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Temperature dependence of the casein micelle structure in the range of 10–40 °C: An in-situ SAXS study

Food Chemistry, ISSN: 0308-8146, Vol: 393, Page: 133389
2022
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Findings from High Energy Accelerator Research Organization Yields New Data on Phosphoproteins (Temperature Dependence of the Casein Micelle Structure In the Range of 10-40 Degrees C: an In-situ Saxs Study)

2022 NOV 08 (NewsRx) -- By a News Reporter-Staff News Editor at Japan Daily Report -- Investigators discuss new findings in Proteins - Phosphoproteins. According

Article Description

Milk is used and processed under various environmental temperature, and its physicochemical properties are also strongly affected by temperature. Therefore, it is important to reveal the structure of milk at variable temperatures. In this study, the temperature dependence of the inner structure of bovine casein micelles in the temperature range of 10–40 °C was investigated by in-situ small-angle X-ray scattering (SAXS) method. The micelle size calculated from the SAXS profiles using a micelle model including water domains was almost independent of temperature. The water domain expanded and the distance between the colloidal calcium phosphates (CCP) decreased with increasing temperature. The number of CCPs in a micelle increased, because CCPs were newly formed by the transfer of calcium and inorganic phosphate from serum into the micelle. These structural changes occurred during the cooling process. Therefore, in the temperature range of 10–40 °C, the structure of the casein micelle varied sensitively with the temperature, and these structural changes were thermoreversible in nature.

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