• Journal of Animal Science and Technology
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• 제51권6호
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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.

• 한국축산식품학회지
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• 제30권1호
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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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• 제50권4호
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• pp.713-717
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• 2012

난백에 있는 40여 가지의 단백질의 기능적 특성에 대한 연구가 폭 넓게 진행되고 있지만, 그 특성이 모두 확인되지 않았다. 난백에서 순수하면서 변성되지 않은 단백질을 분리하는 방법을 연구하기 위해 본 연구에서는 난백 중 함량이 많은 lysozyme, ovotransferrin, ovalbumin을 분리했다. 난백에서 단백질을 다른 분리 방법보다 선택적으로 분리가 가능한 이온 교환 크로마토그래피를 이용했다. 그리고 분리된 단백질을 동정하기 위해서 Reversed-phase HPLC (RP-HPLC)를 사용했다. 이온 교환 크로마토그래피에서 HI Trap ion exchange cartridge (GE Healthcare, USA)를 사용했고, 그 중에서 양이온 교환 수지 SP (완충용액 pH 8.0, pH 5.2)와 음이온 교환 수지 Q (완충용액 pH 8.0)로 난백 단백질을 분리하였다. 분리한 난백 단백질들의 동정용 RP-HPLC에서는 C18 컬럼(Phenomenex, USA)을 사용했고 등용매 용리에서 이동상으로 acetonitrile (ACN)/distilled water (DW)/trifluoroacetic acid (TFA)의 부피비를 50/50/0.1로 사용했다. 이온 교환 크로마토그래피에 의해 각 단계에서 분리된 용출용액을 RP-HPLC으로 분석한 크로마토그램과 표준시료의 크로마토그램의 체류시간을 비교하여 난백에 포함된 ovotransferrin, ovalbumin, lysozyme이 순차적으로 용출됨을 알았다.

• 한국축산식품학회지
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• 제33권4호
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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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• 제22권2호
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• pp.119-122
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• 2007

RP-HPLC에서 주요 변수인 이동상의 조성과 컬럼의 종류를 변화시켜 난백 단백질을 실험하였다. C4, C8 C18 컬럼을 비교 실험하여 C18 컬럼에서 가장 많은 피크를 보여 C18 컬럼을 선택하였다. 등용매 용리에서 ACN : water의 조성이 50 : 50에서 가장 많은 피크를 보여 이 결과를 토대로 기울기 용리를 하여 실험하였다. 기울기 용리에서 얻어진 4가지 피크를 확인하기 위하여 단일성분인 lysozyme와 ovalbumin의 체류시간을 측정하여 확인하였고 논문을 통해 2가지 피크를 예측할 수 있었다.

• 한국가금학회지
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• 제49권4호
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• pp.221-228
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• 2022

주요 계란 난백 단백질과 그 가수분해물은 일부 금속 킬레이트 특성을 갖는 기능성 식품 성분으로 알려져 있다. 식이 oxalate를 제거하기 위해 계란 난백 단백질과 그 가수분해물을 이용할 경우 신장 결석을 예방하는데 도움이 될 것이다. 본 연구의 목적은 계란 난백 단백질인 ovalbumin, ovomucin, ovotransferrin과 이 단백질들의 효소처리를 통해 얻은 가수분해물의 biogenic oxalate chelating 활성을 측정하는 것이었다. 채소 중에서 시금치를 과일 중에서 스타푸르트(starfruit)를 선택하여 HCl처리를 거쳐 옥살레이트 추출물(oxalates extract)을 제조하였다. 계란의 난백 단백질 중, ovalbumin, ovomucin, ovotransferrin를 선택하여 이들의 가수분해물과 함께 옥살레이트 추출물과 별도로 혼합하여 3℃에서 24시간 반응을 위한 배양을 시켰다. 원심분리 후 상등액을 HPLC로 분석하여 단백질과 가수분해물의 biogenic oxalate chelating 활성을 비교 분석하였다. 사용된 모든 계란 난백 단백질과 그 가수분해물은 시금치의 oxalates에 대한 biogenic oxalate chelating 활성을 보였다. 그러나열대과일인 starfruit의 oxalates에 대한 킬레이트 활성에서는ovalbumin, hydrolyzed ovalbumin, ovomucin만이 활성을 보였다. 전반적으로, hydrolyzed ovalbumin은 시금치와 스타프루트 모두에서 oxalates chelating 효과가 가장 좋았다. 따라서 계란의 난백 단백질과 그 가수분해물의 옥살산 킬레이트 활성이 있었으며, 식이 옥살산에 대한 영양 개선을 위한 소재로 개발 가능성이 있다. 그러나, 다른 과일과 야채에 대한 옥살레이트 킬레이트 활성과 특정 생체 내 조건에서의 계란 단백질의 옥살레이트 킬레이팅 효과를 검증하기 위한 추가 연구가 필요하다.

• Food Science and Biotechnology
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• 제15권3호
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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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• 제9권3호
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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.

• 한국음향학회:학술대회논문집
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• 한국음향학회 1998년도 학술발표대회 논문집 제5권
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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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• 제32권6호
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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.