• Advances in nano research
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• 제13권6호
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• pp.561-574
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• 2022

The stability of protein tissues and protein fibers in the human muscle is investigated in the presented paper. The protein fibers are modeled via tube structures embedded in others proteins fibers like the elastic substrate. Physical sport and physical exercise play an important role in the stability of synthesis and strength of the protein tissues. In physical exercise, the temperature of the body increases, and this temperature change impacts the stability of the protein tissues, which is the aim of the current study. The mathematical simulation of the protein tissues is done based on the mechanical sciences, and the protein fibers are modeled via wire structures according to the high-order theory beams. The thermal stress due to the conditions of the sport is applied to the nanoscale protein fibers, then the stability regarding the frequency analysis is investigated. Finally, the impact of temperature change, physical exercise, and small-scale parameters on the stability of the protein tissues are examined in detail.

• Advances in nano research
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• 제13권5호
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• pp.487-497
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• 2022

This study investigates the stability of protein tissues regarding the vibration analysis based on the classical beam theory coupled with the nonlocal elasticity theory concerning the exercise impact. As reported in the previous research, four different types of protein tissues are supposed, and the influence of sports training is investigated. The protein tissues are made of protein fibers surrounded by an elastic foundation. The exercise enhances the muscle area and plays an essential role in the stability and strength of protein and muscle tissues. The results are examined in detail to examine the impact of different parameters on the stability of nano protein fibers.

• Biotechnology and Bioprocess Engineering:BBE
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• 제8권1호
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• pp.9-18
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• 2003

The most challenging and emerging field of biotechnology is the tailoring of proteins to attain the desired characteristic properties. In order to increase the stability of proteins and to study the function of proteins, the mechanism by which proteins fold and unfold should be known. It has been debated for a long time how exactly the linear form of a protein is converted into a stable 3-dimensional structure. The literature showed that many theories support the fact that protein folding E5 a Thermodynamically controlled process. It is also possible to predict the mechanism of protein deactivation and Stability to an extent from thermodynamic studies. This article reviewed various theories that have been proposed to explain the process of protein folding after its biosynthesis in ribosomes. The theories of the determination of the thermodynamic properties and the interpretation of thermodynamic data of protein stability are 3150 discussed in this article.

• Preventive Nutrition and Food Science
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• 제3권2호
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• pp.133-142
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• 1998

Effects of protein heat treatment and surfactant additionoo the orthokindetic stability of $\beta$-lactoglobulin-stabilized emulsions have been investigated under turbulent flow conditions. In studies on protein-stabilized emulsions, samples which had been subjected to heat treatment(i.e. the protein solution orthe emulsion) have been found to be more prone to orthokinetic coalescene than the untreated ones. The emulsions stabilized with protein heated above the denaturation temperature(i.e. 7$0^{\circ}C$) showed the bigger initial average droplet size, which resulted in an increased orthokinetic coalescenece rate. The storage of the protein-stabilized emulsion at high temperature prior to the shearing experiment also made the emulsion less stable in the shear field. Interestingly. the addition of DATEM has been found to produce a substantial increase in orthokinetic stability of the heat-denatured protein-stabilized emulsion system, although Tween 20 is the opposite case.

• 대한가정학회지
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• 제28권2호
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• pp.37-45
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• 1990

The purpose of this study was to determine the foaming properties of two small red bean protein isolates at various conditions. Data concerning the effects of pH, temperature, MaCl concentration, sugar concentration and protein concentration on the properties such as solubility, foam expansion, foam stability were presented. The results were summarized as follows : 1. The crude protein contents of two small red beans were 26.14% and 22.71%. The percentage of nonpolar amino acid group was the highest and that of sulfur containing amino acid group was the lowest. 2. Protein solubility showed the minimum at pH 4.5 which is isoelectric point of small red bean protein isolate adn heat treatment lowered solubility(P<0.05). At pH 4.5, solubility increased sighificantly as 0.4M NaCl was added. However, the effect of sugar concentration in the solubility was not significant. 3. Foam expansion of two small red bean protein isolates was high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam expansion(P<0.05). While addition of NaCl, sugar did not affect the foma expansion, gradual increment of the protein isolates concentration up to 9% decreased the foma expansion slightly. 4. Foam stability was significantly high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam stability. Addition of sugar caused slight decrease in foam stability. From 1% to 9% suspension, foma stability increased significantly as protein concentration increased(P<0.05)

• Applied Biological Chemistry
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• 제35권6호
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• pp.457-461
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• 1992

본 연구에서는 단백질과 기름의 농도가 분리대두단백질의 유화안정성에 미치는 영향을 연구하였다. 특히 유화안정성과 에멀젼의 기름입자크기 및 점도와의 상관관계를 구명하였으며, 또한 유화과정 중 단백질이 물과 기름 사이의 계면에 흡착하는 현상을 조사하였다. 단백질의 농도가 증가할수록 기름입자의 크기는 감소하고 점도는 증가하여 결과적으로 유화안정성이 증가하였다. 반면에 기름농도가 증가한 경우 기름입자의 크기와 점도가 모두 증가하였으며, 이 경우에는 두 요인의 상대적인 지배정도에 따라 에멀젼의 유화안정성이 결정되었다.

• 한국식품과학회지
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• 제37권2호
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• pp.164-170
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• 2005

미생물유래의 중합화효소(microbial transglutaminase, MTGase)를 이용하면 식품 단백질의 기능특성을 향상시키는 것이 가능하다. 본 연구에서는 MTGase를 이용, 동물성 단백질인 ${\beta}$-casein 및 식물성 단백질인 11S globulin의 동종 혹은 이종간을 bio-hybrid시킴으로써 단백질의 기능특성을 향상시키고자 하였다. 즉, SDS-PAGE에 의한 susceptibility 확인, particle size 분석 및 Reddy and Foster 방법에 의한 유화안정성(emulsion stability) 실험, 그리고 유화안정성에 영향을 주는 bio-hybrid된 단백질이 어떤 형태로서 안정성에 영향을 미치는지 주사형 전자현미경(SEM)을 이용하여 유적(oil droplet)에 결합된 단백질을 고배율로 분석하였다. SDS-PAGE에 의해 동종 흑은 이종의 단백질간의 가교결합이 형성되었으며, 특히 이종간의 결합은 그 밴드가 약하게 형성되었으며 oligomer의 형태를 나타내었다. 또한 유화안정성은 동종간에서는 ${\beta}$-casein이 우수하였으며, glycinin은 안정성이 거의 없는 것으로 나타났다. 그러나, 두 단백질 이종간의 안정성은 glycinin보다 더 우수하였다. 전자현미경 사진에서는 유적에 bio-hybrid된 단백질이 고르게 분포될수록 안정성이 더 우수한 것으로 판단되었다.

• 한국식품영양학회지
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• 제9권3호
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• pp.319-324
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• 1996

The functional properties of protein recovered from red crab (Chitinonecetes opiiie) processing in water (RCP) were examined and compared with those of soybean protein isolate at pH 2~10 in water and NaCl solu5ion. The solubilities of RCP and SPI were miniumu at pH 4, the isoelectric point and increased significantly at lower or higher than pH 4. Solubilities in NaCl solution for both proteins decreased with incr NaCl concentration increase at all pH ranges. Emulsion capacity for both proteins was also minimum at pH 4 and increased as protein concentration increased from 2 to 6%. Emulsion capacity of RCP was higher than these of SPI at pH 6∼10 and all protein concentrations. Emulsion stability showed a similar trend to that of emulsion capacity. RCP had higher oft absorption capacity and lower water absorption capacity than SPI.

• Biotechnology and Bioprocess Engineering:BBE
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• 제11권3호
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• pp.258-261
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• 2006

The addition of zeolite particles enhances the stability of mRNA molecules in a cell-free protein synthesis system. When $20{\mu}g/{\mu}L$ of zeolite (Y5.4) is added to a reaction mixture of cell-free protein synthesis, a substantial increase in protein synthesis is observed. The stabilizing effect of zeolite is most dearly observed in an in vitro translation reaction directed by purified mRNA, as opposed to a coupled transcription and translation reaction. Upon the addition of zeolite in the in vitro translation reaction, the life span of the mRNA molecules is substantially extended, leading to an 80% increase in protein synthesis. The effect of zeolite upon the mRNA stability appears be strongly related to the cation exchange (potassium to sodium) reaction. Our results demonstrate the possibility of modifying this biological process using heterogeneous, non-biological substances in a cell-free protein synthesis system.

• 한국식품조리과학회지
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• 제4권2호
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• pp.1-9
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• 1988

This study was carried out in order to study the foaming properties of mungbean protein. Mungbean protein isolate was tested for the purpose of finding out the effect of pH, addition of sucrose on foaming properties. The results were summarized as follows: 1. Foam expansion values were generally depen. dent on protein concentration to 3% protein suspension. From 1% to 3% suspension, foam expansion values increased. However over 3% suspension, the values decreased. In 1% mungbean protein suspension, the foam expansion value of suspension at pH 4.5 was greater than that of at pH9. In 3%, 5%, and 10% suspensiona the foam expansion values of suspension at pH 7 was the lowest. Foam expansion value significantly decreased by the addition of sucrose. 2. The foam stability appeared the greatest value as protein concentration increased. It appeared the greatest value at pH 4.5. When sucrose was added, the foam stability increased. The more sucrose was added, the better foam stability was.