Solubilization and Characterization of Ovomucin without Chemical Modification

Adachi, Noboru; Azuma, Jun-ichi; Janado, Masanobu; Onodera, Kônoshin

doi:10.1080/00021369.1973.10860952

Cited by 5 publications

(3 citation statements)

References 2 publications

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“…ovotransferrin, ovalbumin, ovomucoid, and lysozyme revealed that peak elution volumes were at 57.6, 64.4, 71.2, and 81.3 mL, respectively. The peak elution volume of ovomucin in the present study was 50.0 mL, compared to the previously reported value of 56 mL by Adachi et al (22 ). Our results showed that the major contaminated proteins in the ovomucin precipitates are ovalbumin and lysozyme; at increasing salt concentrations, the peak corresponding to the ovalbumin fraction increased, whereas the peak corresponding to lysozyme decreased.…”

Section: Resultssupporting

confidence: 52%

“…Proximate composition of ovomucin prepared by the 2-step method (after dialysis) revealed a protein content of 69.7% (Table ). The protein content of ovomucin isolated from thick white and thin white was found to be 66.1% and 71.5%, respectively . The protein content of the control ovomucin (without salt addition and without KCl washing) and freeze-dried egg white was found to be high due to the low contents of moisture and ash.…”

Section: Resultsmentioning

confidence: 92%

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A New Method of Separating Ovomucin from Egg White

Omana

2009

J. Agric. Food Chem.

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Ovomucin, a key component in maintaining the viscous nature of egg white, is a glycoprotein contributing to 2-4% of the total egg albumin protein. Preparation of pure ovomucin remains a challenge due to the presence of coprecipitated proteins, mainly ovalbumin and lysozyme. The objectives of the study were to determine the effect of different salt concentrations on the extractability of ovomucin and to develop a simple method to purify ovomucin that could be adapted for further scale-up production. The protein compositions of ovomucin extracts were significantly affected by salt concentrations. The concentration of ovalbumin was increased, whereas that of lysozyme was decreased in the ovomucin extracts at increasing salt concentrations up to 500 mM; lysozyme was the major contaminant at low salt concentrations (<100 mM), whereas ovalbumin was the major contaminant at high concentrations (>or=200 mM). A 2-step method was developed for the first time to prepare ovomucin with a purity of greater than 90%. Egg white was first extracted in the presence of 100 mM NaCl at pH 6.0 to produce a precipitate containing moderate coprecipitated ovalbumin (14.6%) and lysozyme (15.9%); the contaminated proteins in the precipitate were further removed by using 500 mM NaCl. The yield of ovomucin was determined to be 400.2 mg/100 g of egg white. This 2-step method is simple, environmentally friendly, and easy for scale-up preparation.

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Section: Resultssupporting

confidence: 52%

Section: Resultsmentioning

confidence: 92%

A New Method of Separating Ovomucin from Egg White

Omana

2009

J. Agric. Food Chem.

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“…Ovomucin can be extracted and purified from egg white by isoelectric precipitation (IEP) ( − ) as well as by gel filtration ( − ). Although many studies have been conducted to elucidate the physical and chemical properties of ovomucin, ovomucin is still in many ways ill-defined.…”

Section: Introductionmentioning

confidence: 99%

Comparison of Different Egg Albumen Fractions as Sources of Ovomucin

Hiidenhovi

Mäkinen

Huopalahti

et al. 2002

J. Agric. Food Chem.

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Ovomucin was fractionated from whole egg albumen, thick egg albumen, liquid egg albumen, and a liquid egg albumen filtration byproduct by using the isoelectric precipitation method. The amounts of ovomucin measured in the above-mentioned fractions were 280, 340, 500, and 520 mg per 100 g of albumen, respectively. There was great variation between the beta-ovomucin contents of the different albumen fractions. Whole egg albumen contained about 25 mg of beta-ovomucin in 100 g of albumen, whereas thick egg albumen, liquid egg albumen, and the filtration byproduct contained about 1.5, 3, and 5 times more beta-ovomucin, respectively, as compared to whole egg albumen. The results indicate that both the liquid egg albumen fraction and especially the filtration byproduct fraction appear to be potential sources of ovomucin when it is used as an ingredient for functional foods.

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Ovomucin

Hiidenhovi

2007

Bioactive Egg Compounds

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Solubilization and Characterization of Ovomucin without Chemical Modification

Cited by 5 publications

References 2 publications

A New Method of Separating Ovomucin from Egg White

A New Method of Separating Ovomucin from Egg White

Comparison of Different Egg Albumen Fractions as Sources of Ovomucin

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