4.7 Article

Structure rearrangement during rennet coagulation of milk modifies curd density

Journal

JOURNAL OF DAIRY SCIENCE
Volume 103, Issue 4, Pages 3088-3094

Publisher

ELSEVIER SCIENCE INC
DOI: 10.3168/jds.2019-16998

Keywords

curd density; curd temperature; curd pH; curd protein phase density; curd syneresis

Funding

  1. Mexican National Council of Science and Technology (CONACYT, Mexico City)

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Milk curds are a semisolid structure resulting from the enzymatic coagulation of milk, consisting mainly of paracasein micelles, fat globules, and whey. This gel undergoes a series of changes in its composition and structure during setting and curing, affecting curd density. The present study investigated the composition and density of inoculated and noninoculated milk curds during a 60-min curing period conducted at 30, 35, and 40 degrees C. The purpose of the study was to determine the density changes occurring in the protein phase of curds during curing under different conditions of temperature and pH to understand the nature of the structural changes happening in the paracaseiri matrix. Nonirioculated curd density values oscillated between 1.0247 and 1.0294 g/cm(3) after 60 min of curing, whereas inoculated treatments showed values between 1.0222 and 1.0321 g/cm(3). This small difference in density between the studied samples was surprising because the whey content of samples differed greatly. Density of the protein phase reached values of 1.8002 and 1.4388 g/cm(3) for noninoculated arid inoculated curds, respectively, after 60 min of curing. Two independent mechanisms involved in the development of the protein-based structure of curds were identified upon comparison of the development of protein phase density in inoculated arid noninoculated curds. Although the larger increase in protein phase density observed in noninoculated curds was probably due to the concurrent action of calcium-mediated electrostatic bonds and temperature-dependent hydrophobic bonds, inoculated curds showed a lower protein phase density caused by calcium solubilization and by a decrease in the net charge of paracasein micelles induced by pH reduction.

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