Production, purification, and characterization of an extracellular acid protease from the marine Antarctic yeast Rhodotorula mucilaginosa L7.
Identifieur interne : 000137 ( Main/Exploration ); précédent : 000136; suivant : 000138Production, purification, and characterization of an extracellular acid protease from the marine Antarctic yeast Rhodotorula mucilaginosa L7.
Auteurs : Luciana Daniela Lario [Brésil] ; Luciana Chaud [Brésil] ; María Das Graças Almeida [Brésil] ; Attilio Converti [Italie] ; Lara Durães Sette [Brésil] ; Adalberto Pessoa [Brésil]Source :
- Fungal biology [ 1878-6146 ] ; 2015.
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 °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 °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.
DOI: 10.1016/j.funbio.2015.08.012
PubMed: 26466885
Affiliations:
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Prof. Lineu Prestes, 580, 05508-900 São Paulo, SP, Brazil. Electronic address: lucianalario@usp.br.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Department of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, Av. Prof. Lineu Prestes, 580, 05508-900 São Paulo, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName><orgName type="university">Université de São Paulo</orgName></affiliation></author><author><name sortKey="Chaud, Luciana" sort="Chaud, Luciana" uniqKey="Chaud L" first="Luciana" last="Chaud">Luciana Chaud</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biotechnology, University of São Paulo, Lorena Campus, Rod. Itajuba-Lorena, Km 74.5, 12.600-000 Lorena, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Department of Biotechnology, University of São Paulo, Lorena Campus, Rod. 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Prof. Lineu Prestes, 580, 05508-900 São Paulo, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Department of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, Av. Prof. Lineu Prestes, 580, 05508-900 São Paulo, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region></placeName><orgName type="university">Université de São Paulo</orgName></affiliation></author></analytic><series><title level="j">Fungal biology</title><idno type="ISSN">1878-6146</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 °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 °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.</div></front></TEI><affiliations><list><country><li>Brésil</li><li>Italie</li></country><region><li>État de São Paulo</li></region><orgName><li>Université de São Paulo</li></orgName></list><tree><country name="Brésil"><region name="État de São Paulo"><name sortKey="Lario, Luciana Daniela" sort="Lario, Luciana Daniela" uniqKey="Lario L" first="Luciana Daniela" last="Lario">Luciana Daniela Lario</name></region><name sortKey="Almeida, Maria Das Gracas" sort="Almeida, Maria Das Gracas" uniqKey="Almeida M" first="María Das Graças" last="Almeida">María Das Graças Almeida</name><name sortKey="Chaud, Luciana" sort="Chaud, Luciana" uniqKey="Chaud L" first="Luciana" last="Chaud">Luciana Chaud</name><name sortKey="Pessoa, Adalberto" sort="Pessoa, Adalberto" uniqKey="Pessoa A" first="Adalberto" last="Pessoa">Adalberto Pessoa</name><name sortKey="Sette, Lara Duraes" sort="Sette, Lara Duraes" uniqKey="Sette L" first="Lara Durães" last="Sette">Lara Durães Sette</name></country><country name="Italie"><noRegion><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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