Alkaline thermostable and halophilic endoglucanase from Bacillus licheniformis C108

Aygan A., Karcioglu L., ARIKAN B.

AFRICAN JOURNAL OF BIOTECHNOLOGY, cilt.10, sa.5, ss.789-796, 2011 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 10 Sayı: 5
  • Basım Tarihi: 2011
  • Dergi Adı: AFRICAN JOURNAL OF BIOTECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Aquatic Science & Fisheries Abstracts (ASFA), Biotechnology Research Abstracts, CAB Abstracts, Pollution Abstracts, Veterinary Science Database
  • Sayfa Sayıları: ss.789-796
  • Çukurova Üniversitesi Adresli: Evet

Özet

An endoglucanase was purified from halophilic alkaline Bacillus licheniformis isolated from soils of Lake Van in Turkey. The optimal pH and temperature of the endoglucanase produced by B. licheniformis C108 were 10.0 and 30 degrees C, respectively. The enzyme was highly stable up to 100 C at pH 10.0 and the enzyme retained its complete activity for 6 h in 7 to 10% of NaCl. The activity of the enzyme was significantly inhibited by sodium dodecyl sulfate (SDS), Triton X-100, zinc chloride (ZnCl2), phenylmethanesulfonylfluoride (PMSF) and Urea. The partially purified enzyme revealed that, products of carboxymethylcellulosic hydrolysis were glucose, cellobiose and other longer cellooligosaccharides. Thermostability, alkalinity, halostability and high hydrolytic capability make this enzyme a potential candidate for environmental bioremedetion and bioethanol production processes from cellulosic biomasses as well as waste treatment processes.