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

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Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorFederal Rural University of Pernambuco (UFRPE)-
Autor(es): dc.contributorUniversidade Federal de Pernambuco (UFPE)-
Autor(es): dc.contributorUniversidade Católica Portuguesa (UCP) – Escola Superior de Biotecnologia-
Autor(es): dc.creatorGomes, José Erick Galindo [UNESP]-
Autor(es): dc.creatorRosa, Isabel Zaparoli [UNESP]-
Autor(es): dc.creatorNascimento, Talita Camila Evaristo da Silva-
Autor(es): dc.creatorSouza-Motta, Cristina Maria de-
Autor(es): dc.creatorGomes, Eleni [UNESP]-
Autor(es): dc.creatorBoscolo, Mauricio [UNESP]-
Autor(es): dc.creatorMoreira, Keila Aparecida-
Autor(es): dc.creatorPintado, Maria Manuela Estevez-
Autor(es): dc.creatorda Silva, Roberto [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T00:52:40Z-
Data de disponibilização: dc.date.available2022-02-22T00:52:40Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2020-11-30-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.btre.2020.e00552-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/208186-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/208186-
Descrição: dc.descriptionA 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.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionSão Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences (IBILCE) Cristovão Colombo, 2265, Jardim Nazareth-
Descrição: dc.descriptionLaboratory of Microbiology Enzymatic Technology and Bioproducts Academic Unit of Garanhuns Federal Rural University of Pernambuco (UFRPE), Bom Pastor Avenue-
Descrição: dc.descriptionDepartment of Mycology Center of Biosciences Federal University of Pernambuco (UFPE), Prof. Nelson Chaves Avenue-
Descrição: dc.descriptionCentro de Biotecnologia e Química Fina Universidade Católica Portuguesa (UCP) – Escola Superior de Biotecnologia, Rua Arquiteto Lobão Vital, 172-
Descrição: dc.descriptionSão Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences (IBILCE) Cristovão Colombo, 2265, Jardim Nazareth-
Descrição: dc.descriptionFAPESP: 2014/13700-3-
Descrição: dc.descriptionFAPESP: 2017/16482-5-
Descrição: dc.descriptionCNPq: 426578/2016-3-
Idioma: dc.languageen-
Relação: dc.relationBiotechnology Reports-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectEnzymatic characterization-
Palavras-chave: dc.subjectMucor subtilissimus-
Palavras-chave: dc.subjectPeptide sequences by MALDI-TOF-
Palavras-chave: dc.subjectSerine protease-
Título: dc.titleBiochemical and thermodynamic characteristics of a new serine protease from Mucor subtilissimus URM 4133-
Tipo de arquivo: dc.typelivro digital-
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