Hydrophobic Components in Delipidated Granule of Egg Yolk

Tsutsui, Tomomi; Obara, Tetsujirô

doi:10.1080/00021369.1982.10865476

Cited by 7 publications

(6 citation statements)

References 7 publications

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“…F1 from AEC at pH 8 was fractionated into two peaks by gel filtration using Sephadex G-75 column named as F1 (GFC) and F2 (GFC). This result shared some similarities with previous results (Abe et al, 1982;Tsutsui & Obara, 1982). In accordance with Abe et al phosvitin was fractionated into two fractions on a Sephadex G-200 column.…”

Section: Gel-filtration Chromatographysupporting

confidence: 91%

Evaluation of the purification process of phosvitin extracted from chicken egg yolk using liquid chromatography

Tran¹,

Vo²

2021

CTUJS

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Phosvitin from chicken egg yolk, known as a phosphoglycoprotein, owns a very strong metal chelating property due to its polyanionic character. This study aimed to evaluate the factors affecting the purification process and suitable conditions to increase phosvitin’s purity. Phosvitin was separated from yolk granules by using 10% of NaCl solution in 0.05 M NaOH solution and heat treatment which removes lipoprotein from the extracted solution. The highest phosphorus content (58.14 mg) and phosphorus recovery rate (32.4%) were obtained at thermal treatment of 30℃ for 30 minutes. In addition, phosvitin was purified using anion-exchange chromatography (AEC) and gel-filtration chromatography (GFC). The fraction 1 (F1) obtained from AEC using UNO-Sphere Q at pH 8 had the recovery rate of phosvitin approximately 72.73%. Furthermore, fraction F1 was separated on GFC to obtain two main sub-fractions (F1 and F2). Sub-fraction F1 from gel filtration was composed mostly of β-phosvitin with a high recovery rate (81.93%) while F2 was dominant with α-phosvitin in a lower phosvitin recovery rate (16.89%). These findings will provide useful information for further researches on other properties of phosvitin so that it can be applied widely in human needs.

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Section: Gel-filtration Chromatographysupporting

confidence: 91%

Evaluation of the purification process of phosvitin extracted from chicken egg yolk using liquid chromatography

Tran¹,

Vo²

2021

CTUJS

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“…Heating provokes weakening of lipid-protein interactions due to protein unfolding, favoring structural disruption, after which interactions between proteins are increased leading to gel formation. Tsutsui et al (20) assumed that lipids are included in the structure of LDL aggregates.…”

Section: Discussionmentioning

confidence: 99%

Structuring and Functionalization of Dispersions Containing Egg Yolk, Plasma and Granules Induced by Mechanical Treatments

Sirvente

Beaumal

Gaillard

et al. 2007

J. Agric. Food Chem.

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In this study, the impact of mechanical treatments on the physicochemical and emulsifying properties of hen egg yolk and its fractions plasma and granules has been assessed. Yolk, plasma, and granule dispersions at pH 4.0 and 0.75 M NaCl were subjected to rotor-stator and high-pressure pretreatments at different dynamic pressure levels: 30, 100, and 200 bar at 20 degrees C. Physicochemical characteristics (protein solubility, rheological behavior, and micro- and ultra-structures) and emulsifying properties (oil/water 60:40 emulsions: droplet size and flocculation, protein adsorption) of control dispersions and dispersions subjected to mechanical pretreatments (rotor-stator or high pressure) were compared. Homogenization at high pressures (100 and 200 bar) led to a decreased protein solubility and to an increase in apparent viscosity of yolk and plasma dispersions. These pressures certainly disrupted low-density lipoproteins (LDL) particles and generated aggregates of proteins liberated from LDL and livetins in the plasma fraction, and led to a moderated reorganization of the microstructure of granules. Despite the modifications observed in the pretreated plasma and granules dispersions, the oil droplet diameter and the bridging flocculation obtained in emulsions made with these dispersions were similar to that obtained with untreated dispersions. Results concerning interfacial protein adsorption suggested that preformed or natural aggregates at least partially persist at the oil-water interface.

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“…further purification or separation of phosvitin, ion exchange chromatography (Connelly and Taborsky, 1961;McLachlan, 1963, 1964;Castellani et al, 2003) and gel filtration (Connelly and Taborsky, 1961;Clark, 1970;Abe et al, 1982;Tsutsui and Obara, 1982) have been used. However, gel filtration is not appropriate for large-scale separation of phosvitin, and the application of ion exchange chromatography for purifying phosvitin depends on the precise nature of the ion exchangers (Mok et al, 1966) and is not applicable for commercial-scale methods.…”

Section: Introductionmentioning

confidence: 99%

A simple and efficient method for preparing partially purified phosvitin from egg yolk using ethanol and salts

Nam

et al. 2011

Poultry Science

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The objective of this study was to develop a new protocol that could be used for large-scale separation of phosvitin from egg yolk using ethanol and salts. Yolk granules, which contain phosvitin, were precipitated after diluting egg yolk with 9 volumes of distilled water. The pH of the yolk solution was adjusted to pH 4.0 to 8.0 using 6 N HCl or NaOH, and then yolk granules containing phosvitin was separated by centrifugation at 3,220 × g for 30 min. Lipids and phospholipids were removed from the insoluble yolk granules using 85% ethanol. The optimal volumes and concentration of ethanol in removing lipids from the precipitants were determined. After centrifugation, the lipid-free precipitants were homogenized with 9 volumes of ammonium sulfate [(NH(4))(2)SO(4)] or NaCl to extract phosvitin. The optimal pH and concentration of (NH(4))(2)SO(4) or NaCl for the highest recovery rate and purity for phosvitin in final solution were determined. At pH 6.0, all the phosvitin in diluted egg yolk solution was precipitated. Among the (NH(4))(2)SO(4) and NaCl conditions tested, 10% (NH(4))(2)SO(4) or 10% NaCl at pH 4.0 yielded the greatest phosvitin extraction from the lipid-free precipitants. The recovery rates of phosvitin using (NH(4))(2)SO(4) and NaCl were 72 and 97%, respectively, and their purity was approximately 85%. Salt was removed from the extract using ultrafiltration. The salt-free phosvitin solution was concentrated using ultrafiltration, the impurities were removed by centrifugation, and the resulting solution was freeze-dried. The partially purified phosvitin was suitable for human use because ethanol was the only solvent used to remove lipids, (NH(4))(2)SO(4) or NaCl was used to extract phosvitin, and ultrafiltration was used to remove salt and concentrate the extract. The developed method was simple and suitable for a large-scale preparation of partially purified phosvitin.

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Hydrophobic Components in Delipidated Granule of Egg Yolk

Cited by 7 publications

References 7 publications

Evaluation of the purification process of phosvitin extracted from chicken egg yolk using liquid chromatography

Evaluation of the purification process of phosvitin extracted from chicken egg yolk using liquid chromatography

Structuring and Functionalization of Dispersions Containing Egg Yolk, Plasma and Granules Induced by Mechanical Treatments

A simple and efficient method for preparing partially purified phosvitin from egg yolk using ethanol and salts

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