Association behavior of β-casein

O'Connell, J E A; Grinberg, V. Ya.; Kruif, C. G. de

doi:10.1016/s0021-9797(02)00066-8

Cited by 177 publications

(139 citation statements)

References 16 publications

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“…The levels of casein were reduced (p<0.05). It is well known that during mastitis, casein synthesis is usually reduced, similar to results found by Santos et al [53] and O`Connell et al [55]. Nevertheless, some authors found no significant reduction in casein when correlated with high SCC [10,40,[56][57][58][59].…”

Section: Composition Of Milk With Different Somatic Cell Countssupporting

confidence: 70%

Effect of Somatic Cell Count on Bovine Milk Protein Fractions

TM¹

2015

J Anal Bioanal Tech

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Section: Composition Of Milk With Different Somatic Cell Countssupporting

confidence: 70%

Effect of Somatic Cell Count on Bovine Milk Protein Fractions

TM¹

2015

J Anal Bioanal Tech

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“…16 Casein, especially β-casein as the most hydrophobic protein among κ-, α s1 -, and α s2 -casein, may form micelles and submicelles (CMC=0.05%-0.2% w/v). 17 In the comparison with globular proteins, casein is known to be easily hydrolysed by proteases because of its elevated conformational flexibility and the abundance of the enzymeaccessible peptide bonds. 14 It was reported that clusters of hydrophobic amino acid residues in the polypeptide chain of casein substrate cause hydrophobic interaction to be responsible for the steric obstacles shielding peptide bonds against enzymatic attack.…”

Section: Resultsmentioning

confidence: 99%

Monitoring of Demasking of Peptide Bonds During Proteolysis by Analysis of the Apparent Spectral Shift of Intrinsic Protein Fluorescence

et al. 2011

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Demasking of peptide bonds during proteolysis of β-casein and β-lactoglobulin by trypsin was monitored by the measurement of the overall spectral shift of intrinsic protein fluorescence. A clear shift of the apparent emission maxima from approximately 340-345 nm to 355-360 nm during proteolysis was observed, with a time course, which follows protein degradation and structural opening. In contrast to procedures using extrinsic fluorescence labels, this label-free procedure does not bear the risk of structural alterations. It is easy to perform, fast, and has a relatively high accuracy of determination. Proteolysis was modelled as simple two-step process with consecutive demasking and hydrolysis stages. It was shown that the fluorescence shift can be attributed to the demasking stage. Formally, kinetics of the peptide bond demasking obeys a first-order kinetic law. Both the theoretical simulations and experiment are in accordance giving the similar dependences of the hydrolysis degree on the degree of peptide bond demasking.

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“…The thickness and structure of the stabilizing layer are sensitive to pH, ionic strength and calcium ion content. The amphiphilic character of ␤-casein leads to a tendency towards self-assembly in the aqueous phase [54][55][56]. While the protein is monomeric at 4 • C, at higher temperatures it associates into surfactant-like micelles (size ∼25 nm) above a certain critical micelle concentration.…”

Section: 1ˇ-caseinmentioning

confidence: 99%