2006
DOI: 10.1016/j.idairyj.2005.04.001
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Structure and surface properties of the serum heat-induced protein aggregates isolated from heated skim milk

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Cited by 85 publications
(98 citation statements)
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References 34 publications
(54 reference statements)
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“…A band representing the largest casein, α S2 , is present on SDS-PAGE in some of the samples, notably 1.1 and 1.4, and in 2.1 and 2.4. The qualitative compositional analyses of the soluble aggregate fractions are generally in line with previous reports [17,18,22,32]. These studies consider that the primary constituents of the aggregates are β-lactoglobulin, α-lactalbumin and κ-casein.…”
Section: Soluble Aggregate Compositionsupporting
confidence: 88%
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“…A band representing the largest casein, α S2 , is present on SDS-PAGE in some of the samples, notably 1.1 and 1.4, and in 2.1 and 2.4. The qualitative compositional analyses of the soluble aggregate fractions are generally in line with previous reports [17,18,22,32]. These studies consider that the primary constituents of the aggregates are β-lactoglobulin, α-lactalbumin and κ-casein.…”
Section: Soluble Aggregate Compositionsupporting
confidence: 88%
“…Unfortunately many different techniques have been used to separate the micellar and serum phases. Centrifugation is the most common but many different conditions have been used, ranging from 175 000× g/60 min to 19 200× g/240 min [2,4,11,17,18,22,29,32,33,[35][36][37]41]. Other researchers have rejected the use of centrifugation on the basis of being too harsh and likely to cause micellar disintegration and have used treatment with rennet to precipitate the micelle fraction instead [38].…”
Section: Resultsmentioning
confidence: 99%
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“…The protein composition of the initial milk samples and of their serum and colloidal phases separated by ultracentrifugation were determined by RP-HPLC as described in [16]. Briefly, the samples were diluted 5 times with denaturing buffer (7 mol·L -1 urea, 20 mmol·L -1 Bis-Tris Propane, pH 7.5, + 5 µL·mL -1 of fresh β-mercaptoethanol) then incubated for 1 h at 37 °C.…”
Section: Quantification Of Heat-induced Protein Transfers By Reversepmentioning
confidence: 99%