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Production and biochemical and biophysical characterization of fibrinolytic protease of a Mucor subtilissimus strain isolated from the caatinga biome.
Conniff, Amanda Emmanuelle S; Nascimento, Thiago P; Costa, Romero Marcos P B; Breydo, Leonid; Porto, Camila S; Converti, Attilio; Siqueira, Joyce G W; Teixeira, Jose Antonio; Campos-Takaki, Galba Maria DE; Uversky, Vladimir N; Porto, Ana Lúcia F; Porto, Tatiana S.
Afiliación
  • Conniff AES; Universidade Federal Rural de Pernambuco, Departamento de Morfologia e Fisiologia Animal, Rua Dom Manoel de Medeiros, s/n, Dois Irmãos, 52171-900 Recife, PE, Brazil.
  • Nascimento TP; Department of Medical Engineering, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd 33612, Tampa, Florida, USA.
  • Costa RMPB; Universidade Federal do Piauí, Campus Professor Cinobelina Elvas, BR 135, Km 3, Planalto Horizonte, 64049-550 Bom Jesus, PI, Brazil.
  • Breydo L; Universidade de Pernambuco, Instituto de Ciências Biológicas, Rua Arnóbio Marques, 310, Santo Amaro, 50100-130 Recife, PE, Brazil.
  • Porto CS; University of South Florida, Morsani College of Medicine, Department of Molecular Medicine, 12901 Bruce B. Downs Blvd 33612, Tampa, Florida, USA.
  • Converti A; Universidade Federal de Alagoas, Unidade Educacional de Penedo, Avenida Beira Rio, s/n, 57200-000 Penedo, Brazil.
  • Siqueira JGW; Genoa University, Pole of Chemical Engineering, Department of Civil, Chemical and Environmental Engineering, Via Opera Pia 15, 16145 Genoa, Italy.
  • Teixeira JA; Universidade Federal Rural de Pernambuco, Pós-Graduação em Ciência e Tecnologia de Alimentos, Rua Dom Manoel de Medeiros, s/n, Dois Irmãos, 52171-900 Recife, PE, Brazil.
  • Campos-Takaki GM; University Biological of Minho, Centre of Engineering, Institute for Biotechnology and Bioengineering, Campus of Gualtar, 4710-057 Braga, Portugal.
  • Uversky VN; Universidade Católica de Pernambuco, Núcleo de Pesquisas em Ciências Ambientais, Rua do Príncipe, 526, Boa Vista, 50050-900 Recife, PE, Brazil.
  • Porto ALF; University of South Florida, Morsani College of Medicine, Department of Molecular Medicine, 12901 Bruce B. Downs Blvd 33612, Tampa, Florida, USA.
  • Porto TS; Universidade Federal Rural de Pernambuco, Departamento de Morfologia e Fisiologia Animal, Rua Dom Manoel de Medeiros, s/n, Dois Irmãos, 52171-900 Recife, PE, Brazil.
An Acad Bras Cienc ; 96(suppl 1): e20230616, 2024.
Article en En | MEDLINE | ID: mdl-39292103
ABSTRACT
Cardiovascular diseases, resulting from the deposition of clots in blood vessels, are the leading cause of death worldwide. Fibrinolytic enzymatic activity can catalyze blood clot degradation. Findings show that 36 fungal isolates recovered from Caatinga soils have the potential to produce fibrinolytic protease under submerged conditions. About 58 % of the isolates displayed fibrinolytic activity above 100 U/mL, with Mucor subtilissimus UCP 1262 being the most active. The protease was biochemically and biophysically characterized, showing that the enzyme had a high affinity for SAApNA substrate and was significantly inhibited by fluoride methyl phenyl sulfonyl-C7H7FO2S, suggesting that it is a chymotrypsin-like serine protease. The highest enzyme activity was detected at pH 5.0 and 28 °C. This fibrinolytic protease's far-UV circular dichroism (CD) showed that its secondary structure was primarily α-helical. The purified fibrinolytic enzyme may represent a novel therapeutic agent for treating thrombosis. At temperatures above 65 °C, the enzyme lost all its secondary structure. Its melting temperature was 58.1 °C, the denaturation enthalpy 85.1 kcal/mol, and the denaturation entropy 0.26 kcal/K∙mol.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Mucor Idioma: En Revista: An Acad Bras Cienc Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Brasil
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Mucor Idioma: En Revista: An Acad Bras Cienc Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Brasil