Unfolding and refolding of β-lactoglobulin subjected to high hydrostatic pressure at different pH values and temperatures and its influence on proteolysis

Journal of Agricultural and Food Chemistry

Volumn 55, Issue 13, 2007, Pages 5282-5288

  Belloque, Josefina ^a   Chicón, Rosa ^a   López Fandiño, Rosina ^a  

^a INSTITUTO DE FERMENTACIONES INDUSTRIALES CSIC   (Spain)

Author keywords

lactoglobulin; Chymotrypsin; High pressure; Nuclear magnetic resonance; Pepsin; Structure

Indexed keywords

CHYMOTRYPSIN; LACTOGLOBULIN;

ARTICLE; CHEMISTRY; HYDROSTATIC PRESSURE; METABOLISM; PH; PROTEIN FOLDING; TEMPERATURE;

CHYMOTRYPSIN; HYDROGEN-ION CONCENTRATION; HYDROSTATIC PRESSURE; LACTOGLOBULINS; PROTEIN FOLDING; TEMPERATURE;

EID: 34447341183     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf070170w     Document Type: Article

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