold with a yield of 26.9 and 19.56%, respectively, through DE52 anion exchange and Probond affinity chromatography. The molecular mass of the enzyme was determined through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with approximately 38.35 kDa. The enzyme exhibited optimum activity at pH 9 and at temperature 60 °C. It was determined that the enzyme had remained stable at the range of pH 7.0–10.0, and that it had preserved more than 80% of its activity at a broad temperature range (20–80 °C). The enzyme activity was found to retain more than 70% and 55% in the presence of organic solvents and commercial detergents, respectively. In addition, it was observed that the enzyme activity had increased in the presence of 5% SDS. KM and Vmax values were calculated as 0.197 mg/mL and 7.29 μmol.mL−1.min−1, respectively.

• Publisher: Taylor & Francis Ltd
• Subject: Affinity chromatography / Detergents / Enzymatic activity / Enzymes / Gel electrophoresis / pH effects / Polyacrylamide / Serine / Serine proteinase / Sodium lauryl sulfate