Effect of limited enzymatic hydrolysis on linoleic acid binding properties of β-lactoglobulin

Food Chemistry

Volumn 146, Issue , 2014, Pages 577-582

  Sponton, Osvaldo E ^a   Perez, Adrián A ^a   Carrara, Carlos ^a   Santiago, Liliana G ^a  

^a UNIVERSIDAD NACIONAL DEL LITORAL   (Argentina)

Author keywords

Chymotrypsin; Lactoglobulin; Binding properties; Enzymatic hydrolysis; Fluorescence spectroscopy; Linoleic acid

Indexed keywords

BINDING PROPERTIES; HYDROPHOBIC PROTEIN; HYDROPHOBIC RESIDUES; LACTOGLOBULIN; LIMITED ENZYMATIC HYDROLYSIS; SPECTROSCOPIC TECHNIQUE; STRUCTURAL MODIFICATIONS; SURFACE HYDROPHOBICITY;

BINDING ENERGY; ENZYMATIC HYDROLYSIS; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MOLECULAR WEIGHT DISTRIBUTION; PROTEINS;

LINOLEIC ACID;

AGAROSE; BETA LACTOGLOBULIN; CHYMOTRYPSIN; LINOLEIC ACID; PROTEIN HYDROLYSATE;

ARTICLE; ENZYME IMMOBILIZATION; FLUORESCENCE SPECTROSCOPY; HYDROLYSIS; HYDROPHOBICITY; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION;

BINDING PROPERTIES; ENZYMATIC HYDROLYSIS; FLUORESCENCE SPECTROSCOPY; LINOLEIC ACID; Α-CHYMOTRYPSIN; Β-LACTOGLOBULIN;

CHYMOTRYPSIN; HYDROLYSIS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LACTOGLOBULINS; LINOLEIC ACID; PROTEIN BINDING; SPECTROMETRY, FLUORESCENCE;

EID: 84885355568     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.09.089     Document Type: Article

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