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This article has been cited by the following article(s):
Proteolysis of Micellar β-Casein by Trypsin: Secondary Structure Characterization and Kinetic Modeling at Different Enzyme Concentrations
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Application of Multiharmonic QCM-D for Detection of Plasmin at Hydrophobic Surfaces Modified by β-Casein
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Caseins and Casein Hydrolysates. 1. Lipoxygenase Inhibitory Properties
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Kinetics of β-casein hydrolysis by wild-type and engineered trypsin
Impact of the lysine‐188 and aspartic acid‐189 inversion on activity of trypsin
Loı̈c Briand, Jean-Marc Chobert, René Gantier, Nathalie Declerck, Vinh Tran, Joëlle Léonil, Daniel Mollé and Thomas Haertlé FEBS Letters 442(1) 43 (1999) https://doi.org/10.1016/S0014-5793(98)01611-1
How the Substitution of K188 of Trypsin Binding Site by Aromatic Amino Acids Can Influence the Processing of β-Casein
Jean-Marc Chobert, Loı̈c Briand, Vinh Tran and Thomas Haertlé Biochemical and Biophysical Research Communications 246(3) 847 (1998) https://doi.org/10.1006/bbrc.1998.8627
INFLUENCE OF G187W/K188F/D189Y MUTATION IN THE SUBSTRATE BINDING POCKET OF TRYPSIN ON ?-CASEIN PROCESSING
Enzymatic Hydrolysis of Milk Proteins Used for Emulsion Formation. 1. Kinetics of Protein Breakdown and Storage Stability of the Emulsions
Samson O. Agboola and Douglas G. Dalgleish Journal of Agricultural and Food Chemistry 44(11) 3631 (1996) https://doi.org/10.1021/jf9602840
Selective determination of phosphopeptide β-CN(1–25) in a β-casein digest by adding iron: characterization by liquid chromatography with on-line electrospray-ionization mass spectrometric detection
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Peptic proteolysis of esterified β‐casein and β‐lactoglobulin
