Characterization of an acid-tolerant -1,4-glucosidase from Fusarium oxysporum and its potential as an animal feed additive. Academic Article uri icon


  • An extracellular -glucosidase (BGL) from Fusarium oxysporum was purified to homogeneity by a single chromatography step on a gel filtration column. The optimum activity of BGL on cellobiose was observed at pH 5.0 and 60 C. Under the same conditions, the K(m) and V(max) values for p-nitrophenyl -D-glucopyranoside and cellobiose were 2.53 mM, 268 U mg protein(-1) and 20.3 mM, 193 U mg protein(-1), respectively. The F. oxysporum BGL enzyme was highly stable at acidic pH (t 1/2 = 470 min at pH 3). A commercial BGL Novo188 (Novozymes) and F. oxysporum BGL were compared in their ability to supplement Celluclast 1.5 L (Novozymes). In comparison with the commercial Novo188 (267 mg g substrate(-1)), F. oxysporum BGL supplementation released more reducing sugars (330 mg g substrate(-1)) from cellulose under simulated gastric conditions. These properties make F. oxysporum BGL a good candidate as a new commercial BGL to improve the nutrient bioavailability of animal feed.

published proceedings

  • Appl Microbiol Biotechnol

author list (cited authors)

  • Zhao, Z., Ramachandran, P., Kim, T., Chen, Z., Jeya, M., & Lee, J.

citation count

  • 12

complete list of authors

  • Zhao, Zongpei||Ramachandran, Priyadharsini||Kim, Tae-Su||Chen, Zhilei||Jeya, Marimuthu||Lee, Jung-Kul

publication date

  • January 2013