- Tytuł:
- Purification and characterization of a novel metalloprotease from fruiting bodies of Oudemansiella radicata
- Autorzy:
-
Geng, Xueran
Te, Rigen
Tian, Guoting
Zhao, Yongchang
Zhao, Liyan
Wang, Hexiang
Ng, Tzi - Powiązania:
- https://bibliotekanauki.pl/articles/1038592.pdf
- Data publikacji:
- 2017
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
edible mushroom
Oudemansiella radicata
protease
purification - Opis:
- In this study, a 39-kDa metalloprotease was purified from a rare edible mushroom with health-promoting activities, Oudemansiella radicata, using a purification protocol which entailed anion exchange chromatography on DEAE-cellulose and Q-Sepharose columns and gel filtration by fast protein liquid chromatography on a Superdex 75 column. Some peptide sequences were obtained by LC-MS/MS analysis and one of the sequences, DAWIQADVNR, manifested 90% identity to Coprinopsis cinerea metalloprotease. The optimal reaction pH and temperature for Oudemansiella radicata protease were pH 7.0 and 50°C, respectively. The protease was purified 79-fold and demonstrated a specific protease activity of 2.42 U/mg. The Km of the purified protease for the casein substrate was 0.65 mg/mL at pH 7.0 and 50°C. The activity of the protease was inhibited by Cd2+, Hg2+, Cu2+, Pb2+ and Fe3+ ions, but was enhanced by K+, Mn2+ and Fe2+ ions. The marked suppression of the protease activity by EDTA indicates that the protease is a metalloprotease.
- Źródło:
-
Acta Biochimica Polonica; 2017, 64, 3; 477-483
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki