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• W2022503408 abstract "We studied the ability of protein aggregates for loading and protection of α-tocopherol, a model of heat- and light-sensitive bioactive compounds. Aqueous dispersions of whey proteins (4.5 wt.%, pH 6.7) in the absence and presence of α-tocopherol (4 wt.%) were prepared using an ultradisperser (10,000 rpm for 10 min and 65 °C), and then submitted to further high-pressure homogenisation (HPH) at 300 or 1200 bar for 12 cycles. Relative to free-vitamin dispersions, increasing HPH conditions in the presence of vitamin led to higher protein denaturation, more tryptophan quenching and wavelength blue-shift (by 10nm), in parallel with increased zeta potential values (by -10 mV), particle sizes (by 50%), and newly formed protein dimers, trimers and high molecular weight aggregates. As a result, the degree of vitamin degradation under increasing HPH and long-term storage was shown to decrease from 66% (ultradisper) to 50%, or to 30% (subject to further treatments at 300 or 1200 bar, respectively)." @default.
• W2022503408 created "2016-06-24" @default.
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• W2022503408 date "2012-10-01" @default.
• W2022503408 modified "2023-10-14" @default.
• W2022503408 title "Food protein aggregates as vitamin-matrix carriers: Impact of processing conditions" @default.
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• W2022503408 doi "https://doi.org/10.1016/j.foodchem.2012.04.020" @default.
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