Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Production, purification, and characterization of an extracellular acid protease from the marine Antarctic yeast Rhodotorula mucilaginosa L7

Full text
Author(s):
Lario, Luciana Daniela [1] ; Chaud, Luciana [2] ; Almeida, Maria das Gracas [2] ; Converti, Attilio [3] ; Duraes Sette, Lara [4] ; Pessoa, Adalberto [1]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Sch Pharmaceut Sci, Dept Biochem & Pharmaceut Technol, BR-05508900 Sao Paulo, SP - Brazil
[2] Univ Sao Paulo, Dept Biotechnol, Lorena, SP - Brazil
[3] Univ Genoa, Pole Chem Engn, Dept Civil Chem & Environm Engn, I-16145 Genoa - Italy
[4] Statal Paulista Univ Julio Mesquita Filho UNESP, Dept Biochem & Microbiol, Inst Biosci, BR-13506900 Rio Claro, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: FUNGAL BIOLOGY; v. 119, n. 11, p. 1129-1136, NOV 2015.
Web of Science Citations: 6
Abstract

The production, purification, and characterization of an extracellular protease released by Rhodotorula mucilaginosa L7 were evaluated in this study. This strain was isolated from an Antarctic marine alga and previously selected among others based on the capacity to produce the highest extracellular proteolytic activity in preliminary tests. R. mucilaginosa L7 was grown in Saboraud-dextrose medium at 25 degrees C, and the cell growth, pH of the medium, extracellular protease production and the glucose and protein consumption were determined as a function of time. The protease was then purified, and the effects of pH, temperature, and salt concentration on the catalytic activity and enzyme stability were determined. Enzyme production started at the beginning of the exponential phase of growth and reached a maximum after 48 h, which was accompanied by a decrease in the pH as well as reductions of the protein and glucose concentrations in the medium. The purified protease presented optimal catalytic activity at pH 5.0 and 50 degrees C. Finally, the enzyme was stable in the presence of high concentrations of NaCl. These characteristics are of interest for future studies and may lead to potential biotechnological applications that require enzyme activity and stability under acidic conditions and/or high salt concentrations. (C) 2015 The British Mycological Society. Published by Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 13/19486-0 - Marine and Antarctic biotechnology: microbial enzymes and their applications
Grantee:Lara Durães Sette
Support Opportunities: Regular Research Grants
FAPESP's process: 12/23726-4 - "purification of proteases secreted by the psicrotroph yeast Rhodoturola mucilagionosa by aqueous two-phase systems (PEG/NaPA) and chromatographic processes"
Grantee:Luciana Daniela Lario
Support Opportunities: Scholarships in Brazil - Post-Doctoral