• Journal of Animal Science and Technology
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• v.51 no.6
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• pp.521-526
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• 2009

Irradiation of egg white increased foaming ability significantly. To investigate the protein modification by irradiation responsible for the increase of foaming ability, 3 major egg white proteins were purchased and mixed (7.7 g/L ovalbumin, 1.8 g/L ovotransferrin, 0.5 g/L lysozyme) as a model system and irradiated at 0, 2.5, and 5 kGy. The different protein expressions were evaluated using 2-D electrophoresis and it was found that ovotransferrin was cleaved by irradiation and molecular weight and isoelectric point were changed. In addition, many uncharacterized proteins were found and it indicated that irradiation modified proteins randomly but mainly fragmentation was observed. Therefore, it can be concluded that protein fragmentation of 3 major egg white proteins responsible for foaming ability may be the main reason for the improvement of foaming ability.

• Food Science of Animal Resources
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• v.30 no.1
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• pp.36-41
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• 2010

The Hen's egg is widely used in many processed foods as an ingredient and is one of the most prevalent food allergens in children. To detect egg proteins in processed foods, we developed a competitive indirect enzyme-linked immunosorbent assay (ciELISA) using an anti-ovomucoid (OM) antibody, which was produced by immunization of rabbits with OM, the most heat-stable component of the egg proteins. The detection limit of this quantitative assay system was 30 ng/mL. Cross-reactivity of the anti-OM antibody toward OM, ovalbumin, skim milk, casein, whey protein isolate, and isolated soy protein was 100, 0.4, 0.2, 0.04, 0, and 0%, respectively. In the spike test of egg white powder in milk replacer, commercial sausage, and in-house sausage, the assay recoveries ($mean{\pm}SD$) were $129{\pm}13.7%$, $73.9{\pm}12.5%$, and $65.5{\pm}13.6%$, respectively. When egg white in a commercial crab meat analog and sausage was determined by ciELISA, the assay recovery was found to be 108% and 127%, respectively. The combined results of this study indicate that this novel ciELISA for OM detection could be applied for the quantification of hen's egg proteins in processed foods.

• Korean Chemical Engineering Research
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• v.50 no.4
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• pp.713-717
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• 2012

Approximately forty proteins in egg white have been widely studied for their functional properties. To develop a procedure of separation for pure and non-altered proteins from egg white, purification study was conducted to isolate lysozyme, ovotransferrin, and ovalbumin. Ion exchange cartridge can selectively separate proteins from egg white, and reversed-phase HPLC (RP-HPLC) could identify separated proteins. Proteins in egg white were purified by HI trap ion exchange cartridge SP and Q with buffers pH 8.0 and 5.2. C18 column (Phenomenex, USA) was used for RP-HPLC analysis and isocratic mobile phase was used with acetonitrile (ACN)/distilled water (DW)/trifluoroacetic acid (TFA) in the ratio of 50/50/0.1. Comparing the retention times of standards in RP-HPLC experiments showed that ovotransferrin, ovalbumin, and lysozyme in egg white were eluted successively in the RP-HPLC column after the pretreatment in SP and Q ion exchange cartridges.

• Food Science of Animal Resources
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• v.33 no.4
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• pp.501-507
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• 2013

Lysozyme was trapped from $2{\times}$ diluted egg white using Amberlite FPC 3500 ion exchange resin (1 g/10mL of egg white). The lysozyme bound to the resin was recovered using 0.1 N glycine-NaOH buffers, pH 9.0, containing 0.5 M NaCl. After separating lysozyme, the pH of the egg white solution was adjusted to 4.75 and centrifuged to remove interfering proteins. The supernatant was collected, added with 2.5% citric acid and 5.0% ammonium sulfate combination to precipitate egg white proteins, except for ovalbumin. After centrifugation, both supernatant (S1) and precipitant were collected. The precipitant was dissolved with 4 volumes of distilled water, and then 2.0% ammonium sulfate and 1.5% citric acid combinations added, stirred overnight in a cold room, and centrifuged. The resulting supernatant (S2) was pooled with the first supernatant (S1), desalted using an ultrafiltration unit, heat-treated at $70^{\circ}C$ for 15 min, and then centrifuged. The supernatant was collected as an ovalbumin fraction and lyophilized. The separated proteins were confirmed using Western blotting. The yield of lysozyme and ovalbumin was > 88.9% and > 97.7%, respectively, and the purity of lysozyme and ovalbumin was > 97% and 87%, respectively. The results indicated that the protocol was simple, and separated lysozyme and ovalbumin effectively.

• KSBB Journal
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• v.22 no.2
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• pp.119-122
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• 2007

Since egg white contains various protein, it is important to research the protein distribution of egg white. Specially, lysozyme and ovalbumin important proteins, are used in medicine and food industry. Reversed phase high performance liquid chromatography has been used for separation of egg white, and column of RP-HPLC is available in variety. We have used C4, C8 and C18 columns to obtain chromatograms by varying carbon chain length of stationary phase. Long carbon chain length of stationary phase has good separation of egg white. Also, we have changed the composition of mobile phase (acetonitrile, water, and trifluoroacetic acid) to find optimum chromatograms. Acetonitrile and water composition of 50 : 50 show many peaks from egg white. Isocartic and gradient elution in RP-HPLC were used to compare the chromatography of egg white.

• Korean Journal of Poultry Science
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• v.49 no.4
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• pp.221-228
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• 2022

Major egg white proteins and their hydrolysates serve as functional food ingredients that have certain metal-chelating properties. Employing egg white proteins and their hydrolysates to scavenge dietary oxalates is anticipated to have beneficial effect in the prevention of kidney stones. The objective of this study was to determine the biogenic oxalate-chelating activity of ovalbumin, ovomucin, and ovotransferrin and their hydrolysates. To prepare oxalate extracts, 30 mL of 0.25 N HCl was added to separately to 0.5 g of dried spinach and starfruit powders followed by boiling for 15 min, and after cooling, the addition of a further 20 mL of 0.25 N HCl. Having prepared these extracts, ovalbumin, ovomucin, and ovotransferrin and their hydrolysates were separately mixed with oxalate extracts and incubated at 3℃ for 24 h. Following centrifugation, supernatants were analyzed by HPLC using a reverse-phase C18 column coupled with a diode array detector. We found that all assessed proteins and their hydrolysates showed biogenic oxalate-chelating activity against the oxalates of spinach. In contrast, however, only ovalbumin, ovalbumin-hydrolysate, and ovomucin showed chelating activity (57.10%±8.84%, 85.44%±5.30%, 73.20%±4.13%, respectively) against the oxalates of starfruit (P<0.05). Overall, hydrolyzed ovalbumin was identified as the most effective chelator of the oxalates both spinach and starfruit. In this study, we thus established that the assessed egg white proteins and their hydrolysates have oxalate-chelating activity in vitro, thereby indicating that these compounds have potential utility as nutraceuticals for the chelation of dietary oxalate. However, further research will be necessary to verify their oxalate-chelating activities against different fruits and vegetables and under specific in vivo conditions and against purified oxalate.

• Food Science and Biotechnology
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• v.15 no.3
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• pp.418-423
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• 2006

Egg white powders (EWPs) were produced after pH adjustment (PH 6-9) of fresh egg white, followed by spray-drying, and foaming and gelling properties of EWPs were examined. EWP produced after pH adjustment to 6.5 (EWP-6.5) resulted in significantly higher foaming ability and gel hardness than control and other pH-adjusted EWP. Significant increases in surface -SH content and surface hydrophobicity of EWP-6.5 coincided with improved foaming ability and gel hardness. Significantly higher consistency index for reconstituted EWP-6.5 indicates unfolding of egg white protein was substantially increased in EWP-6.5. Decreased a-helix content in EWP-6.5 was confirmed by circular dichroism spectral analysis. These results indicate pH adjustment prior to spray-drying leads to structural changes in egg white proteins, significantly affecting major functionalities of EWP.

• Journal of Microbiology and Biotechnology
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• v.9 no.3
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• pp.292-296
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• 1999

The high density mixed mode adsorbent known by the trade name of Mimo-AD was used to purify lysozyme directly from the hen egg white (HEW). The homogenized hen egg white was treated with the adsorbent in a stirred vessel for lysozyme adsorption, and then the adsorbent, easily separated from the HEW by sedimentation, was packed into a column. The remaining HEW and contaminant proteins were removed by washing with pH 11 distilled water in an expanded-bed state, and subsequently the elution was performed with pH 12 distilled water in a packed-bed state. By this simple and rapid adsorption, washing, and elution procedure, lysozyme was purified to＞95％ with an overall recovery yield of 66％. This process offers a great potential for industrial application by allowing the extraction of lysozyme while retaining the commercial value of HEW.

• Proceedings of the Acoustical Society of Korea Conference
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• 1998.06d
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• pp.29-34
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• 1998

Egg white의 gel화에 따른 음속과 흡수의 변화가 60와 75$^{\circ}C$에서 크게 나타난 것이 egg white의 어느 단백질 성분에 의한 것인가를 조사하기 위해 egg white의 주요한 단백질 성분인 obalbumin, conalbumin, ovomucoid protein에 대해 gel화에 따른 음속 및 흡수의 변화를 온도 10-95$^{\circ}C$의 범위에서 초음파pulse법을 사용하여 측정하였다. Ovalbumin는 7$0^{\circ}C$, conalbumin는 5$0^{\circ}C$에서 gel화가 시작되었고 ovomucoid는 측정온도범위내에서는 gel화가 진행되지 않았다. Gel화하는 이상의 온도에서 음속과 흡수에 대하여 aging측정을 행하여 gel화에 의한 dam속과 흡수의 변화를 관측하였다. 그 결과 conalbumin는 5$0^{\circ}C$, ovalbumin는 75$^{\circ}C$에서 음속과 흡수의변화가 많이 일어났다. Egg white의 60와 75$^{\circ}C$의 gel화에 의한 음속과 흡수의 큰 변화는 각각 conalbumin과 ovalbumin에 의한 것임을 알았고 Conalbumin과 ovalbumin는 aging 온도를 parameter로하여 이력현상이 관측되었다.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.6
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• pp.881-890
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• 2019

Objective: A study was conducted to develop non-dairy creamer analogs/mimics using egg white, egg yolk, soy protein and their combinations, and their nutrient content, shelf-life and flavor acceptability were compared. Methods: Spray dried egg white, egg yolk, and soy protein isolate were purchased from manufacturers and used for the formulae. Results: The protein contents of the non-dairy creamer analogs/mimics were about 8.5% as calculated. The amounts of oleic and linoleic acid content increased as the amount of yolk increased in the formula, but the increases of polyunsaturated fatty acids were <0.5% of total fat. Addition of egg yolk to the formula increased choline and lutein content in the products, but the amounts were <0.4 mg/g for choline and $4{\mu}g/g$ for lutein. The lutein in the products continued to decrease over the storage time, and only about 15% to 20% of the 0-month amounts were left after 3 months of storage. Although the thiobarbituric acid reactive substances values of the spray-dried non-dairy creamer analogs/mimics increased as storage time increased, the values were still low. Yellowness, darkness, and egg flavor/odor of the non-dairy creamer analogs/mimics increased as the amount of egg yolk in the formula increased. The overall acceptability of the non-dairy creamer analogs/mimics was closely related to the intensity of egg flavor/odor, but storage improved their overall acceptance because most of the off-odor volatiles disappeared during the storage. Water temperature was the most important parameter in dissolving spray-dried non-dairy creamer analogs/mimics, and $55^{\circ}C$ to $75^{\circ}C$ was the optimal water temperature conditions to dissolve them. Conclusion: Higher amounts of yolk and soy protein combinations in place of egg white reduced the cost of the products significantly and those products contained better and balanced nutrients than the commercial coffee creamers. However, off-flavor and solubility were two important issues in the products.