2011
DOI: 10.1016/j.foodchem.2010.10.021
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Temperature dependence of calcium and magnesium induced caseinate precipitation in H2O and D2O

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Cited by 34 publications
(13 citation statements)
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References 30 publications
(31 reference statements)
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“…Presumably, the addition of glutamic acid derivatives (D-gluconate, L-pidolate) contributed to the increase in cross-linking of casein bonds and the creation of a better matrix to retain whey. Cuomo et al [39] concluded that Ca 2+ and Mg 2+ ions have different binding sites on the casein, phosphoserine for calcium and glutamic and aspartic acids for magnesium. The authors also suggested that the presence of calcium aids the binding of magnesium by making more sites available.…”
Section: Physicochemical Propertiesmentioning
confidence: 99%
“…Presumably, the addition of glutamic acid derivatives (D-gluconate, L-pidolate) contributed to the increase in cross-linking of casein bonds and the creation of a better matrix to retain whey. Cuomo et al [39] concluded that Ca 2+ and Mg 2+ ions have different binding sites on the casein, phosphoserine for calcium and glutamic and aspartic acids for magnesium. The authors also suggested that the presence of calcium aids the binding of magnesium by making more sites available.…”
Section: Physicochemical Propertiesmentioning
confidence: 99%
“…The existence of enzymatic activity in FL and DL was preliminary examined in vivo by monitoring the changes of the endogenous phenolic profile of leaves after an heating treatment performed at 60°C for 24 h. The temperature conditions used (60°C) was chosen in accordance with other studies (R. Briante et al, 2004;De Leonardis & Macciola, 2011;. Moreover, the effects induced by exposure of proteins to temperature treatments have been recognized as a suitable tool to shed light on the general mechanisms responsible for the structural stability and functionality of peptides (Cuomo, Ceglie, & Lopez, 2011). Both the FL and DL samples were homogenized with distilled water and changes of their phenolic content were monitored during the following 24 h at 60°C by HPLC.…”
Section: Enzymatic Activity Of Olive Leaf Homogenatementioning
confidence: 99%
“…The photophysical properties of tyrosine and its derivatives are very complex and have been widely investigated [1][2][3][4][5][6]. The fluorescence of aromatic amino acids and their residues incorporated into a peptide or protein chain is the subject of extensive studies because of their use as internal probes in conformational analysis [7][8][9].…”
Section: Introductionmentioning
confidence: 99%