Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus.
Identifieur interne : 000063 ( PubMed/Corpus ); précédent : 000062; suivant : 000064Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus.
Auteurs : Paula Monteiro Souza ; Bahar Aliakbarian ; Edivaldo Ximenes Ferreira Filho ; Pérola Oliveira Magalhães ; Adalberto Pessoa Junior ; Attilio Converti ; Patrizia PeregoSource :
- International journal of biological macromolecules ; 2015.
Abstract
The kinetics of a thermostable extracellular acid protease produced by an Aspergillus foetidus strain was investigated at different pH, temperatures and substrate concentrations. The enzyme exhibited maximal activity at pH 5.0 and 55°C, and its irreversible deactivation was well described by first-order kinetics. When temperature was raised from 55 to 70°C, the deactivation rate constant increased from 0.018 to 5.06h(-1), while the half-life decreased from 37.6 to 0.13h. The results of activity collected at different temperatures were then used to estimate, the activation energy of the hydrolysis reaction (E*=19.03kJ/mol) and the standard enthalpy variation of reversible enzyme unfolding (ΔH°U=19.03kJ/mol). The results of residual activity tests carried out in the temperature range 55-70°C allowed estimating the activation energy (E(*)d=314.12kJ/mol), enthalpy (311.27≤(ΔH°d≤311.39kJ/mol), entropy (599.59≤ΔS(*)d≤610.49kJ/mol K) and Gibbs free energy (103.18≤ΔG(*)d≤113.87kJ/mol) of the enzyme irreversible denaturation. These thermodynamic parameters suggest that this new protease is highly thermostable and could be important for industrial applications. To the best of our knowledge, this is the first report on thermodynamic parameters of an acid protease produced by A. foetidus.
DOI: 10.1016/j.ijbiomac.2015.07.043
PubMed: 26210038
Links to Exploration step
pubmed:26210038Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus.</title><author><name sortKey="Souza, Paula Monteiro" sort="Souza, Paula Monteiro" uniqKey="Souza P" first="Paula Monteiro" last="Souza">Paula Monteiro Souza</name><affiliation><nlm:affiliation>Department of Biochemical and Pharmaceutical Technology, University of São Paulo, São Paulo, SP, 05508-000, Brazil. Electronic address: paulasouza@usp.br.</nlm:affiliation></affiliation></author><author><name sortKey="Aliakbarian, Bahar" sort="Aliakbarian, Bahar" uniqKey="Aliakbarian B" first="Bahar" last="Aliakbarian">Bahar Aliakbarian</name><affiliation><nlm:affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Filho, Edivaldo Ximenes Ferreira" sort="Filho, Edivaldo Ximenes Ferreira" uniqKey="Filho E" first="Edivaldo Ximenes Ferreira" last="Filho">Edivaldo Ximenes Ferreira Filho</name><affiliation><nlm:affiliation>Laboratory of Enzymology, Department of Cellular Biology, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Magalhaes, Perola Oliveira" sort="Magalhaes, Perola Oliveira" uniqKey="Magalhaes P" first="Pérola Oliveira" last="Magalhães">Pérola Oliveira Magalhães</name><affiliation><nlm:affiliation>Department of Pharmaceutical Sciences, School of Health Sciences, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Junior, Adalberto Pessoa" sort="Junior, Adalberto Pessoa" uniqKey="Junior A" first="Adalberto Pessoa" last="Junior">Adalberto Pessoa Junior</name><affiliation><nlm:affiliation>Department of Biochemical and Pharmaceutical Technology, University of São Paulo, São Paulo, SP, 05508-000, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name><affiliation><nlm:affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Perego, Patrizia" sort="Perego, Patrizia" uniqKey="Perego P" first="Patrizia" last="Perego">Patrizia Perego</name><affiliation><nlm:affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26210038</idno><idno type="pmid">26210038</idno><idno type="doi">10.1016/j.ijbiomac.2015.07.043</idno><idno type="wicri:Area/PubMed/Corpus">000063</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus.</title><author><name sortKey="Souza, Paula Monteiro" sort="Souza, Paula Monteiro" uniqKey="Souza P" first="Paula Monteiro" last="Souza">Paula Monteiro Souza</name><affiliation><nlm:affiliation>Department of Biochemical and Pharmaceutical Technology, University of São Paulo, São Paulo, SP, 05508-000, Brazil. Electronic address: paulasouza@usp.br.</nlm:affiliation></affiliation></author><author><name sortKey="Aliakbarian, Bahar" sort="Aliakbarian, Bahar" uniqKey="Aliakbarian B" first="Bahar" last="Aliakbarian">Bahar Aliakbarian</name><affiliation><nlm:affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Filho, Edivaldo Ximenes Ferreira" sort="Filho, Edivaldo Ximenes Ferreira" uniqKey="Filho E" first="Edivaldo Ximenes Ferreira" last="Filho">Edivaldo Ximenes Ferreira Filho</name><affiliation><nlm:affiliation>Laboratory of Enzymology, Department of Cellular Biology, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Magalhaes, Perola Oliveira" sort="Magalhaes, Perola Oliveira" uniqKey="Magalhaes P" first="Pérola Oliveira" last="Magalhães">Pérola Oliveira Magalhães</name><affiliation><nlm:affiliation>Department of Pharmaceutical Sciences, School of Health Sciences, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Junior, Adalberto Pessoa" sort="Junior, Adalberto Pessoa" uniqKey="Junior A" first="Adalberto Pessoa" last="Junior">Adalberto Pessoa Junior</name><affiliation><nlm:affiliation>Department of Biochemical and Pharmaceutical Technology, University of São Paulo, São Paulo, SP, 05508-000, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name><affiliation><nlm:affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Perego, Patrizia" sort="Perego, Patrizia" uniqKey="Perego P" first="Patrizia" last="Perego">Patrizia Perego</name><affiliation><nlm:affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</nlm:affiliation></affiliation></author></analytic><series><title level="j">International journal of biological macromolecules</title><idno type="e-ISSN">1879-0003</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 kinetics of a thermostable extracellular acid protease produced by an Aspergillus foetidus strain was investigated at different pH, temperatures and substrate concentrations. The enzyme exhibited maximal activity at pH 5.0 and 55°C, and its irreversible deactivation was well described by first-order kinetics. When temperature was raised from 55 to 70°C, the deactivation rate constant increased from 0.018 to 5.06h(-1), while the half-life decreased from 37.6 to 0.13h. The results of activity collected at different temperatures were then used to estimate, the activation energy of the hydrolysis reaction (E*=19.03kJ/mol) and the standard enthalpy variation of reversible enzyme unfolding (ΔH°U=19.03kJ/mol). The results of residual activity tests carried out in the temperature range 55-70°C allowed estimating the activation energy (E(*)d=314.12kJ/mol), enthalpy (311.27≤(ΔH°d≤311.39kJ/mol), entropy (599.59≤ΔS(*)d≤610.49kJ/mol K) and Gibbs free energy (103.18≤ΔG(*)d≤113.87kJ/mol) of the enzyme irreversible denaturation. These thermodynamic parameters suggest that this new protease is highly thermostable and could be important for industrial applications. To the best of our knowledge, this is the first report on thermodynamic parameters of an acid protease produced by A. foetidus.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="In-Process"><PMID Version="1">26210038</PMID><DateCreated><Year>2015</Year><Month>12</Month><Day>22</Day></DateCreated><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>81</Volume><PubDate><Year>2015</Year><Month>Nov</Month></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int. J. Biol. Macromol.</ISOAbbreviation></Journal><ArticleTitle>Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus.</ArticleTitle><Pagination><MedlinePgn>17-21</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2015.07.043</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(15)00514-0</ELocationID><Abstract><AbstractText>The kinetics of a thermostable extracellular acid protease produced by an Aspergillus foetidus strain was investigated at different pH, temperatures and substrate concentrations. The enzyme exhibited maximal activity at pH 5.0 and 55°C, and its irreversible deactivation was well described by first-order kinetics. When temperature was raised from 55 to 70°C, the deactivation rate constant increased from 0.018 to 5.06h(-1), while the half-life decreased from 37.6 to 0.13h. The results of activity collected at different temperatures were then used to estimate, the activation energy of the hydrolysis reaction (E*=19.03kJ/mol) and the standard enthalpy variation of reversible enzyme unfolding (ΔH°U=19.03kJ/mol). The results of residual activity tests carried out in the temperature range 55-70°C allowed estimating the activation energy (E(*)d=314.12kJ/mol), enthalpy (311.27≤(ΔH°d≤311.39kJ/mol), entropy (599.59≤ΔS(*)d≤610.49kJ/mol K) and Gibbs free energy (103.18≤ΔG(*)d≤113.87kJ/mol) of the enzyme irreversible denaturation. These thermodynamic parameters suggest that this new protease is highly thermostable and could be important for industrial applications. To the best of our knowledge, this is the first report on thermodynamic parameters of an acid protease produced by A. foetidus.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Souza</LastName><ForeName>Paula Monteiro</ForeName><Initials>PM</Initials><AffiliationInfo><Affiliation>Department of Biochemical and Pharmaceutical Technology, University of São Paulo, São Paulo, SP, 05508-000, Brazil. Electronic address: paulasouza@usp.br.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aliakbarian</LastName><ForeName>Bahar</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Filho</LastName><ForeName>Edivaldo Ximenes Ferreira</ForeName><Initials>EX</Initials><AffiliationInfo><Affiliation>Laboratory of Enzymology, Department of Cellular Biology, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Magalhães</LastName><ForeName>Pérola Oliveira</ForeName><Initials>PO</Initials><AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences, School of Health Sciences, University of Brasilia, Campus Darcy Ribeiro, Asa Norte, Brasilia, DF, 70910900, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Junior</LastName><ForeName>Adalberto Pessoa</ForeName><Initials>AP</Initials><AffiliationInfo><Affiliation>Department of Biochemical and Pharmaceutical Technology, University of São Paulo, São Paulo, SP, 05508-000, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Converti</LastName><ForeName>Attilio</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Perego</LastName><ForeName>Patrizia</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, via Opera Pia 15, 16145 Genoa, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>07</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biol Macromol</MedlineTA><NlmUniqueID>7909578</NlmUniqueID><ISSNLinking>0141-8130</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Acid protease</Keyword><Keyword MajorTopicYN="N">Aspergillus foetidus</Keyword><Keyword MajorTopicYN="N">Thermostability</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>12</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>7</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>7</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="aheadofprint"><Year>2015</Year><Month>7</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>7</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>7</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>7</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26210038</ArticleId><ArticleId IdType="pii">S0141-8130(15)00514-0</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2015.07.043</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Musique/explor/OperaV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000063 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000063 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Musique
|area= OperaV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:26210038
|texte= Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:26210038" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a OperaV1
| This area was generated with Dilib version V0.6.21. |  |