RESEARCH ARTICLE


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



Na Liu*, Liang Huang
Henan University of Technology, Zhengzhou 450001, China


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Creative Commons License
© 2015 Liu and Huang

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.

* Address correspondence to this author at the author at Henan University of Technology, Zhengzhou 450001, China; Tel: 86-0371-67756253; Fax: 86-0371-67756253; E-mail: liuna3456@163.com


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.