Heat-induced fibril assembly of vicilin at pH2.0: Reaction kinetics, influence of ionic strength and protein concentration, and molecular mechanism

Food Research International

Volumn 51, Issue 2, 2013, Pages 621-632

  Liu, Jing ^a   Tang, Chuan He ^a  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Aggregation; Amyloid fibril; Fibril assembly; Ionic strength; Legume vicilin; Protein concentration

Indexed keywords

ACID HYDROLYSIS; AMINO ACID COMPOSITIONS; AMYLOID FIBRIL; CHAIN TERMINATIONS; CONFORMATION CHANGE; DYNAMIC LASER SCATTERING; ELECTROSTATIC SCREENING; FIBRIL ELONGATION; FIBRIL MORPHOLOGY; MOLECULAR MECHANISM; OLIGOMERIC PROTEINS; PROTEIN CONCENTRATIONS; PROTOFIBRILS; RED BEANS; THERMAL DENATURATIONS; THIOFLAVIN T; VICILIN;

AGGLOMERATION; AGGREGATES; AMINO ACIDS; ASSOCIATION REACTIONS; ATOMIC FORCE MICROSCOPY; HYDROLYSIS; IONIC STRENGTH; KINETICS; OLIGOMERS; POLYPEPTIDES; REACTION KINETICS;

PROTEINS;

EID: 84873892393     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2012.12.049     Document Type: Article

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