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Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin
Jeanette Otte
*
,
Richard Ipsen
, Rogert Bauer,
Morten J. Bjerrum
, Rianne Waninge
*
Corresponding author for this work
Food Chemistry
Dairy Technology
Department of Chemistry
37
Citations (Scopus)
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Keyphrases
α-lactalbumin (α-La)
100%
Amyloid-like
100%
Limited Proteolysis
100%
Hydrolysis
50%
Bacillus Licheniformis
50%
Thioflavin T
50%
Main Components
50%
Hydrolysis Products
50%
Stronger Binding
50%
Protease
50%
Secondary Structure
50%
Molecular Mechanism
50%
Biochemistry, Genetics and Molecular Biology
Lactalbumin
100%
Amyloid Protein
100%
Proteolysis
100%
Enzymatic Hydrolysis
100%
Protease
50%
Bacillus Licheniformis
50%
Thioflavin
50%
Protein Secondary Structure
50%
Chemistry
formation
100%
dimer
100%
Limited Proteolysis
100%
Enzymatic Hydrolysis
50%
Secondary Structure
25%
Monomer
25%
Chemical Engineering
Dimer
100%