Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unit
ABSTRACT: The effect of ethanol on milk has been shown to be temperature-dependent, with higher ethanol concentrations and temperatures reversibly dissociating casein micelles. This work looked to expand on this knowledge, while also demonstrating the efficiency and precision of a custom-made contin...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2022-09-01
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| Series: | Journal of Dairy Science |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022030222004283 |
| _version_ | 1811338482076876800 |
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| author | G. Lewis L.R. Bodinger F.M. Harte |
| author_facet | G. Lewis L.R. Bodinger F.M. Harte |
| author_sort | G. Lewis |
| collection | DOAJ |
| description | ABSTRACT: The effect of ethanol on milk has been shown to be temperature-dependent, with higher ethanol concentrations and temperatures reversibly dissociating casein micelles. This work looked to expand on this knowledge, while also demonstrating the efficiency and precision of a custom-made continuous monitoring unit that combines solutions at defined concentrations and temperatures while measuring various parameters (i.e., absorbance, fluorescence, pressure). Caseins were found to self-associate at moderate ethanol concentrations (i.e., 12–36% vol/vol ethanol); however, they dissociated and remained in the serum at higher ethanol concentrations (≥48% vol/vol) and temperatures (24 and 34°C). Although serum casein content was found to be positively correlated with protein hydrophobicity, the addition of ethanol only increased protein hydrophobicity when the sample was held at high temperatures (34–64°C). Overall, the greatest dissociation of casein micelles was found between 40 and 60% (vol/vol) ethanol concentration at elevated temperatures (≥34°C). At these ethanol concentrations and temperatures, skim milk absorbance was minimized, serum casein content (including β-casein content) was maximized, and protein hydrophobicity reached a relative maximum. |
| first_indexed | 2024-04-13T18:11:30Z |
| format | Article |
| id | doaj.art-ada4ce5787e1459da8f6f77eefb7993b |
| institution | Directory Open Access Journal |
| issn | 0022-0302 |
| language | English |
| last_indexed | 2024-04-13T18:11:30Z |
| publishDate | 2022-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Dairy Science |
| spelling | doaj.art-ada4ce5787e1459da8f6f77eefb7993b2022-12-22T02:35:52ZengElsevierJournal of Dairy Science0022-03022022-09-01105972667275Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unitG. Lewis0L.R. Bodinger1F.M. Harte2Department of Animal and Food Science, University of Wisconsin–River Falls, River Falls 54022Department of Food Science, The Pennsylvania State University, University Park 16802Department of Food Science, The Pennsylvania State University, University Park 16802; Corresponding authorABSTRACT: The effect of ethanol on milk has been shown to be temperature-dependent, with higher ethanol concentrations and temperatures reversibly dissociating casein micelles. This work looked to expand on this knowledge, while also demonstrating the efficiency and precision of a custom-made continuous monitoring unit that combines solutions at defined concentrations and temperatures while measuring various parameters (i.e., absorbance, fluorescence, pressure). Caseins were found to self-associate at moderate ethanol concentrations (i.e., 12–36% vol/vol ethanol); however, they dissociated and remained in the serum at higher ethanol concentrations (≥48% vol/vol) and temperatures (24 and 34°C). Although serum casein content was found to be positively correlated with protein hydrophobicity, the addition of ethanol only increased protein hydrophobicity when the sample was held at high temperatures (34–64°C). Overall, the greatest dissociation of casein micelles was found between 40 and 60% (vol/vol) ethanol concentration at elevated temperatures (≥34°C). At these ethanol concentrations and temperatures, skim milk absorbance was minimized, serum casein content (including β-casein content) was maximized, and protein hydrophobicity reached a relative maximum.http://www.sciencedirect.com/science/article/pii/S0022030222004283ethanolmilkcaseinhydrophobicity |
| spellingShingle | G. Lewis L.R. Bodinger F.M. Harte Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unit Journal of Dairy Science ethanol milk casein hydrophobicity |
| title | Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unit |
| title_full | Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unit |
| title_fullStr | Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unit |
| title_full_unstemmed | Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unit |
| title_short | Characterization of ethanol-induced casein micelle dissociation using a continuous protein monitoring unit |
| title_sort | characterization of ethanol induced casein micelle dissociation using a continuous protein monitoring unit |
| topic | ethanol milk casein hydrophobicity |
| url | http://www.sciencedirect.com/science/article/pii/S0022030222004283 |
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