• 대한화학회지
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• 제28권1호
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• pp.14-19
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• 1984

메트미오글로빈의 압력에 의한 변성의 $H_2O$와 $D_2O$에서의 차이를 pH 5.7과 pH 7.0에서 연구하였다. 메트미오글로빈은 $D_2O$에서 $H_2O$보다 더 작은 압력에서 변성하였다. 그 차이가 pH 5.7에서가 pH 7에서 보다 더 컸다. $H_2O$와 $D_2O$에서 이 안정도의 차이가 단백질에 대한 $H^+$와 $D^+$의 결합에 차이가 있기 때문이며 또한, 수소가 중수소로 바뀜에 따르는 구조 변화 때문인 것으로 사료된다.

• 한국식품영양학회지
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• 제24권4호
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• pp.740-745
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• 2011

Ohmic heating uses electric resistance heat which occurs equally and rapidly inside food when an electrical current is passed throught. In this study, we observed the physical & chemical characteristics changes which occurs in soybean protein during heating denaturation by using ohmic and conventional heating. After the ohmic heating process, we could not find any change of the primary protein structure in the denaturated soy protein samples. However, the rate of imbibed water(RIW) of the ohmic samples was 2 times faster than that of the conventional samples. Also the ANS-surface hydrophobicity was decreased, which is very closely related to RIW. In the differential scanning calorimeter(DSC) analysis result, all 7S soyprotein fraction samples were completely denaturated by ohmic and conventional heating. However, the 11S samples were completely denatured only by ohmic heating. According to the DSC result, we decided that soyprotein was damaged by temperature and electrical current during ohmic heating. The damage of electrical current was a cause of the characteristic changes.

• Bulletin of the Korean Chemical Society
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• 제30권9호
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• pp.1973-1977
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• 2009

In the present study, at first, 2,4-Dihydroxy Salophen (2,4-DHS), has been synthesized by combination of 1, 2-diaminobenzene and 2,4-dihydroxybenzaldehyde in a solvent system. This ligand containing meta-quinone functional groups were characterized using UV-Vis and IR spectroscopies. Subsequently, the interaction between native calf thymus deoxyribonucleic acid (ct-DNA) and 2,4-DHS, was investigated in 10 mM Tris/HCl buffer solution, pH 7.2, using UV-visible absorption and fluorescence spectroscopies, thermal denaturation technique and viscosity measurements. From spectrophotometric titration experiments, the binding constant of 2,4-DHS with ct-DNA was found to be (1.1 ${\pm}\;0.2)\;{\times}\;10^4\;M^{-1}.$ The fluorescence study represents the quenching effect of 2,4-DHS on bound ethidium bromide to DNA. The quenching process obeys linear Stern-Volmer equation in extended range of 2,4-DHS concentration. Thermal denaturation experiments represent the increasing of melting temperature of DNA (about 3.5 ${^{\circ}C}$) due to binding of 2,4-DHS. These results are consistent with a binding mode dominated by interactions with the groove of ct-DNA.

• Journal of Microbiology and Biotechnology
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• 제28권9호
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• pp.1457-1466
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• 2018

In the present study, the stabilizing effect of four different biological osmolytes on Bacillus licheniformis ${\gamma}$-glutamyl transpeptidase (BlGGT) was investigated. BlGGT appeared to be stable under temperatures below $40^{\circ}C$, but the enzyme retained less than 10% of its activity at $60^{\circ}C$. The tested osmolytes exhibited different degrees of effectiveness against temperature inactivation of BlGGT, and sucrose was found to be the most effective among these. The use of circular dichroism spectroscopy for studying the secondary structure of BlGGT revealed that the temperature-induced conformational change of the protein molecule could be prevented by the osmolytes. Consistently, the molecular structure of the enzyme was essentially conserved by the osmolytes at elevated temperatures as monitored by fluorescence spectroscopy. Sucrose was further observed to counteract guanidine hydrochloride (GdnHCl)-and urea-induced denaturation of BlGGT. Taken together, we observed evidently that some well-known biological osmolytes, especially sucrose, make a dominant contribution to the structural stabilization of BlGTT.

• 한국수산과학회지
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• 제42권6호
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• pp.574-579
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• 2009

Acid- and pepsin-solubilized collagens were extracted from the skin of shark (Isurus oxyrinchus) and their physicochemical properties were characterized by amino acid analysis, SDS-PAGE, the composition of collagen types, solubility and denaturation temperature. Acid - and pepsin-solubilized collagens from shark skin had an imino acid of 188.8 and 186.2 residues/1,000 amino acids, respectively. SDS-PAGE showed two different${\alpha}$ chains ($\alpha1$ and $\alpha2$) and $\beta$-component. The component ratio of type I and V was 10:1, and the type III was not found. Solubility of acid-soluble collagen was low in the range of pH 6.0 to pH 11.0. On the other hand, pepsin-solubilized collagen showed a low solubility in the range of pH 7.0-9.0. Temperature for denaturation of acid- and pepsin-solubilized collagens were $25^{\circ}C$ and $27^{\circ}C$, respectively.

• 한국응용곤충학회지
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• 제30권2호
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• pp.138-143
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• 1991

배추흰나비 P. rapae와 P. brassicae GV의 DNA성상과 이를 기초로한 상동성을 검정한 결과 Tm값에서는 P. rapae GV DNA는 $83.7^{\circ}C$이고, P. brassicae GV DNA의 경우는 $84.0^{\circ}C$로 G+C 함량은 전자가 35.5%, 후자가 35.9%였다. 그리고 제한산소처리에 의한 DNA의 분석에서는 P. Rapae GV의 genome의 크기는 103 kb, P. brassicae GV DNA는 108kb로 나타났으며, 두바이러스 간의 상동성은 97.0%였다.

• BMB Reports
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• 제39권5호
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• pp.636-641
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• 2006

Our previous studies indicated that native carbonic anhydrase does not interact with hydrophobic adsorbents and that it acquires this ability upon denaturation. In the present study, an apo form of the enzyme was prepared by removal of zinc and a comparative study was performed on some characteristic features of the apo and native forms by far- and near-UV circular dichroism (CD), intrinsic fluorescent spectroscopy, 1-anilino naphthalene-8-sulfonate (ANS) binding, fluorescence quenching by acrylamide, and Tm measurement. Results indicate that protein flexibility is enhanced and the hydrophobic sites become more exposed upon conversion to the apo form. Accordingly, the apo structure showed a greater affinity for interaction with hydrophobic adsorbents as compared with the native structure. As observed for the native enzyme, heat denaturation of the apo form promoted interaction with alkyl residues present on the adsorbents and, by cooling followed by addition of zinc, catalytically-active immobilized preparations were obtained.

• Fisheries and Aquatic Sciences
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• 제17권3호
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• pp.291-298
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• 2014

We investigate the effects of cryoprotectant mixtures on the quality of sand lance surimi (SLS) during storage at $-30^{\circ}C$. We monitored freeze-induced denaturation of myofibrillar protein in SLS and examined the texture profile of SLS gel. Freeze-induced denaturation was assessed by evaluating SLS $Ca^{+2}$-ATPase activity. SLS gels prepared with sorbitol or sucrose and a mixture of both as cryoprotectant. Higher concentrations of cryoprotectants resulted in significantly higher residual SLS $Ca^{+2}$-ATPase activity at the same storage time (P < 0.05). Residual $Ca^{2+}$-ATPase activity of SLS prepared with sorbitol was higher than that of sucrose when cryoprotectant concentration and storage period were same. A blend of sorbitol and sucrose resulted in a stronger cryoprptective effect of SLS myofibrillar protein than did sorbitol or sucrose alone. The presence of a phosphate compound in SOP (3% sorbitol + 0.2% phosphate compound) resulted in higher SLS $Ca^{2+}$-ATPase activity than that of did 5% sorbitol. The hardness, brittleness, and elasticity values and a folding test of the SLS gels were significantly affected by cryoprotectant concentrations and the storage time. Preference scores and acceptance for texture in a sensory evaluation of the SLS gels increased with increasing sorbitol or sucrose concentration.

• 한국식품과학회지
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• 제2권2호
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• pp.49-55
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• 1970

대두단백육(textured soybean protein food)의 제조 과정에서 분리한 대두단백의 건조공정은 단백 gel의 성질과 보수력, 점성도 같은 단백질 특성에 영향을 미쳤다. 모델시스템의 실험에서 질소용해계수로 표시한 대두단백의 변성도는 분리대두단백 gel의 강도의 중요한 변수로 나타났다. gel strength는 질소용해계수가 43이었을 때 최대가 되었고 질소 용해계수가 그보다 증가할 때나 감소할 때는 gel strength가 감소되었다. 이러한 사실은 분리대두단백의 건조공정 중 적당한 단백의 변성은 단백육제조에 필요하며 그 이상의 높은 질소용해계수를 갖도록 할 필요는 없다.

• 한국수산과학회지
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• 제18권5호
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• pp.455-463
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• 1985

말쥐치 육의 근원섬유단백질을 추출하고 몇가지 온도조건이 그 변성에 미치는 영향을 실험하였으며, sucrose와 sorbitol 및 아미노산을 첨가하였을 때의 변성억제효과에 관하여도 비교 검토하였다. 실험에서 얻은 결과를 요약하면 다음과 같다. 1. 말쥐치 근원섬유단백질의 $25^{\circ}C,\;30^{\circ}C,\;35^{\circ}C$에서의 변성속도정수($K_D$값)는 각각 $19.52{\times}10^{-5},\;112.25{\times}10^{-5},\;247.20{\times}10^{-5}$이었다. 활성화 에너지${\Delta}E$값은 43 kcal/mole, 활성화엔탈피 ${\Delta}H$는 42.4kcal/mole, 활성화 엔트로피 ${\Delta}S$는 66.79 e.u., 그리고 자유에너지 ${\Delta}G$는 22.4kcal/mole이었다. 2. 말쥐치 근원섬유단백질이 $0^{\circ}C$에서 96시간 경과했을 때는 최초 활성의 $53\%$가 감소하였고, $-20^{\circ}C$에서 60시간이 경과했을 때는 약 $72\%$가 감소했다. 3. 농도별 첨가제의 가열변성에 대한 억제 효과는 1M Na-Glu>1M sorbitol>1.25M Gly>0.5M sucrose>1.25M Ala의 순이며, 변성억제효과 값 ${\Delta}E$는 Na-Glu가 1.25, sorbitol이 0.58, Gly이 0.28, sucrose가 0.21, Ala이 0.05이였다. 4. 혼성 첨가시는 1M Na-Glu+1.25M Gly>1M sorbitol+1.25 M Gly>1M sorbito1+0.5M sucrose>1M sorbito1+1M Na-Glu순으로 가열변성억제효과를 가지고 있으며, 이들의 $K_D$값은 위의 순서대로 $25^{\circ}C$에서 각각 $1.38{\times}10^{-5},\;11.75{\times}10^{-5},\;14.95{\times}10^{-5},\;15.66{\times}10^{-5}$으로서 무첨가시보다 $7{\sim}l.2$배의 효과를 나타내고 있었다. 5. 혼성 첨가시의 열역학적 함수로서 활성화 에너지, 활성화 엔탈피, 활성화 엔트로피, 자유 에너지는 Na-Glu+Gly 일 때, 68.4kcal/mole, 67.8 kcal/mole, 146.70 e. u., 24kca1/mole이며, sorbitol+Gly은 44kcal/mole, 43.4kcal/mole, 69.14 e. u., 22.8kcal/mole, sorbitol+sucrose는 42.7kcal/mole, 42.1kcal/mole 65.26 e. u., 22.6kcal/mole이고. sorbitol+Na-Glu는 49kcal/mole, 48.4kcal/mole, 86.49 e. u., 22.6kcal/mole이었다. 6. 냉동중의 변성억제효과는 1M Na-Glu+1.25M Gly/1M sorbito1+0.5M sucrose>1M sorbitol+1.25M $Gly{\sim}lM$ sorbito1+1M Na-Glu의 순으로 좋았다.