Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto
Resource
Journal of Agricultural and Food Chemistry 57 (2): 503-508
Journal
Journal of Agricultural and Food Chemistry
Journal Volume
57
Journal Issue
2
Pages
503-508
Date Issued
2008
Date
2008
Author(s)
Abstract
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. ? 2009 American Chemical Society.
Subjects
Amyloid; Amyloid degradation; Amyloidosis; Fibril; Natto; Nattokinase; Subtilisin nat
SDGs
Other Subjects
Bacillus subtilis; amyloid; bacterial protein; nattokinase; serine proteinase; subtilisin; Alzheimer disease; article; Bacillus subtilis; bacterium; chemistry; enzyme stability; enzymology; human; metabolism; prion disease; Alzheimer Disease; Amyloid; Bacillus subtilis; Bacteria; Bacterial Proteins; Enzyme Stability; Humans; Prion Diseases; Serine Endopeptidases; Subtilisins
Type
journal article
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