RESEARCH ARTICLE
Partial Characterization of an Acidic Protease from Rhizopus stolonifer RN-11
Na Liu*, Liang Huang
Article Information
Identifiers and Pagination:
Year: 2015Volume: 9
First Page: 199
Last Page: 203
Publisher ID: TOBIOTJ-9-199
DOI: 10.2174/1874070701509010199
Article History:
Received Date: 05/06/2015Revision Received Date: 20/08/2015
Acceptance Date: 11/09/2015
Electronic publication date: 21/10/2015
Collection year: 2015
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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.