Effect of pH, NaCl, CaCl 2 and temperature on self-assembly of β-lactoglobulin into nanofibrils: A central composite design study

Journal of Agricultural and Food Chemistry

Volumn 59, Issue 15, 2011, Pages 8467-8474

  Loveday, S M ^a   Wang, X L ^a   Rao, M A ^b   Anema, S G ^c   Singh, H ^a  

^a MASSEY UNIVERSITY   (New Zealand)

^b Department of Obstetrics Gynecology   (United States)

^c FONTERRA RESEARCH CENTRE   (New Zealand)

Author keywords

acid hydrolysis; amyloid; beta lactoglobulin; central composite design; heat; nanofibril; protein; self assembly; thioflavin T; transmission electron microscopy; whey protein

Indexed keywords

ACID HYDROLYSIS; AMYLOID; BETA-LACTOGLOBULIN; CENTRAL COMPOSITE DESIGNS; HEAT; NANOFIBRIL; THIOFLAVIN T; TRANSMISSION ELECTRON; WHEY PROTEINS;

BIOLOGICAL MATERIALS; CALCIUM CHLORIDE; COAGULATION; GELATION; GLYCOPROTEINS; KINETICS; MORPHOLOGY; PROTEINS; SELF ASSEMBLY; SODIUM CHLORIDE; TRANSMISSION ELECTRON MICROSCOPY;

PH EFFECTS;

LACTOGLOBULIN; NANOMATERIAL; SODIUM CHLORIDE;

ARTICLE; CHEMISTRY; DRUG EFFECT; KINETICS; PH; PROTEIN CONFORMATION; TEMPERATURE;

HYDROGEN-ION CONCENTRATION; KINETICS; LACTOGLOBULINS; NANOSTRUCTURES; PROTEIN CONFORMATION; SODIUM CHLORIDE; TEMPERATURE;

EID: 79961143384     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf201870z     Document Type: Article

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