Partial purification and characterisation of endoglucanase from an edible mushroom, Lepista flaccida

ELVAN H., Ertunga N., Yildirim M., ÇOLAK A.

FOOD CHEMISTRY, vol.123, no.2, pp.291-295, 2010 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 123 Issue: 2
  • Publication Date: 2010
  • Doi Number: 10.1016/j.foodchem.2010.04.034
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.291-295
  • Keywords: Characterisation, Endoglucanase, Lepista flaccida, Mushroom, POLYPHENOL OXIDASE, TRICHODERMA-REESEI, CELLULASES, BACTERIUM
  • Karadeniz Technical University Affiliated: Yes


A crude extract was prepared from the fruiting body of Lepista flaccid, an edible mushroom and endoglucanase activity of the extract was increased 14-fold with ammonium sulphate precipitation. Maximum enzyme activity was seen at pH 4.0 and 50 degrees C when carboxymethylcellulose was used as a substrate. K-0.5 and V-max values of the partially purified endoglucanase were 7.7 mg/ml and 25 +/- 0.9 U/mg protein, respectively. The enzyme was quite stable over a broad range of pH (2.0-9.0) at 4 degrees C. When it was incubated at temperatures between 20 degrees C and 60 degrees C for 12 h, it conserved much of its original activity (over 40%). The activity of the enzyme increased by 234 +/- 3.6% in the presence of 1 mM Mn2+. The endoglucanase was inhibited by EDTA, PMSF, beta-ME and DDT. In conclusion, pH and thermal stability of the L. flaccida endoglucanase could make it useful for industrial purposes. (C) 2010 Elsevier Ltd. All rights reserved.