This study investigated the effects of supplementing diets consisting of two dent corn hybrids (soft- and hard-type) with different amounts of rapeseed oil (2, 3, and 4%) and with (0.05%) or without emulsifier (Lysoforte Extended, Kemin) on the content and deposition of carotenoids in egg yolk. The feeding trial was conducted with 216 Lohmann Brown laying hens which were by 3 located in 72 cages.
View Article and Find Full Text PDFCarotenoids in maize grain degrade during storage, but the relationship between their stability and the physicochemical properties of the grain is unclear. Therefore, the carotenoid degradation rate in milled grain of three dent hybrids differing in grain hardness was evaluated at various temperatures (-20, 4 and 22 °C). The carotenoid degradation rate was calculated using first-order kinetics based on the content in the samples after 7, 14, 21, 28, 42, 56, 70 and 90 days of storage and related to the physicochemical properties of the grain.
View Article and Find Full Text PDFThe aim of this study was to evaluate the effect of a supplementation diet for hens consisting of dried basil herb and flowers of calendula and dandelion for color, carotenoid content, iron-induced oxidative stability, and sensory properties of egg yolk compared with commercial pigment (control) and marigold flower. The plant parts were supplemented in diets at two levels: 1% and 3%. In response to dietary content, yolks from all diets differed in carotenoid profile ( < 0.
View Article and Find Full Text PDFBackground: The kinetics of starch digestion is a key determinant of poultry performance. Research so far has shown that starch digestibility kinetics depends on the molecular structure of starch but also on the properties of the complex matrix in which starch granules are embedded in most feedstuffs. However, the manner in which genotype differences in the same plant affect starch digestibility kinetics has not yet been addressed.
View Article and Find Full Text PDFLiquid chromatography coupled with electrospray ionization mass spectrometry (ESI-MS) is routinely used in proteomics research. Mass spectrometry-based peptide analysis is performed de facto in positive-ion mode, except for the analysis of some post-translationally modified peptides (e.g.
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