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EC number: 947-990-9 | CAS number: -
Vapour pressure
Administrative data
Link to relevant study record(s)
- Endpoint:
- vapour pressure
- Data waiving:
- study technically not feasible
- Justification for data waiving:
- other:
- Reason / purpose for cross-reference:
- data waiving: supporting information
Reference
Description of key information
Protein denaturation through heat involves changes in protein structure (generally an unfolding) with the loss of structure, solubility and function of the protein. Depending on the temperature, denaturation is usually reversible. Heat denaturation of proteins at temperatures >80°C on the other hand is usually irreversible induced through aggregation of the proteins after heat denaturation (Matsuura et. al., 2015).
A study investigated the denaturation of whey protein and caseins in raw milk after heat treatment dependent on treatment duration as well as temperature. As expected, the denaturation ratio of the proteins increased with longer duration and higher temperatures. After treatment for 30 min at 85°C for instance, approximately 100 % of the whey proteins and caseins were denatured (Fang et. al., 2017). Based on these findings and the fact that the protein composition of milk and yoghurt is very similar (for details see cross-reference link), treatment of yoghurt powder with high temperature over a period of time will lead to denaturation of the contained proteins. This denatured form differs from the non-denatured one in terms of physical and chemical properties.
The milk proteins contained in Bos taurus, milk, fermented, spray-dried EC 917 -734 -0 (for details check the composition) will therefore undergo thermal denaturation upon heating. Hence, it will be not possible to determine the vapour pressure for Bos taurus, milk, fermented, spray-dried.
Key value for chemical safety assessment
Additional information
References:
Matsuura Y, Takehira M, Joti Y, Ogasahara K, Tanaka T, Ono N, Kunishima N, Yutani K. (2015). Thermodynamics of protein denaturation at temperatures over 100°C: CutA1 mutant proteins substituted with hydrophobic and charged residues. Sci. Rep. Oct 26;5:15545.
Fang Qian, Jiayue Sun, Di Cao, Yanfeng Tuo, Shujuan Jiang, and Guangqing Mu (2017). Experimental and Modelling Study of the Denaturation of Milk Protein by Heat Treatment. Korean J. Food. Sci. Anim. Resour. 2017; 37(1): 44–51.
Information on Registered Substances comes from registration dossiers which have been assigned a registration number. The assignment of a registration number does however not guarantee that the information in the dossier is correct or that the dossier is compliant with Regulation (EC) No 1907/2006 (the REACH Regulation). This information has not been reviewed or verified by the Agency or any other authority. The content is subject to change without prior notice.
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