• Preventive Nutrition and Food Science
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• 제2권1호
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• pp.17-22
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• 1997

Casein was chemically modified with acetic, succinic, and maleic anhydride and changes in functional pro-perties were evaluated as affected by the degree of modification. Chemical modification resulted in casein with unique functional properties depending upon the type of anhydrid used and the degree of modification. It was possible to control heat coagulation, calcium precipitability, forming and emulsion capacity and stability. At pH 4.5 heat coagulation was 0% in the case 74.1% acetylated casein; on the contrary, succinylation and maleyation resulted in highly heat sensitive protein. Foaming properties were improved markedly by suc-cinylation and maleylation at pH 4.5. However, emulsifying properties were enhanced only by maleylation.

• KSBB Journal
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• 제5권2호
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• pp.141-149
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• 1990

Aspergillus niger유래의 $\beta$-glucosidase를 (1)glutarald-ehyde를 가교제로 한 chitin과 chitosan담체에 covalent linkage (2)Amberite IRA93과 DEAE-cellulose담체에 succinylation시킨 후 흡착, 그리고 (3)alginarte, polyacry-lamide를 각종 가교제를 이용 entrapment등의 방법으로 고정화 하였다. Glutaraldehyde를 가교제로써 chitosan을 활성화시킨후 $\beta$-glucosidase를 고정화 시켰을때 효소활성 회수율이 31.5%로 가장 높았고, 또한 column형 반응기에서의 15일 경과 후 효소활성 유지도도 69%로서 가장 우수하였다. 또한 succinylation시킨 효소를 Amberite IRA93 담체에 흡착시켰을 때 효소활성 회수율은 24.7%였고 효소 활성유지도는 62%였다. 반면에 entra-pment 방법에 의한 $\beta$-glucosidase의 고정화는 효소의 계속적인 용출로 $\beta$-glucosidase의 고정화에는 적합하지 않았다. Chitosan담체에서의 고정화 최적조건을 조사한 결과 가교제인 glutaraldehyde의 최적농도는 0.4%였고, glutaraldehyde의 최적 반응 pH는 4.8이었다. 또한 column형 반응기를 이용하여 cellobiose로부터 glucose로의 전환율을 조사하여 고정화 효소의 효용성을 검토하였다.

• Applied Biological Chemistry
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• 제38권5호
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• pp.393-397
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• 1995

어류껍질 젤라틴의 탄닌산과의 반응성을 개선하여 청정제 및 chewing gum base 등으로 유효 이용할 목적으로 각시가자미껍질 젤라틴의 숙시닐화를 시도하여 탄닌산과의 반응특성에 대하여 검토하였다. 각시가자미껍질 젤라틴의 숙시닐화는 succinic anhydride의 농도가 10%까지는 직선적으로 증가하였고, 그 이상의 농도에서는 거의 변화가 없었다. 본 실험에서는 젤라틴에 대하여 15%에 해당하는 succinic anhydride로 숙시닐화시켜 탄닌산과의 반응성을 살펴 보았고, 이 젤라틴의 숙시닐화 정도는 약 80%이었다. 등전점은 숙시닐화 어류껍질 젤라틴의 경우 4.08로 대조 어류껍질 젤라틴의 5.54에 비하여 감소하였고, 일반성분 및 아미노산 조성은 두 젤라틴이 유사하였다. 용액의 pH가 숙시닐화 어류점질 젤라틴의 경우 4.0부근에서, 대조 어류껍질 젤라틴의 경우 4.8 부근에서 젤라틴 및 탄닌산의 침전율이 최대이었다. 젤라틴 농도는 젤라틴 침전율의 경우 숙시닐화에 관계없이 농도가 증가할수록 감소하였고, 탄닌산의 침전율의 경우 탄닌산에 대하여 숙시닐화 젤라틴은 $2{\sim}4$배, 대조 젤라틴은 $2{\sim}3$배로 첨가한 것이 최대이었다. 젤라틴 및 탄닌산의 침전율은 에탄올의 존재에 의해서는 영향을 받았으나, sucrose의 존재에 의해서는 거의 영향을 받지 않았다.

• 대한가정학회지
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• 제28권4호
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• pp.41-50
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• 1990

Soy protein was isolated from Korean soy bean 'Chang ryub' and chemically modified with succinic anhydride. Functionality of the soy protein isolate(SPI), succinylated SPI(SPPI), and PP590(commercial) at various pH were investigated. The mechanical and sensory properties of soy bean curds made from several mixing ratio of succinylated soy bean milk were observed. The solubility of SPI significantly increased with succinylation. The solubility of PP590 was lower than that of SSPI. The solubility of SPPI increased significantly in 0.03M CaCl2 solution. The emulsifying activity of SSPI increased. On the range of pH above pI the emulsifying activity of PP590 was higher than that of SPI. There was no difference in emulsion stability among the groups. The foam expansion capacity of SPPI increased at higher pH than pI but the foam stability decreased significantly above pH 9. Mechanical texture profile analysis revealed the modified soy bean curds had the lower hardniss, chewiness and cohesiveness with increased modification. The mechanical characteristics of modified soy bean curds revealed generalized Maxwell Model of 7-elements or 5-elements. In sensory evaluation, the hardness, the springiness and acceptability of modified soy bean curds were lower significantly than those of control soy bean curd.

• 한국식품과학회지
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• 제25권3호
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• pp.277-281
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• 1993

콜로이드 식품에서의 단백질의 구조적 안정성을 연구하기 위하여 7개의 BSA structural intermediates, succinylated ${\beta}-lactoglobulin$을 만든 후 CD, 이황화물 결합함량, hydrodynamic radius 등을 측정하여 그 구조적 특성을 규명했다. Refolding time이 길수록 BSA intermediates들은 native BSA 구조에 근접하는 것을 나타냈고 succinylation은 ${\beta}-lactoglobulin$의 순 음전하를 변화시켜 보다 aperiodic structure를 갖게하였다. Perchlorate 존재하 ${\beta}-casein$의 구조는 소수성 상호작용에 크게 영향 받는 것으로 나타났다.

• 한국식품조리과학회지
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• 제7권2호
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• pp.97-104
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• 1991

This study was carried out in order to study the protein functionality such as foaming and emulsifying properties by succinylation of peanut protein isolates. Succinylated and unsuccinylated peanut protein isolate was tested for to find out the effect of pH, heat treatment and sodium chloride concentration on the solubility, foam expansion, foam stability, emulsion capacity and emulsion stability. The results are summarized as follows; 1. Succinylation enhanced the solubility of peanut protein isotate (PPI). The solubility of succinylated PPI markedly increased at pH 4.5. When the protein solutions was heated, the solubility of succinylated PPI greatly increased than PPI at pH 3. With addition of NaCl, solubility of succinylated PPI increased at pH 7 and pH 9. 2. The foam expansion of PPI and succinylated PPI on pH was no difference between both proteins. Addition of NaCl and heat treatment caused steeply increased in foam expansion at pH 3. 3. The foam stability of PPI and succinylated PPI showed the lowest value at pH 4.5. When PPI and succinylated PPI was heated, foam stability of two proteins incensed at pH 3 and showed similar aspects between PPI and succinylated PPI. However, at pH 9 stability of succinylated PPI decreased by heat treatment over $60^{\circ}C$. 4. Emulsion capacity of succinylated PPI on pH was markedly increased and showed the highest value at pH 11. At pH 4.5 which is isoelectric point of PPI, emulsion capacity of PPI by succinylation improved than that of PPI. When succinylated PPI was heated, emulsion capacity was greatly increased at pH 2 and pH 7. With NaCl was added, emulsion capacity of succinylated PPI increased than that of PPI. 5. Emulsion stability of PPI and succinylated PPI was affected by pH and showed its highest value at pH 11. At pH 4.5, emulsion stability of succinylated PPI increased than that of PPI. Addition of NaCl and heat treatment caused slightly increased in emulsion stability of succinylated PPI.

• 한국식품영양과학회지
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• 제18권4호
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• pp.410-422
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• 1989

숙시닐화 또는 트립신처리에 의한 대두단백질분리물의 화학적 변형은 단백질의 함량을 감소시키는 것으로 나타났고, 아미노산 조성에서 tyrosine의 증가가 현저하였으나 lysine은 트립신처리시에만 크게 증가하였다. 화학적 변형은 단백질의 용해성을 증가시키고 pH의존성이 뚜렷하여 등전점 변이시키는 효과를 나타내었다. 단백질의 용해성은 염류의 농도증가에 의해 감소하는 경향을 나타내었으며, 화학적 변형은 유흡수성과 수분흡수성, 유화특성 및 기포성 등을 증가시키는 반면에 기포안정성을 다소 저하시키고 자외선흡광도와 용적밀도를 감소시켰다. 한편 대두단백질 분리물과 우육단백질의 혼합에 따른 상호작용에 의해서는 유화활성, 유화활성지수 및 기포성의 증가를 가져봤으나 유화안정성에 대해서는 현저한 효과가 나타나지 않았다.

• 한국식품과학회지
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• 제12권4호
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• pp.263-271
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• 1980

피마자박 단백질을 사료 또는 식품화 하기 위하여 탈지 피마자박으로부터 독성분이 완전하게 제거된 단백질을 만들었다. 이 피마자 단백질의 용해도는 ${\varepsilon}$-아미노기의 숙시닐화 및 아세틸화로 $pH\;7{\sim}8$에서 현저하게 증가하였다. 아미노산 분석결과, 황-함유 아미노산과 L-리신이 제한 아미노산이었고, 아실화 과정은 아미노산 함량에 약간의 손실을 주었다. 파파인을 이용한 1 단계법 plastein 반응으로 피마자 단백질 또는 아실화 피마자 단백질과 DL-메티오닌 에틸 에스테르로부터 L-메티오닌 강화 피마자 단백질을 합성하였고, 이 방법으로 L-메티오닌 도입율은 50%였다. 피마자 단백질 및 수식된 피마자 단백질의 펩신에 의한 소화율은 모두 92% 정도였으나, 트립신에 의한 소화율은 숙시닐화 및 아세틸화 단백질이 현저하게 떨어져서 각각 42% 및 26%였다. 피마자 단백질의 단백질 효율은 L-메티오닌 강화로 카제인의 단백질 효율의 90%까지 향상되었으나, 피마자 단백질을 숙시닐화 및 아세틸화 하면 단백질 효율은 감소되어, 각각 카제인의 55% 및 69%였다.

• Toxicological Research
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• 제29권2호
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• pp.81-86
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• 2013

Toxicoproteomics integrates the proteomic knowledge into toxicology by enabling protein quantification in biofluids and tissues, thus taking toxicological research to the next level. Post-translational modification (PTM) alters the three-dimensional (3D) structure of proteins by covalently binding small molecules to them and therefore represents a major protein function diversification mechanism. Because of the crucial roles PTM plays in biological systems, the identification of novel PTMs and study of the role of PTMs are gaining much attention in proteomics research. Of the 300 known PTMs, protein acylation, including lysine formylation, acetylation, propionylation, butyrylation, malonylation, succinylation, and crotonylation, regulates the crucial functions of many eukaryotic proteins involved in cellular metabolism, cell cycle, aging, growth, angiogenesis, and cancer. Here, I reviewed recent studies regarding novel types of lysine acylation, their biological functions, and their applicationsin toxicoproteomics research.

• Journal of Applied Biological Chemistry
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• 제42권3호
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• pp.125-129
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• 1999

The changes in gel characteristics of soy protein and succinylated soy protein due to various specific interaction-altering reagents which affect the formation and textural properties of gels, were studied. The reagents were added to 15% soy protein solutions prior to heat treatment. Succinylated soy protein formed harder gel without the addition of reagents. Hardly no gels were formed with urea, indicating that hydrogen bonds significantly contributed to the formation and hardness of the gel and the effects of urea on the hardness of succinylated soy protein gel were more significant. Disulfide bonds were important in the formation of hard gels whether they were succinylated or not, but the contributions of hydrophobic interactions to gel hardness were relatively insignificant. The hardness reducing effects of NaCl and NaSCN were more significant in succinylated soy protein gel. As such, electrostatic interactions were important for succinylated soy protein to form hard gel but not for unmodified soy protein.