Statistical thermodynamics of casein aggregation: Effects of salts and water

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Statistical thermodynamics of casein aggregation: Effects of salts and water. / Harton, Kaja; Shimizu, Seishi.

In: Biophysical Chemistry, Vol. 247, 12.02.2019, p. 34-42.

Research output: Contribution to journalArticlepeer-review

Harvard

Harton, K & Shimizu, S 2019, 'Statistical thermodynamics of casein aggregation: Effects of salts and water', Biophysical Chemistry, vol. 247, pp. 34-42. https://doi.org/10.1016/j.bpc.2019.02.004

APA

Harton, K., & Shimizu, S. (2019). Statistical thermodynamics of casein aggregation: Effects of salts and water. Biophysical Chemistry, 247, 34-42. https://doi.org/10.1016/j.bpc.2019.02.004

Vancouver

Harton K, Shimizu S. Statistical thermodynamics of casein aggregation: Effects of salts and water. Biophysical Chemistry. 2019 Feb 12;247:34-42. https://doi.org/10.1016/j.bpc.2019.02.004

Author

Harton, Kaja ; Shimizu, Seishi. / Statistical thermodynamics of casein aggregation: Effects of salts and water. In: Biophysical Chemistry. 2019 ; Vol. 247. pp. 34-42.

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@article{32a038f39940463da2b4f14f3b3709d3,
title = "Statistical thermodynamics of casein aggregation:: Effects of salts and water",
abstract = "Salts, when added to milk, profoundly influence casein aggregation.. Even though this well-known phenomenon has been widely exploited, there are still many unanswered questions. How do salts affect casein aggregation? Does water contribute significantly to the aggregation change? The key to answering these questions comes from statistical thermodynamics, i.e., the principles of physics that can link macroscopic data to the collective behaviour of molecules. We present two theoretical approaches, a rigorous approach which demands far more measurements than reported hitherto, and an approximate and pragmatic approach based on stoichiometric models (isodesmic model for aggregation equilibria and von Smoluchowski model for kinetics) that can yield information on protein-water and protein-salt interactions from “real life” experimental measurements on a model systems available in a wide variety of formats. Using the experimental data in the literature, casein aggregation in the absence of κ-casein has been shown to be modulated by protein-salt interaction, while the contribution from water structure changes has been shown to be negligible. ",
author = "Kaja Harton and Seishi Shimizu",
note = "{\textcopyright} 2019 Elsevier B.V. All rights reserved. This is an author-produced version of the published paper. Uploaded in accordance with the publisher{\textquoteright}s self-archiving policy. ",
year = "2019",
month = feb,
day = "12",
doi = "10.1016/j.bpc.2019.02.004",
language = "English",
volume = "247",
pages = "34--42",
journal = "Biophysical Chemistry",
issn = "0301-4622",
publisher = "Elsevier",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Statistical thermodynamics of casein aggregation:

T2 - Effects of salts and water

AU - Harton, Kaja

AU - Shimizu, Seishi

N1 - © 2019 Elsevier B.V. All rights reserved. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy.

PY - 2019/2/12

Y1 - 2019/2/12

N2 - Salts, when added to milk, profoundly influence casein aggregation.. Even though this well-known phenomenon has been widely exploited, there are still many unanswered questions. How do salts affect casein aggregation? Does water contribute significantly to the aggregation change? The key to answering these questions comes from statistical thermodynamics, i.e., the principles of physics that can link macroscopic data to the collective behaviour of molecules. We present two theoretical approaches, a rigorous approach which demands far more measurements than reported hitherto, and an approximate and pragmatic approach based on stoichiometric models (isodesmic model for aggregation equilibria and von Smoluchowski model for kinetics) that can yield information on protein-water and protein-salt interactions from “real life” experimental measurements on a model systems available in a wide variety of formats. Using the experimental data in the literature, casein aggregation in the absence of κ-casein has been shown to be modulated by protein-salt interaction, while the contribution from water structure changes has been shown to be negligible.

AB - Salts, when added to milk, profoundly influence casein aggregation.. Even though this well-known phenomenon has been widely exploited, there are still many unanswered questions. How do salts affect casein aggregation? Does water contribute significantly to the aggregation change? The key to answering these questions comes from statistical thermodynamics, i.e., the principles of physics that can link macroscopic data to the collective behaviour of molecules. We present two theoretical approaches, a rigorous approach which demands far more measurements than reported hitherto, and an approximate and pragmatic approach based on stoichiometric models (isodesmic model for aggregation equilibria and von Smoluchowski model for kinetics) that can yield information on protein-water and protein-salt interactions from “real life” experimental measurements on a model systems available in a wide variety of formats. Using the experimental data in the literature, casein aggregation in the absence of κ-casein has been shown to be modulated by protein-salt interaction, while the contribution from water structure changes has been shown to be negligible.

U2 - 10.1016/j.bpc.2019.02.004

DO - 10.1016/j.bpc.2019.02.004

M3 - Article

VL - 247

SP - 34

EP - 42

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

ER -