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  • Title: Biochemical and functional characterization of a metalloprotease from the thermophilic fungus Thermoascus aurantiacus.
    Author: Merheb-Dini C, Cabral H, Leite RS, Zanphorlin LM, Okamoto DN, Rodriguez GO, Juliano L, Arantes EC, Gomes E, da Silva R.
    Journal: J Agric Food Chem; 2009 Oct 14; 57(19):9210-7. PubMed ID: 19746980.
    Abstract:
    Protease production was carried out in solid state fermentation. The enzyme was purified through precipitation with ethanol at 72% followed by chromatographies in columns of Sephadex G75 and Sephacryl S100. It was purified 80-fold and exhibited recovery of total activity of 0.4%. SDS-PAGE analysis indicated an estimated molecular mass of 24.5 kDa and the N-terminal sequence of the first 22 residues was APYSGYQCSMQLCLTCALMNCA. Purified protease was only inhibited by EDTA (96.7%) and stimulated by Fe(2+) revealing to be a metalloprotease activated by iron. Optimum pH was 5.5, optimum temperature was 75 degrees C, and it was thermostable at 65 degrees C for 1 h maintaining more than 70% of original activity. Through enzyme kinetic studies, protease better hydrolyzed casein than azocasein. The screening of fluorescence resonance energy transfer (FRET) peptide series derived from Abz-KLXSSKQ-EDDnp revealed that the enzyme exhibited preference for Arg in P(1) (k(cat)/K(m) = 30.1 mM(-1) s(-1)).
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