Effect of limited hydrolysis on the interfacial rheology and foaming properties of β-lactoglobulin A

Colloids and Surfaces B: Biointerfaces

Volumn 21, Issue 1-3, 2001, Pages 173-178

  Ipsen, Richard ^a   Otte, Jeanette ^a   Sharma, Ranjan ^a   Nielsen, Anni ^a   Gram Hansen, Lene ^a   Bruun Qvist, Karsten ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Lactoglobulin A; Air water interface; Enzymatic hydrolysis; Foaming; Interfacial rheology; Serine protease

Indexed keywords

FOAMS; HYDROLYSIS; HYDROPHOBICITY; INTERFACES (MATERIALS); RHEOLOGY; VISCOELASTICITY;

INTERFACIAL RHEOLOGY;

ENZYME KINETICS;

ASPARTIC ACID; BETA LACTOGLOBULIN; FOAMING AGENT; GLUTAMIC ACID; SERINE PROTEINASE;

BACILLUS LICHENIFORMIS; COMPARATIVE STUDY; CONFERENCE PAPER; ENZYME SPECIFICITY; FLOW KINETICS; FOAM; HYDROLYSIS; HYDROPHOBICITY; MOLECULAR STABILITY; PRIORITY JOURNAL; VISCOELASTICITY;

EID: 0034987782     PISSN: 09277765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0927-7765(01)00170-9     Document Type: Conference Paper

References (13)

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4. Large scale preparation of β-lactoglobulin A and B by ultrafiltration and ion exchange chromatography
5. Isolation of two tryptic fragments from bovine β-lactoglobulin and assessment of their thermal gelation ability
6. Micro-scale method for determining foaming properties of protein
7. Dynamic surface tension shear rheology studies of mixed β-lactoglobulin/Tween 20 systems
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9. Aggregate formation during hydrolysis of β-lactoglobulin with a glu and asp specific protease from Bacillus licheniformis
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11. Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology
12. β-Lactoglobulin hydrolysis. 1. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and Staphylococcus aureus V8 protease