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

YILDIRIM V., BALTACI M. Ö., OZGENCLI I., ŞİŞECİOĞLU M., ADIGÜZEL A., Adiguzel G.

Journal of Enzyme Inhibition and Medicinal Chemistry, cilt.32, sa.1, ss.468-477, 2017 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 32 Sayı: 1
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1080/14756366.2016.1261131
  • Dergi Adı: Journal of Enzyme Inhibition and Medicinal Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.468-477
  • Anahtar Kelimeler: Thermotolerant, Aeribacillus pallidus, alkaline serine protease, biochemical characterization, purification, SOLVENT-STABLE PROTEASE, SOLID-STATE FERMENTATION, ORGANIC-SOLVENT, MOLECULAR CHARACTERIZATION, BACILLUS-SUBTILIS, OPTIMIZATION, HALOALKALINE, SALT
  • Atatürk Üniversitesi Adresli: Evet

Özet

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 degrees 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 degrees 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. K-M and V-max values were calculated as 0.197 mg/mL and 7.29 lmol. mL(-1). min(-1), respectively.