title: Amyloid-degrading ability of nattokinase from Bacillus subtilis natto.
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.
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
authors.forename: Ruei-Lin
authors.initials: RL
authors.lastname: Hsu
authors.forename: Kung-Ta
authors.initials: KT
authors.lastname: Lee
authors.forename: Jung-Hao
authors.initials: JH
authors.lastname: Wang
authors.forename: Lily Y-L
authors.initials: LY
authors.lastname: Lee
authors.forename: Rita P-Y
authors.initials: RP
authors.lastname: Chen
mesh_terms: D000544:Alzheimer Disease / Q000628:therapy; D000682:Amyloid / Q000378:metabolism*; D001412:Bacillus subtilis / Q000737:chemistry / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability; D006801:Humans; D017096:Prion Diseases / Q000628:therapy; D012697:Serine Endopeptidases / Q000378:metabolism; D013381:Subtilisins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000682:Amyloid; D001426:Bacterial Proteins; D012697:Serine Endopeptidases; D013381:Subtilisins; C053771:nattokinase