• 생명과학회지
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• 제5권2호
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• pp.57-62
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• 1995

Casein or soybean protein was subjected to there action with caffeic acidtyrosinase system at 30-35$\circ$C, pH 6.8 with aeration for 5hr. The resulting brown proteins were washed with acetone until the washings were on longer colored. However, modified protein still retained a light brown. The effects of the modified proteins and brown compounds on male Wistar strain rats were studied by pair-feeding of a cholesterol-free diet for 14days. Significant decrease in protein digestibility for the rats fed with the modified proteins were observed. Weight gain and protein digestibility were not influenced by feeding brown compounds, but the feeding of brown compound from casein caused an enlargement of caecum. The concentrations of serum cholesterol and triglyceride in the rats fed with modified proteins and brown compounds were mostly unchanged against the rats fed with untreated proteins. These results suggest that the decrease in protein digestibility induced by enzymic browning-reaction did not cause the decrease in concentration of serum cholesterol.

• 생명과학회지
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• 제5권2호
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• pp.1-1
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• 1995

Casein or soybean protein was subjected to there action with caffeic acidtyrosinase system at 30-35$\circ$C, pH 6.8 with aeration for 5hr. The resulting brown proteins were washed with acetone until the washings were on longer colored. However, modified protein still retained a light brown. The effects of the modified proteins and brown compounds on male Wistar strain rats were studied by pair-feeding of a cholesterol-free diet for 14days. Significant decrease in protein digestibility for the rats fed with the modified proteins were observed. Weight gain and protein digestibility were not influenced by feeding brown compounds, but the feeding of brown compound from casein caused an enlargement of caecum. The concentrations of serum cholesterol and triglyceride in the rats fed with modified proteins and brown compounds were mostly unchanged against the rats fed with untreated proteins. These results suggest that the decrease in protein digestibility induced by enzymic browning-reaction did not cause the decrease in concentration of serum cholesterol.

• Applied Biological Chemistry
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• 제37권5호
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• pp.379-384
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• 1994

카제인, 대두 단백질에 caffeic acid와 tyrosinase를 첨가한 후 온도 $30{\sim}35^{\circ}C$, pH 6.8에서 5시간 반응시켜 갈변단백질을 조제하였다. 이러한 갈변단백질 및 무처리 카제인, 대두단백질을 단백질 수준 20.0% 되도록 콜레스테롤 무첨가 사료에 혼합, 7주령의 Wistar계 흰쥐 수컷에 14일간 급여하였다. 갈변단백질의 아미노산 cystine의 손실이 눈에 띄는 것 이외 아미노산 손실은 인정되지 않았다. 단백질 소화율은 갈변에 의하여 저하되고, 갈변 카제인의 경우는 현저한 맹장의 비대가 인정되었다. 혈청 총콜레스테롤, LDL-콜레스테롤, 트리글리세라이드 농도는 갈변에 의해 유의차는 인정되지 않았으나, 상승하는 경향이었다. 단백질은 효소적 갈변에 의해 단백질 소화율이 저하되고, 그로 인한 분량(糞量)도 증가하지만, 혈청지질의 저하작용은 없었다.

• Journal of the Korean Wood Science and Technology
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• 제39권1호
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• pp.21-27
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• 2011

This study was carried out to examine properties of water resistant plywood by using serum protein adhesive which is natural, environment-friendly and human-friendly. For the preparation of the serum protein adhesive, pig blood from slaughterhouse was centrifuged and serum was separated from corpuscles and concentrated to 30% by dry weight basis. This concentrated serum protein was modified with PF resin (50% NVC) with the ratio of 9 : 2.5. Plywood made by this modified serum protein gave 1.21 N/$mm^2$ of dry bonding strength, 0.80 N/$mm^2$ of wet boil bonding strength, 0% of cyclic delamination test value, and 0.025 ppm of HCHO emission, which met the excellent super $E_0$ grade and water resistant plywood.

• 한국식생활문화학회지
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• 제14권5호
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• pp.467-476
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• 1999

We studied to improve the functional properties of soybean protein isolate by dimethylglutarylation and acetylation. Soybean protein isolate was acylated rapidly up to 80% modification and more of 80% modification was proceed slowly. Electrophoretic analysis showed that more changes in modified protein. Also, modification of soybean protein produced more ionizable tyrosines and exposed more hydrophobic groups, while modified protein exhibited a loss of reactive sulfhydryl groups. Spectrophoretic studies demonstrated that the shift was occurred at the UV 278nm and fluorescence 333nm, respectively, and the intensity decreased as the degree of modification was increased.

• 한국환경보건학회지
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• 제30권4호
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• pp.314-319
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• 2004

Glycinin of more than $97\%$ purity was modified using maleic anhydride. Glycinin samples of $0\%,\;65\%,\;and\;95\%$ lysine residue modifications were used to determine the changes in turbidimetric characteristics of the protein due to maleylation. The solubility behavior of the protein as a function of pH was changed with maleylation. The isoelectric point of $65\%\;and\;95\%$ modified glycinin shifted to pH 4.0 and pH 3.5-4.0, respectively, as compared to pH 4.6 for native glycinin. Maleylated glycinins exhibited increased solubility at pH above 4.6. Turbidity of native glycinin decreased substantially by the addition of NaCl, but the stabilizing effect of NaCl decreased when the protein was chemically modified. The effect of NaCl on $65\%$ modified glycinin was intermediate between native glycinin and $95\%$ modified sample. Thermal aggregation of native glycinin was completed within 5 min of heating at $80^{\circ}C$. Maleylation contributed significantly to the thermostability of the protein at pH of 7.0 and 9.0, exhibiting little turbidity. Addition of NaCl suppressed thermal aggregation of native glycinin, but turbidity actually increased for the samples of $65\%\;and\;95\%$ modification.

• 한국콘텐츠학회논문지
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• 제9권5호
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• pp.332-336
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• 2009

유전체 분석에서 중요한 부분 중 하나는 기능이 알려지지 않은 미지 단백질에 대한 기능 예측이다. 단백질-단백질 상호작용 네트워크를 분석하는 것은 미지 단백질에 대한 기능을 보다 쉽게 예측할 수 있게 한다. 단백질-단백질 상호작용 네트워크로부터 미지 단백질의 기능을 예측하기 위한 다양한 연구들이 시도되어 왔다. 카이-제곱(Chi-square) 방식은 단백질-단백질 상호작용 네트워크를 통해 기능을 예측하고자 하는 연구 중 대표적인 방식이다. 하지만 카이-제곱 방식은 네트워크의 토폴로지를 반영하지 않아 네트워크 크기에 따라 예측의 정확성이 떨어지는 문제점이 있다. 따라서 본 논문에서는 카이-제곱 방식을 보완하여 정확성을 높인 새로운 기능 예측 방법을 제안한다 이를 위해 MIPS, DIP 그리고 SGD와 같은 공개된 단백질 상호작용 데이터베이스들로부터 데이터를 수집하여 분석하였다. 그리고 제안된 방식의 우수성을 입증하기 위해 각 데이터베이스들에 대해 카이-제곱방식과 제안하는 보완된 카이-제곱(Modified Chi-square)방식으로 예측해보고 이들의 정확성을 평가하였다.

• Food Science and Biotechnology
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• 제15권3호
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• pp.385-391
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• 2006

In Korea, different kinds of genetically modified (GM) crops are under development, including GM-rice expressing insecticidal crystal (Cry) proteins of Bacillus thuringiensis (Bt) modified to change a single amino acid. In this study, amino acid (aa) sequences of modified Cry proteins were compared to that of known allergens, and Cry proteins expressed in GM-rice were identified by using Cry protein specific polyclonal antibody. The antigen-antibody reactions were compared between GM and commercial rice to assess the allergic risk of Cry proteins. This analysis showed no known allergen to have more than 35% aa sequence homology with modified Cry proteins in Bt rice over an 80 aa window or to have more than 8 consecutive identical aa. Sera from allergic patients showed some IgE reactivity via immunoblotting and enzyme-linked immunosorbent assay (ELISA), although no differences were seen between GM and commercial rice. Based on these results we conclude that GM rice with modified Cry proteins has no differences in its protein composition or allergenicity relative to commercial rice.

• Journal of Applied Biological Chemistry
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• 제42권4호
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• pp.180-185
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• 1999

Protein concentrate was produced and succinylated from rice bran to assess and improve its functional properties for the purpose of expanding the uses of rice bran proteins. The most effective solvent for the extraction of rice bran proteins was 20% aqueous ethanol at pH 9. The protein content of rice bran protein concentrate produced was 70.0% and the total protein yield was 64.3%. The extent of succinylation of free amino groups in the modified products was 72.8%. Though the modified protein products showed good functional properties including solubility, emulsion properties, and oil absorption capacity, it did not form gel. Succinylation improved solubility and emulsion and gelling properties. These improvements in functionality will enhance the value of rice bran proteins, thus enabling them to be more competitive with other food proteins.

• BMB Reports
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• 제46권10호
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• pp.495-500
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• 2013

Turnip yellow mosaic virus (TYMV) is a positive strand RNA virus. We have modified TYMV coat protein (CP) by inserting a c-Myc epitope peptide at the N- or C-terminus of the CP, and have examined its effect on assembly. We introduced the recombinant CP constructs into Nicotiana benthamiana leaves by agroinfiltration. Examination of the leaf extracts by agarose gel electrophoresis and Western blot analysis showed that the CP modified at the N-terminus produced a band co-migrating with wild-type virions. With C-terminal modification, however, the detected bands moved faster than the wild-type virions. To further examine the effect, TYMV constructs producing the modified CPs were prepared. With N-terminal modification, viral RNAs were protected from RNase A. In contrast, the viral RNAs were not protected with C-terminal modification. Overall, the results suggest that virion assembly and RNA packaging occur properly when the N-terminus of CP is modified, but not when the C-terminus is modified.