The topography of bovine β-casein at an oil/water interface as determined from the kinetics of trypsin-catalysed hydrolysis-Reference-Cited by-同舟云学术

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The topography of bovine β-casein at an oil/water interface as determined from the kinetics of trypsin-catalysed hydrolysis

Published:1990-12 Issue:3 Volume:1041 Page:217-222
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Leaver Jeffrey,Dalgleish Douglas G.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference16 articles.

1. Interfacial Composition of Sodium Caseinate Emulsions

2. Competitive adsorption of αs1-casein and β-casein in oil-in-water emulsions

3. The conformations of proteins on solid/water interfaces — caseins and phosvitin on polystyrene latices

4. Dynamic and static properties of proteins adsorbed at the air/water interface

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2. Determination of kinetic parameters for casein hydrolysis by chymotrypsin using two ranges of substrate concentration;International Dairy Journal;2016-10

3. Emulsions and Foams Stabilised by Milk Proteins;Advanced Dairy Chemistry;2016

4. Casein Micelle Structure and Stability;Milk Proteins;2014

5. In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides;Food Chemistry;2014-01

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