ARPN Journal of Science and Technology Logo

ARPN Journal of Science and Technology >> Volume 7, Issue 1, January 2017

ARPN Journal of Science and Technology

Isolation and Partial Purification of Cellulase from Rhizopus Stolonifer

Full Text Pdf Pdf
Author M.A. Milala, A. Shugaba, H. Zanna, B. Appollos
ISSN 2225-7217
On Pages 433-438
Volume No. 4
Issue No. 8
Issue Date September 01, 2014
Publishing Date September 01, 2014
Keywords Cellulase, Rhizopus stolonifer, Sawdust and Millet stalk


Cellulase produced by Rhizopus stolonifer isolated from decayed wood was partially purified using ammonium sulphate precipitation and dialysis. Sawdust and millet stalk were the feed substrates and served as carbon sources for the growth of the organism and induction of the enzyme. Cellulase activity was determined at 24 hour interval and lasted for 192 hours using 1% standard cellulose powder as the enzyme substrate at room temperature 281oC and pH 5. The optimum cellulase induction/secretion was achieved at 72 hour incubation period in both feed substrates (millet stalk had 41.8 U/ml and sawdust had 25.3 U/ml cellulase activity respectively). Ammonium sulphate precipitation of the 72 hour culture gave cellulase activity of 33.00U/ml at 80% saturation for millet stalk and 28.00U/ml at 50% saturation in sawdust feed substrate which indicated increase in activity in sawdust and a decrease in millet stalk. In the dialysis step with acetate buffer pH 4.0, there was a general decrease in activity in the two substrates (millet stalk 31.00U/ml and sawdust 21.67U/ml). The dialysis may have caused the loss of some cofactors essential for the activity of the cellulase. From the result obtained, it was obvious that Rhizopus stolonifer has the ability of secreting cellulase in culture media containing the two carbon sources (sawdust and millet stalk). The study also revealed that proper pretreatment methods of millet stalk feed substrate may support higher yield of the enzyme. As with most enzyme purifications, dialysis reduced the activity of the enzyme.

    Journal of Computing | Journal of Systems and Software     
2014 ARPN Publishers