Eneje, L.O. and Odibo , F.J.C. and Nwani , C.D. (2013) Purification and characterization of a protease isolated from millet malt variety of Sossat. International Journal of AgriScience, 3 (1). pp. 53-61.
![[img]](http://eprints.icrisat.ac.in/style/images/fileicons/application_pdf.png) |
PDF
- Published Version
Restricted to ICRISAT researchers only |
Abstract
A protease from Sossat millet was purified by dialysis against 6M sucrose solution followed by ion exchange chromatography on Q-sepharose (fast flow), hydrophobic interaction chromatography on phenyl sepharose (off high sub) and gel filtration chromatography on sephadex G-200. The enzyme was purified 1.55 fold to give 2.99% yield on total activity in the crude extract and final specific activity of 95.8 µmgml-1 protein. The SDS-PAGE electrophoresis showed a migrating protein band corresponding to molecular weight <35 KDa or 35-45 KDa as calculated from migrating in relation to reference protein. The purified protease had optimal activity at 50°C and most stable at 40°C but retained about 70% of its activity at 70°C after incubation at test temperature for 30 minutes. The protease was optimally active at pH 5 and maximally stable at pH6. The purified enzymes were stimulated by various cations such as Ag+, Ba2+, Co2+, Fe2+, Hg2+, Mg2+, Mn2+, Pb2+, Sr2+ and Cu2+ at varying degrees
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | chromatography, Sossat malt, protease, purification, inhibitors |
| Author Affiliation: | Department of Applied Microbiology and Brewing, Enugu State University of Science and Technology, Enugu, Nigeria |
| Subjects: | Plant Production Plant Protection |
| Divisions: | Millet |
| Depositing User: | Mr B Krishnamurthy |
| Date Deposited: | 25 Jun 2013 13:50 |
| Last Modified: | 25 Jun 2013 13:50 |
| URI: | http://eprints.icrisat.ac.in/id/eprint/10768 |
Actions (login required)
 |
View Item |
