RESEARCH ARTICLE

Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11

The Open Biotechnology Journal 21 Oct 2015 RESEARCH ARTICLE DOI: 10.2174/1874070701509010199

Abstract

The present study characterises an acidic protease purified from the Rhizopus stolonifer strain, RN-11. The acidic protease with a 70 kDa molecular weight, was stable within pH 2-4 at temperatures 40-50°C. The temperature and pH value conducive to optimal catalytic activity were pH 2.5 and 50°C, respectively. Treatment with 5 mmol metal ions showed that the acidic protease was activated by Na+, K+, Mn2+, Cu2+ and Ca2+, inhibited by Zn2+, Li2+ and Fe2+, and unaffected by Mg2+. It was proposed that the studied acidic protease might represent a previously uncharacterised type of acidic protease produced by the Rhizopus stolonifer RN-11 strain.

Keywords: Enzyme characteristics, purification, Rhizopuspepsins.
Fulltext HTML PDF
1800
1801
1802
1803
1804