Details

Autor(en) / Beteiligte

• Hsu, Ruei-Lin
• Lee, Kung-Ta
• Wang, Jung-Hao
• Lee, Lily Y.-L
• Chen, Rita P.-Y

Titel

Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto

Ist Teil von

• Journal of agricultural and food chemistry, 2009-01, Vol.57 (2), p.503-508

Ort / Verlag

Washington, DC: American Chemical Society

Erscheinungsjahr

2009

Quelle

MEDLINE

Beschreibungen/Notizen

• More than 20 unrelated proteins can form amyloid fibrils in vivo which are related to various diseases, such as Alzheimer’s disease, prion disease, and systematic amyloidosis. Amyloid fibrils are an ordered protein aggregate with a lamellar cross-β structure. Enhancing amyloid clearance is one of the targets of the therapy of these amyloid-related diseases. Although there is debate on whether the toxicity is due to amyloids or their precursors, research on the degradation of amyloids may help prevent or alleviate these diseases. In this study, we explored the amyloid-degrading ability of nattokinase, a fibrinolytic subtilisin-like serine protease, and determined the optimal conditions for amyloid hydrolysis. This ability is shared by proteinase K and subtilisin Carlsberg, but not by trypsin or plasmin.