AI Article Synopsis

  • The study investigated how high intensity ultrasound (HIU) affects whey protein isolates, focusing on thermal behavior and bonding changes during gelling.
  • Results indicated that ultrasonication reduced the energy needed for protein denaturation but did not alter the secondary structure of the proteins.
  • The findings revealed that the ratio of different whey proteins, specifically α-lactalbumin to β-lactoglobulin, influenced gel formation and the reliance on disulfide bonds, which could improve HIU applications in food processing.

Article Abstract

In this study, the impact of high intensity ultrasound (HIU) on proteins in whey protein isolates was examined. Effects on thermal behavior, secondary structure and nature of intra- and intermolecular bonds during heat-induced gelling were investigated. Ultrasonication (24 kHz, 300 W/cm(2), 2078 J/mL) significantly reduced denaturation enthalpies, whereas no change in secondary structure was detected by circular dichroism. The thiol-blocking agent N-ethylmaleimide was applied in order to inhibit formation of disulfide bonds during gel formation. Results showed that increased contents of α-lactalbumin (α-La) were associated with increased sensitivity to ultrasonication. The α-La:β-lactoglobulin (β-Lg) ratio greatly affected the nature of the interactions formed during gelation, where higher amounts of α-La lead to a gel more dependent on disulfide bonds. These results contribute to clarifying the mechanisms mediating the effects of HIU on whey proteins on the molecular level, thus moving further toward implementing HIU in the processing chain in the food industry.

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http://dx.doi.org/10.1016/j.foodchem.2015.07.037DOI Listing

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