title: Food protein aggregates as vitamin-matrix carriers: impact of processing conditions.
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).
authors: AgroParisTech, UMR1145 (INRA, AgroParisTech, CNAM), Department of Science and Engineering of Food and Bioproducts, 1 Avenue des Olympiades, 91300 Massy, France. perla.relkin@agroparistech.fr
authors: Perla
authors: P
authors: Relkin
authors: Rizwan
authors: R
authors: Shukat
mesh_terms: D005511:Food Handling; D006358:Hot Temperature; D008894:Milk Proteins / Q000737:chemistry*; D010316:Particle Size; D011312:Pressure; D011485:Protein Binding; D014815:Vitamins / Q000737:chemistry*; D000067816:Whey Proteins
chemical_list: D008894:Milk Proteins; D014815:Vitamins; D000067816:Whey Proteins