• Journal of Dairy Science and Biotechnology
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• v.19 no.1
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• pp.13-21
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• 2001

Milk can be regarded as a complete food, containing protein, fat, lactose, vitamins and minerals. Milk is heated for a variety of reasons. The main reasons are: to remove pathogenic organisms; to increase shelf-life. But, when milk is heated, many changes take place: denaturation of whey proteins and interaction with casein, Maillard browning, losses of vitamin and minerals. The addition of a additive and milk powder to flavor and taste may cause undesirable change of quality during heating milk. The reconstituted milk is the milk product resulting from the addition of water to the dried or condensed form in the amount necessary to re-establish the specified water solids ratio. Therefore, according to the increasement of consumption of processed milk, the necessity for study about the quality of processed milk mixed with reconstituted milk arose.

• 축산식품과학과 산업
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• v.5 no.2
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• pp.58-69
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• 2016

건강지향의 식육, 육제품에 대한 사회적 요구에 부응하기 위해 기능성 첨가물 대체 연구로부터 원재료인 신선육과 가공공정 중 식육 단백질의 변성을 제어하고 최적화하기 위한 연구과제로써 온도체 가공/급속동결송풍냉각/저온 세절혼합 조합 기술(처리구)에 대한 유효성이 평가되었다. 그 결과 새로 제안된 조합 공정기술은 기존의 냉도체/수침냉각/세절혼합 조합(대조구)과 비교했을 때 단백질 변성 제어를 통한 기능성 단백질 추출성의 향상으로 인해 신선육의 품질향상뿐만 아니라 가열 처리 후 단백질 겔의 수율과 조직감 모두 증진되었으며, 특히 나트륨을 저감화한 조건($2%{\rightarrow}1%$)에서도 기존의 대조구와 유사한 특성을 보여 나트륨 저감화를 위한 기술로 제안될 수 있었다.

• Food Science of Animal Resources
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• v.36 no.1
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• pp.19-22
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• 2016

This study was conducted to improve sensory quality of Jokbal (Korean Pettitoes) made from frozen pig feet by addition of herbal mixture (glasswort, raspberry and Sansa powders). After adding herbal mixture, lipid oxidation (2-thiobarbituric acid values, TBARS), sensory property, and textural property were determined. Herbs were individually added into cooking soup at concentration of 6% (low concentration treatment, LCT) or 12% (high concentration treatment, HCT) of raw pig feet. Refrigerated pig feet were used as control. Thawed feet without any herbal mixture were used as freezing treatment (FT). TBARS in LCT or HCT were lower than that in FT, and showed the similar to that in Control. Addition of the herbal mixture was effective in improving the flavor and textural property of thawed feet by inhibiting lipid oxidation and protein denaturation in a dose-dependent manner.

• Animal cells and systems
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• v.5 no.3
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• pp.195-198
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• 2001

Hepatitis B virus (HBV) polymerase, which possesses the activities of terminal binding, DNA polymerase, reverse transcriptase and RNaseH, has been shown to accomplish viral DNA replication through a pregenomic intermediate. Because the HBV polymerase has not been purified, the expression of HBV polymerase was examined in an E. coli expression system that is under the regulation of arabinose operon. The expressed individual domain containing terminal binding protein, polymerase, or RNaseH turned out to be insoluble. The activities of those domains were not able to be recovered by denaturation and renaturation using urea or guanidine-HCI. The expressed reverse transcriptase containing the polymerase and RNaseH domains became extensively degraded, whereas the proteolysis was reduced in a Ion- mutant. These results indicate that Lon protease proteolyzes the HBV reverse transcriptase expressed in E. coli.

• Annals of Clinical Neurophysiology
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• v.5 no.2
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• pp.214-216
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• 2003

High voltage electrical injury can cause considerable damage to the nervous system including spinal cord, but, the pathophysiology of myelopathy remains to be studied. A 44-year old man with paraparesis after electrical injury was diagnosed as electrical injury induced- myelopathy by normal spine MRI and somatosensory evoked potential showing central conduction abnormality. It implicates that the presumed mechanism of the myelopathy prefers the electroporation or electroconformational protein denaturation to the joule heating.

• Mycobiology
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• v.43 no.3
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• pp.272-279
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• 2015

To screen molecular chaperones similar to small heat shock proteins (sHsps), but without ${\alpha}$-crystalline domain, heat-stable proteins from Schizosaccharomyces pombe were analyzed by 2-dimensional electrophoresis and matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Sixteen proteins were identified, and four recombinant proteins, including cofilin, NTF2, pyridoxin biosynthesis protein (Snz1) and Wos2 that has an ${\alpha}$-crystalline domain, were purified. Among these proteins, only Snz1 showed the anti-aggregation activity against thermal denaturation of citrate synthase. However, pre-heating of NTF2 and Wos2 at $70^{\circ}C$ for 30 min, efficiently prevented thermal aggregation of citrate synthase. These results indicate that Snz1 and NTF2 possess molecular chaperone activity similar to sHsps, even though there is no ${\alpha}$-crystalline domain in their sequences.

• The Korean Journal of Food And Nutrition
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• v.7 no.4
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• pp.353-360
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• 1994

Effect of pH, calcium, sucrose, heating and mixing ratio of soy and cow milk was studied on the viscosity and the sensory characteristics of cow-soy milk. The viscosity of soymilk was significantly affected by pH with showing maximum at 6.0 and the pH effect was decreased as the ratio of cow talk increased. A addition of sucrose or calcium affected little on the viscosity and a negative linear relationship was found be tween viscosity and an increase in cow milk ratio. Sensory characteristics of grassy and beany odor and taste of soymilk were rapidly decreased and nutty flavor and total acceptability were increased during initial 30 min of boiling. A further increase in boiling affected little on tastes and odors of soymilk. The beany odor and taste linearly decreased and milk flavor Increased as the ratio of cow milk increased. The total acceptability of 50 : 50 was found to be maximum for cow and soy mixed milks.

• BMB Reports
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• v.33 no.6
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• pp.493-498
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• 2000

Aquifex pyrophilus, a hyperthermophilic bacterium, has a serine-type protease that is located at the cell wall fraction with a mature size of 43 kDa. Molecular cloning of the protease gene revealed that it has an ORF of 619 amino acids with homologous catalytic site of serine-type proteases [Choi, I.-G., Bang, W.-K., Kim, S.-H., Yu, G. Y., J. Biol. Chem. (1999), Vol. 274, pp. 881-888]. Constructs containing different regions of the protease gene, including a alanine-substituted mutant at the active site serine, were constructed, and the factors affecting the expression level of the cloned protease gene in E. coli were examined. The presence of the C-terminus hydrophobic region of the protease hindered over-expression in E. coli. Also, the proteolytic activity of the expressed protein appeared to toxic to E. coli. An inactive form that deleted both of the N-terminal signal sequence and the C-terminal polar residues was over-expressed in a soluble form, purified to homogeneity, and its thermostability examined. The purified protein showed three disulfide bonds and three free sulfhydryl group. The thermal denaturation temperature of the protein was measured around $90^{\circ}C$ using a differential scanning calorimeter and circular dichroism spectrometry. The disulfide bonds were hardly reduced in the presence of reducing agents, suggesting that these disulfide bonds were located inside of the protein surface.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.17 no.4
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• pp.271-279
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• 1984

Effects of temperature and additives on the stability of actomyosin extracted from skeletal muscle of Israeli carp, Cyprinus carpio nudus, were studied by analyzing free SH-group, ATP-sensitivity and Ca-ATPase activity. The used additives were sucrose, sorbitol, Na-glutamate and L-cysteine. Furthermore, the denaturation constant($K_D$), protective effect(${\Delta}E/M$) and the other thermo-dynamic parameters on protein denaturation are systematically discussed. The actomyosin showed $4.12{\sim}4.68 mg/ml$ in protein concentration, $2.63{\sim}2.93\%$ in ribonucleic acid to the protein, $1:2.20{\sim}2.63$ in the binding ratio of myosin and actin, $4.33{\sim}5.26\%$ in fat content, 109.78 in ATP-sonsitivity, $0.159{\sim}0.201\;{\mu}M-Pi/min/mg-protein$ in Ca-ATPase activity and $3.3{\sim}3.4M/10^5$g-protein in free SH-group content. The first-order rate plots were obtained on the decrease of Ca-ATPase activity and ATP-sensitivity with an increase in temperature, while the free SH-group was increased to $60^{\circ}C$ and decreased rapidly above the temperature. The half-life of Ca-ATPase activity on the actomyosin Ca-ATPase was 280 min at $12^{\circ}C$, 125 min at $20^{\circ}C$, 55 min at $30^{\circ}C$ and 13 min at $40^{\circ}C$, and activation energy, activation enthalpy, activation entropy and free energy of the proteins at $20^{\circ}C$ wene 5,395 cal/mole, 4,814 cal/mole, -40.42 e.u. and 17,626 cal/mole, respectively. The protective effect of the additives on the actomyosin Ca-ATPase showed that the most effective material is $3\%$ sorbitol and followed in the order of $8\%$ Na-glutamate, $1\%$ sucrose and $1\%$ L-cysteine. The actomyosin was more stable at $-30^{\circ}C$ than at $0^{\circ}C$ and $-20^{\circ}C$. and when the additives were used in the low temperature storage, $8\%$ Na-glutamate was the most effective. $3\%$ sorbitol, $1\%$ sucrose and $1\%$ L-cysteine was to become lower in the order.

• Journal of Life Science
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• v.17 no.2 s.82
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• pp.211-217
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• 2007

The goal of this study is to investigate effects of temperature and co-chaperonin requirement for in vitro protein refolding assisted by E. coli chaperone GroEL under permissive and nonpermissive temperature conditions. In vitro protein refolding of two denatured proteins was kinetically investigated under several conditions in the presence of GroEL. Effects of temperature and GroES-requirement on the process of prevention of protein aggregation and refolding of denatured protein were extensively monitored. We have found that E. coli GroEL chaperone system along with ATP is required for invitro refolding of unfolded polypeptide under nonpermissive temperature of $37^{\circ}C$. However, under permissive condition spontaneous refolding can occur due to lower temperature, which can competes with chaperone-mediated protein refolding via GroEL chaperone system. Thus, GroEL seemed to divert spontaneous refolding pathway of unfolded polypeptide toward chaperone-assisted refolding pathway, which is more efficient protein refolding pathway.