Bioactive Egg Compounds by Marc Anton (auth.), Professor Rainer Huopalahti, Rosina

By Marc Anton (auth.), Professor Rainer Huopalahti, Rosina López-Fandiño, Marc Anton, Rüdiger Schade (eds.)

Hen eggs have unparalleled strength as an inexhaustible resource for numerous items with distinct homes. those items are beneficial to human well-being and nutrients and will be used as uncooked fabrics for varied reasons within the cosmetics and pharmaceutical industries.

Bioactive Egg Compounds provides the most recent effects and ideas within the biotechnological use of egg compounds. Following an creation to different compounds of egg white, yolk and shell, the nutritive worth of egg compounds is mentioned. tactics for processing egg compounds to enhance their nutritive price are defined, together with the idea that of so-called enriched eggs. additionally defined is the isolation and alertness of egg compounds with distinctive homes, corresponding to antibiotic motion.

The chapters are by means of authors from 12 nations, all well known experts, who're energetic in a variety of fields of egg study, similar to qc, biochemistry, biophysics and biotechnology.

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Iron fixation by phosvitin as influenced by pH and ionic strength. 5 (Baumy and Brulé 1988). 6 M NaCl. 2. For higher pH values, increase in salt concentration leads to a decrease in iron binding capacity, and for lower pH values the opposite tendency is observed. 8), and so the proportion of partially protonated phosphates begins to be important. Consequently, when phosvitin has a large proportion of completely dissociated phosphates, the presence of salt ions might have a screening effect between iron atoms and phosvitin when increasing NaCl concentration.

74 M; this provokes the disruption of the phosphocalcic bridges binding phosvitin and HDL, and replacing them with sodium ions. The solution is then dialyzed against distilled water for 24 h. Calcium ions and excess sodium ions are eliminated by the dialysis. 25 and the solution is centrifuged at 10,000 g for 30 min at 4 °C. 2 M. This provokes the precipitation of phosvitin after a centrifugation at 10,000 g for 30 min. The pellet enriched in phosvitin contains about 15% impurities (βlivetin, α-HDL et β-HDL; Fig.

331 kDa in spite of a slight heterogeneity, and its amino acid sequence has been totally confirmed through the analysis of trypsin peptides. Hen apo-B is known to be cleaved into several protein fragments by cathepsin D. The structural homology of hen apo-B with human apoB-100 has been verified, and sequence alignment could be an interesting tool for further the characterization of hen apo-B. 98) allowed an efficient separation. However, this type of technique is extremely time consuming (several days of centrifugation) and the yield of extraction is very low (only few grams of LDL), prohibiting a scale-up of the method.

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