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Biochemical and thermodynamic characteristics of a new serine protease from Mucor subtilissimus URM 4133

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dc.contributor.authorGomes, José Erick Galindo
dc.contributor.authorRosa, Isabel Zaparoli
dc.contributor.authorNascimento, Talita Camila Evaristo da Silva
dc.contributor.authorSouza-Motta, Cristina Maria de
dc.contributor.authorGomes, Eleni
dc.contributor.authorBoscolo, Mauricio
dc.contributor.authorMoreira, Keila Aparecida
dc.contributor.authorPintado, Maria Manuela Estevez
dc.contributor.authorda Silva, Roberto
dc.date.accessioned2020-11-13T16:50:28Z
dc.date.available2020-11-13T16:50:28Z
dc.date.issued2020
dc.description.abstractA protease from the fungus Mucor subtilissimus URM 4133, capable of producing bioactive peptides from goat casein, was purified. SDS-PAGE and zymography showed a molecular mass of 30 kDa. The enzyme was active and stable in a wide pH range (6.0–10.5) and (5.0–10.5), respectively. Optimum temperature was at 45–50 °C and stability was above 80 % (40 °C/2 h). Activity was not influenced by ions or organic substances (Triton, Tween, SDS and DMSO), but was completely inhibited by PMSF, suggesting that it belongs to the serine protease family. The Km and Vmax were 2.35 mg azocasein.mL-1 and 333.33 U.mg protein-1, respectively. Thermodynamic parameters of irreversible denaturation (40–60 °C) were enthalpy 123.63 – 123.46 kJ.mol-1, entropy 120.24–122.28 kJ.mol-1 and Gibbs free energy 85.97 – 82.45 kJ.mol-1. Any peptide sequences compatible with this protease were found after analysis by MALDI-TOF, which suggests that it is a new serine protease.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationGomes, J.E.G., Rosa, I.Z., Nascimento, T.C.E.S., Souza-Motta, C.M., Gomes, E., Boscolo, M., ... Silva, R. (2020). Biochemical and thermodynamic characteristics of a new serine protease from Mucor subtilissimus URM 4133. Biotechnology Reportspt_PT
dc.identifier.doi10.1016/j.btre.2020.e00552pt_PT
dc.identifier.eid85096704864
dc.identifier.issn2215-017X
dc.identifier.pmcPMC7683317
dc.identifier.pmid33294402
dc.identifier.urihttp://hdl.handle.net/10400.14/31353
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectSerine proteasept_PT
dc.subjectEnzymatic characterizationpt_PT
dc.subjectPeptide sequences by MALDI-TOFpt_PT
dc.subjectMucor subtilissimuspt_PT
dc.titleBiochemical and thermodynamic characteristics of a new serine protease from Mucor subtilissimus URM 4133pt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F50016%2F2013/PT
oaire.citation.titleBiotechnology Reportspt_PT
oaire.fundingStream5876
person.familyNamePintado
person.givenNameMaria Manuela
person.identifier456608
person.identifier.ciencia-id2F13-AAE0-3405
person.identifier.orcid0000-0002-0760-3184
person.identifier.ridF-5696-2013
person.identifier.scopus-author-id7004483898
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublicationba387c7d-27c9-4016-895c-b35597e91ebc
relation.isAuthorOfPublication.latestForDiscoveryba387c7d-27c9-4016-895c-b35597e91ebc
relation.isProjectOfPublication3fe5970e-de39-42f7-a29d-18521b591a09
relation.isProjectOfPublication.latestForDiscovery3fe5970e-de39-42f7-a29d-18521b591a09

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