Journal
FOOD CHEMISTRY
Volume 192, Issue -, Pages 415-423Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2015.07.037
Keywords
Whey protein isolates; High intensity ultrasound; Differential scanning calorimetry; Circular dichroism; Dynamic rheology; Denaturation; Protein structure
Funding
- Danish Dairy Research Foundation
- Arla Foods
- Arla Foods Ingredients
- Future Food Innovation
- inSPIRe Food platform via the Innovation Fund Denmark
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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 a-lactalbumin (a-La) were associated with increased sensitivity to ultrasonication. The alpha-La:beta-lactoglobulin (8-Lg) ratio greatly affected the nature of the interactions formed during gelation, where higher amounts of a-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. (C) 2015 Elsevier Ltd. All rights reserved.
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