2005
DOI: 10.1016/j.jfoodeng.2004.04.032
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The influence of main milk components on the hydrophobic interactions of milk protein system in the course of heat treatment

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Cited by 26 publications
(14 citation statements)
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“…The main reaction occurs between b-lactoglobulin and j-casein. Aggregation of casein micelles during fermentation accounts for the presence of fractions with high molecular weight in the protein profile of fermented milk beverages (Steffl et al 1999;Yüksel and Erdem 2005;Rodriguez-Nogales 2006). Figure 2a depicts this phenomenon as a peak with molecular weight above 66 kDa.…”
Section: Influence Of Transglutaminase On Protein Profile Changes In mentioning
confidence: 99%
“…The main reaction occurs between b-lactoglobulin and j-casein. Aggregation of casein micelles during fermentation accounts for the presence of fractions with high molecular weight in the protein profile of fermented milk beverages (Steffl et al 1999;Yüksel and Erdem 2005;Rodriguez-Nogales 2006). Figure 2a depicts this phenomenon as a peak with molecular weight above 66 kDa.…”
Section: Influence Of Transglutaminase On Protein Profile Changes In mentioning
confidence: 99%
“…The difference may be due to the decrease in ''solute phase" effect, which was a result of decreasing SNF concentration. On the other hand, the increasing distance between the micelles caused an increase in the bound ANS, explained as increasing access of the hydrophobic marker to hydrophobic regions in the protein structure (Yuksel & Erdem, 2005). So, decreasing SNF concentration leads to an increase of the accessibility of the ANS to the hydrophobic sites, resulting in an increased F max (Table 1).…”
Section: Reconstituted Milk/green Tea Systemmentioning
confidence: 99%
“…Usually, heating affects the hydrophobic sites of proteins, resulted in protein aggregates via hydrophobic interactions. This aggregation is strongly related to the surface hydrophobicity and the protein denaturation (Yazdi & Corredig, 2012;Yüksel & Erdem, 2005). The SH measurement probed by ANS is one of a simple method that can be used to evaluate the protein denaturation (Alizadeh-Pasdar & Li-Chan, 2000;Hayakawa & Nakai, 1985;Nakai, 1983).…”
Section: Encapsulation Efficiency and Surface Hydrophobicitymentioning
confidence: 99%