Production, purification and characterization of novel fibrinolytic enzyme from Bacillus atrophaeus V4

Varol A., ALBAYRAK Ş., ÖZKAN H., Demir Y., TAŞKIN M., ADIGÜZEL A.

Biologia, cilt.78, sa.2, ss.591-600, 2023 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 78 Sayı: 2
  • Basım Tarihi: 2023
  • Doi Numarası: 10.1007/s11756-022-01281-7
  • Dergi Adı: Biologia
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Animal Behavior Abstracts, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Veterinary Science Database
  • Sayfa Sayıları: ss.591-600
  • Anahtar Kelimeler: Microbial, Fibrinolytic enzyme, Optimization, Molecular weight, BIOCHEMICAL-CHARACTERIZATION, PROCESS OPTIMIZATION, STRAIN
  • Atatürk Üniversitesi Adresli: Evet

Özet

© 2022, The Author(s), under exclusive licence to Plant Science and Biodiversity Centre, Slovak Academy of Sciences (SAS), Institute of Zoology, Slovak Academy of Sciences (SAS), Institute of Molecular Biology, Slovak Academy of Sciences (SAS).This study was performed to investigate the fibrinolytic enzyme-producing potentials of locally isolated soil bacteria and to purify and characterize the fibrinolytic enzyme of the most potent bacterial isolate. Among 40 isolates, the isolate V4 was found to have the highest potential to produce the fibrinolytic enzyme. According to 16 S rRNA sequence analysis, the isolate V4 was identified as Bacillus atrophaeus (GenBank number: OL662991). The optimal parameters for fibrinolytic enzyme production from B. atrophaeus were determined as a skim milk powder concentration of 15 g/L, an initial pH of 7.0, a temperature of 35 °C and an incubation time of 72 h. The molecular weight of the purified enzyme was calculated as 36 kDa. After ammonium sulphate precipitation, ion-exchange chromatography and gel filtration chromotography-based processes, the specific activity of the fibrinolytic enzyme was determined as 6414.7 U/mg. The purified enzyme showed the maximum activity at pH 7.0 and 35 °C. The enzyme was inhibited by PMSF and EDTA. The substrate specifity of the enzyme was in the following order; fibrin (62.3 U/mg) > fibrinogen (46.2 U/mg) > casein (42.1 U/mg) > serum albumin (6.8 U/mg). This is the first report on the fibrinolytic enzyme production potential of the species B. atrophaeus.