Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto
Citations Over TimeTop 10% of 2008 papers
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-beta 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.
Related Papers
- → Genetic map of the Bacillus stearothermophilus NUB36 chromosome(1990)16 cited
- → Increased production of extracellular enzymes by the synergistic effect of genes introduced into Bacillus subtilis by stepwise transformation(1980)28 cited
- → Physiological Characteristics of Bacillus sp. HR6 in the Process of Decomposing Bean Curd Refuse.(1999)9 cited
- Screening of the related genes of antimicrobial peptides for antagonistic activity of Bacillus subtilis SC-8 against Bacillus cereus(2018)
- → A note on the effect of storage on the chemical resistance of spores of Bacillus subtilis SA22 and Bacillus subtilis globigii B17(1988)