Abstract
The dissociation of curds by enzymic coagulation by EDTA, urea, and ionic strength was considered to study the forces involved in the curd matrix structure. Curds were obtained at 25 (C25) and 38 °C (C38) and the effect of temperature on these forces was studied. Curd dissociation was followed by quantifying the release of proteins, calcium, and phosphate by the curds mechanically disrupted in the presence of the dissociating agent. In all the cases, the release of whey proteins and mineral revealed the liberation of entrapped whey. At difference with C38, C25 at low EDTA concentrations or with NaCl liberated αS- and β-casein in similar proportions and higher amounts of minerals. Then, coagulation at low temperatures could favor the formation of weak electrostatic bonds involving Ca. Their dissociation by urea at a concentration of 4 M or higher was very effective, especially for C38, suggesting that high temperature favored the formation of hydrophobic interactions.
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Acknowledgments
The authors would like to thank Agencia Nacional de Promoción Científica y Tecnológica, Universidad Nacional de Rosario, and Consejo Nacional de Investigación Científica y Tecnológica, Argentina, for their support in this research. The authors also would like to thank Lic. Mariano Borraccetti for technical assistance and Marcela Culasso, Susana Spirandelli, and María Robson for their assistance in the language correction.
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Alessi, A., Fontana, A., Risso, P. et al. Identification of interactions involved in rennet gel structures using dissociating chemical agents. Colloid Polym Sci 285, 1281–1286 (2007). https://doi.org/10.1007/s00396-007-1692-y
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DOI: https://doi.org/10.1007/s00396-007-1692-y