Stability of casein micelles cross-linked with genipin: A physicochemical study as a function of pH
Chemical or enzymatic cross-linking of casein micelles (CMs) increases their stability against dissociating agents. In this paper, a comparative study of stability between native CMs and CMs cross-linked with genipin (CMs-GP) as a function of pH is described. Stability to temperature and ethanol wer...
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Published in | International dairy journal Vol. 68; pp. 70 - 74 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Ltd
01.05.2017
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | Chemical or enzymatic cross-linking of casein micelles (CMs) increases their stability against dissociating agents. In this paper, a comparative study of stability between native CMs and CMs cross-linked with genipin (CMs-GP) as a function of pH is described. Stability to temperature and ethanol were investigated in the pH range 2.0–7.0. The size and the charge (ζ-potential) of the particles were determined by dynamic light scattering. Native CMs precipitated below pH 5.5; CMs-GP precipitated from pH 3.5 to 4.5, whereas no precipitation was observed at pH 2.0–3.0 or pH 4.5–7.0. The isoelectric point of CMs-GP was determined to be pH 3.7. Highest stability against heat and ethanol was observed for CMs-GP at pH 2, where visible coagulation was determined only after 800 s at 140 °C or 87.5% (v/v) of ethanol. These results confirmed the hypothesis that cross-linking by GP increased the stability of CMs. |
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ISSN: | 0958-6946 1879-0143 |
DOI: | 10.1016/j.idairyj.2016.12.006 |