Biochemical and thermodynamic characteristics of a new serine protease from Mucor subtilissimus URM 4133
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2020-12-01
Autores
Gomes, José Erick Galindo [UNESP]
Rosa, Isabel Zaparoli [UNESP]
Nascimento, Talita Camila Evaristo da Silva
Souza-Motta, Cristina Maria de
Gomes, Eleni [UNESP]
Boscolo, Mauricio [UNESP]
Moreira, Keila Aparecida
Pintado, Maria Manuela Estevez
da Silva, Roberto [UNESP]
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Resumo
A 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.
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Enzymatic characterization, Mucor subtilissimus, Peptide sequences by MALDI-TOF, Serine protease
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Biotechnology Reports, v. 28.