• 제목/요약/키워드: Thermal stability of protein

검색결과 101건 처리시간 0.025초

Sport impact on the strength of the nanoscale protein tissues under the thermal condition

  • Xin, Fang;Mengqian, Hou
    • 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.

Thermal Stabilization of Aspergillus phytase by L-Arginine

  • Sunghoon Ryu;Park, Tae-Gwan
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제3권1호
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    • pp.32-34
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    • 1998
  • Phytase from Aspergillus species is a very heat unstable enzyme which inactivates to a great extent during the thermal processing of animal feed formulation. Various protein stabilization additives were tested to improve its heat stability. Among them, a basic amino acid, L-arginine remarkably increased the thermal stability of phytase in an aqueous solution state.

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높은 cAMP 농도에서 cAMP 수용성 단백질의 열 안정화 (Cyclic AMP Receptor Protein Adopts the Highly Stable Conformation at Millimolar cAMP Concentration)

  • 강종백;최영
    • 생명과학회지
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    • 제13권5호
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    • pp.751-755
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    • 2003
  • Cyclic AMP receptor proteins(CRP) activate many genes in Escherichia coli by binding of cAMP with not fully known mechanism. CRP existed as apo-CRP in the absence of cAMP, $CRP;(cAMP)_2$$_2$ at low(micromolar) cAMP concentration, or $CRP;(cAMP)_4$ at high(millimolar) concentration of cAMP. This study is designed to measure the thermal stability of S83G CRP, which substituted glycine for serine at amino acid 83 position, with CD spectrapolarimeter at 222nm by the constant elevation of temperature from $20^{\circ]C\; to\; 90^{\circ}C\; at\; 1^{\circ}C/min$. The non-linear regression analysis showed that melting temperatures were 68.4, 72.0, and $82.3^{\circ}C$ for no cAMP, 0.1mM cAMP, and 5mM cAMP, respectively. Result showed the strong thermal stability of CRP by binding of additional cAMP molecules to region between the hinge region and helix-turn-helix(HTH) motif at 5mM cAMP concentration.

Dimethylglutarylation에 의한 변형대두단백질의 기능적 특성 (Functional Properties of Modified Soybean Protein Isolate by Dimethylglutarylation)

  • 최원균;정철원
    • 한국식생활문화학회지
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    • 제14권5호
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    • pp.477-485
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    • 1999
  • This study was conducted to improve the functional properties of soybean protein isolate by dimethylglutarylation and acetylation. Amino acid composition and solubility of modified soybean protein by dimethylglutarylation were not changed, but lysine and trypsin inhibitor activity was decreased an isoelectric point was moved from pH5 to pH4 as a result of modification. Emulsification capacity and stability, foaming capacity and thermal stability were increased by the modification. In that 91% dimethylglutarylated protein did not coagulate when heating at $100^{\circ}C$ for 20 min. while its foaming stability was decreased. Whereas specific gravity was decreased by the modification of the soybean protein, relative viscosity and whiteness were improved. Generally, dimethylglutarylation produced more conformational changes in protein system than did in acetylation.

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Bio-film Composites Composed of Soy Protein Isolate and Silk Fiber: Effect of Concentration of Silk Fiber on Mechanical and Thermal Properties

  • Prabhakar, M.N.;Song, Jung Il
    • Composites Research
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    • 제27권5호
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    • pp.196-200
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    • 2014
  • A novel, simple and totally recyclable method has been developed for the synthesis of nontoxic, biocompatible and biodegradable bio-composite films from soy protein and silk protein. Bio films are defined as flexible films prepared from biological materials such as protein. These materials have potential application in medical and food as a packaging material. Their use depends on various parameters such as mechanical (strength and modulus), thermal, among others. In this study, prepare and characterization of bio films made from Soy Protein Isolate (SPI) (matrix) and Silk Fiber (SF) (reinforcement) through solution casting method by the addition of plasticizer and crosslinking agent. The obtained SPI and SPI/SF composites were subsequently subjected to evaluate their mechanical and thermal properties by using Universal Testing Machine and Thermal Gravimetric Analyzer respectively. The tensile testing showed significant improvements in strength with increasing amount of SF content and the % elongation at break of the composites of the SPI/SF was lower than that of the matrix. Though the interfacial bonding was moderate, the improvement in tensile strength and modulus was attributed to the higher tensile properties of the silk fiber.

Stability and Structure of S128A Mutant cAMP Receptor Protein

  • Choi, Young;Gang, JongBack
    • 통합자연과학논문집
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    • 제4권3호
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    • pp.222-226
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    • 2011
  • Cyclic AMP receptor protein(CRP) is involved in the activation of many genes corresponding to catabolite enzymes in Escherichia coli. In this study, mutant CRP(S128A) was used to elucidate the effect of Ser 128 on the cAMP-induced structural change. Based on the protease digestion and thermal analysis, serine 128 in CRP affects the cAMP binding capability and then structural change of CRP protein. In addition, CD spectra in near UV region revealed that S128A CRP retained the sensitive conformation to thermal effect relative to that of wild-type CRP, in spite of identical Tm values in the absence of cAMP.

Backbone Cyclization of Flavin Mononucleotide-Based Fluorescent Protein Increases Fluorescence and Stability

  • Tingting Lin;Yuanyuan Ge;Qing Gao;Di Zhang;Xiaofeng Chen;Yafang Hu;Jun Fan
    • Journal of Microbiology and Biotechnology
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    • 제33권12호
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    • pp.1681-1691
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    • 2023
  • Flavin mononucleotide-binding proteins or domains emit cyan-green fluorescence under aerobic and anaerobic conditions, but relatively low fluorescence and less thermostability limit their application as reporters. In this work, we incorporated the codon-optimized fluorescent protein from Chlamydomonas reinhardtii with two different linkers independently into the redox-responsive split intein construct, overexpressed the precursors in hyperoxic Escherichia coli SHuffle T7 strain, and cyclized the target proteins in vitro in the presence of the reducing agent. Compared with the purified linear protein, the cyclic protein with the short linker displayed enhanced fluorescence. In contrast, cyclized protein with incorporation of the long linker including the myc-tag and human rhinovirus 3C protease cleavable sequence emitted slightly increased fluorescence compared with the protein linearized with the protease cleavage. The cyclic protein with the short linker also exhibited increased thermal stability and exopeptidase resistance. Moreover, induction of the target proteins in an oxygen-deficient culture rendered fluorescent E. coli BL21 (DE3) cells brighter than those overexpressing the linear construct. Thus, the cyclic reporter can hopefully be used in certain thermophilic anaerobes.

가소제 및 가교제에 의해 개질된 대두단백질의 특성 (Characteristics of Soybean Protein Resin Modified by Plasticizers and Cross-Linking Agents)

  • 최한나;이태상;양지우;이승구
    • 접착 및 계면
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    • 제12권2호
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    • pp.73-80
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    • 2011
  • 식물성 고분자인 대두단백질을 기반으로 하는 환경친화성 고분자 신소재에 관한 연구를 위해 가소제(1,3-propandiol, glycerol) 및 가교제(glutaraldehyde, epichlorohydrin, glyoxal, urea)에 의한 대두단백질 수지의 열적 특성을 TGA를 이용하여 분석하였고, 기계적 특성 분석과 SEM을 통하여 파단면을 관찰하였다. 그 결과, 가소제인 1,3-propandiol과 glycerol을 SPI (대두단백질)에 첨가함으로써 수지의 유연성이 증가하였고, 1,3-propandiol에 비하여 glycerol의 가소화 효과가 상대적으로 크게 나타났으며, 가교제인 glycerol, epichlorohydrin, glyoxal의 적용으로 첨가량이 증가할수록 대두단백질 수지의 강도와 열안정성이 증가하는 반면, urea의 경우, 대두단백과의 가교가 용이하지 않아 열안정성이 오히려 낮아지고, 강도가 감소함을 알 수 있었다.

Effect of NaCl, Gum Arabic and Microbial Transglutaminase on the Gel and Emulsion Characteristics of Porcine Myofibrillar Proteins

  • Davaatseren, Munkhtugs;Hong, Geun-Pyo
    • 한국축산식품학회지
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    • 제34권6호
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    • pp.808-814
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    • 2014
  • This study investigated the effect of gum arabic (GA) combined with microbial transglutaminase (TG) on the functional properties of porcine myofibrillar protein (MP). As an indicator of functional property, heat-set gel and emulsion characteristics of MP treated with GA and/or TG were explored under varying NaCl concentrations (0.1-0.6 M). The GA improved thermal gelling ability of MP during thermal processing and after cooling, and concomitantly added TG assisted the formation of viscoelastic MP gel formation. Meanwhile, the addition of GA decreased cooking yield of MP gel at 0.6 M NaCl concentration, and the yield was further decreased by TG addition, mainly attributed by enhancement of protein-protein interactions. Emulsion characteristics indicated that GA had emulsifying ability and the addition of GA increased the emulsification activity index (EAI) of MP-stabilized emulsion. However, GA showed a negative effect on emulsion stability, particularly great drop in the emulsion stability index (ESI) was found in GA treatment at 0.6 M NaCl. Consequently, the results indicated that GA had a potential advantage to form a viscoelastic MP gel. For the practical aspect, the application of GA in meat processing had to be limited to the purposes of texture enhancer such as restructured products, but not low-salt products and emulsion-type meat products.

Biological Characterization of the Omp1-like Protein from Actinobacillus actinomycetemcomitans

  • Ha, Jung-Hye;Jeong, Mi-Suk;Jo, Wol-Soon;Jeong, Min-Ho;Jang, Se-Bok
    • Bulletin of the Korean Chemical Society
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    • 제31권2호
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    • pp.275-280
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    • 2010
  • Actinobacillus actinomycetemcomitans is a gram-negative, nonmotile coccobacillus bacterium that is associated with several human diseases, including endocarditis, meningitis, osteomyelitis, subcutaneous abscesses and periodontal diseases. A full-length Omp1-like protein gene from A. actinomycetemcomitans was cloned into a pQE30 vector and overexpressed in Escherichia coli BL21(DE3) cells. The protein revealed sequence homologies to Seventeen kilodalton proteins (Skp) from Pasteurella multocida and E. coli that have been characterized as periplasmic chaperones. This soluble Omp1-like protein was successfully purified to homogeneity for further folding and functional studies. The purity, identity, and conformation of the protein were determined using sodium dodecyl sulfate polyacrylamide gel electrophoresis, matrix-assisted laser desorption ionization mass spectrometry, circular dichroism, fluorescence spectroscopic, and differential scanning calorimetric studies. We showed that the protein formed an oligomer larger than a tetramer. We found, further, that it is comprised of mostly $\alpha$-helices and boasts high thermal stability.