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- W2334005577 abstract "An acid protease from the broth of a 24 h cultivated Aspergillus niger BCRC 32720 was purified to electrophoretical homogeneity by CM Sepharose FF and Sephacryl S-100 HR chromatographs. The specific activity, purification fold, and yield were 23.29 kU/mg, 2.5, and 24.2%, respectively. Molecular mass (M) and N-terminal amino acid sequence were 47.5 kDa and SKGSAVTT, whereas the pH and temperature optima were at 2.5 and 50 °C, respectively. It was stable at pH 2.0–4.0 or ≤40 °C and activated by Fe2+ and cysteine, but partially inhibited by phenylmethanesulfonyl fluoride and tosyllysine chloromethyl ketone and highly inhibited by Ag+, Sn2+, Fe3+, Sb3+, and pepstatin A. It was considered to be an aspartic protease." @default.
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- W2334005577 date "2013-01-11" @default.
- W2334005577 modified "2023-09-29" @default.
- W2334005577 title "Characterization of Acidic Protease from Aspergillus niger BCRC 32720" @default.
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- W2334005577 doi "https://doi.org/10.1021/jf3041726" @default.
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