4.7 Article

Prevention of low-temperature gelation in milk protein concentrates by calcium-binding salts

Journal

JOURNAL OF DAIRY SCIENCE
Volume 105, Issue 1, Pages 32-39

Publisher

ELSEVIER SCIENCE INC
DOI: 10.3168/jds.2021-20264

Keywords

low-temperature gel; calcium-binding salt; emulsifying salt; milk protein concentrate

Funding

  1. National Dairy Coun-cil (Rosemont, IL)
  2. USDA National Institute ofFood and Agriculture (Washington, DC) Federal Ap-propriations [PEN04565, 1002916]

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The study showed that adding low concentrations of calcium-binding salts can effectively prevent low-temperature gelation in milk protein concentrates (MPC), with sodium polyphosphate and sodium monophosphate being the most effective. All MPC samples exhibited shear-thinning behavior, with salt addition reducing viscosity and impacting gel formation.
The objective of this study was to determine the effect of adding low concentrations of calcium-binding salts on the prevention of low-temperature gelation in milk protein concentrates (MPC). The MPC were created by a combination of ultrafiltration and diafiltration, standardized from 14 to 17% (wt/vol) protein content and mixed with one of 5 calcium-binding salts (sodium citrate, sodium hexametaphosphate, sodium polyphos-phate, sodium pyrophosphate, and sodium monophos-phate) adjusted to a pH of 6.75. The flow properties, apparent viscosity, and gel strength were determined for MPC containing a wide range of calcium-binding salt concentrations. Low-temperature gelation occurred in MPC with 16.0% and higher protein content. Low-temperature gelation at 16.0% protein content was prevented by the addition of any of the 5 salts tested at low concentrations (0.30 mM or less; sodium citrate, so-dium hexametaphosphate, sodium polyphosphate, so-dium pyrophosphate or sodium monophosphate), with sodium polyphosphate and sodium monophosphate be -ing the most consistent in preventing low-temperature gels. All MPC samples exhibited shear-thinning behav-ior (n = 0.52-0.72), which increased (lower n values) as the protein content increased and decreased by ad-dition of salt. At concentrations of salt above 1.00 mM, thermally irreversible gels were observed with relative strength dependent on the salt and protein content.

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