• Food Science of Animal Resources
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• v.21 no.3
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• pp.265-271
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• 2001

We investigated changes of immunoglobulin G (IgG) concentrations by heating and drying condition. Also it is performed to group for commercial product by promoting of IgG preservation and reducing of protein denaturation. The result was that content of IgG in colostrum was higher than normal milk. Especially, IgG content of colostrum within 12 hrs after parturition was over 44.67mg/ml and it is 60 times of normal milk. IgG contents was reduced rapidly according as passage of the time. IgG content of the sample heating at 30min at 65$^{\circ}C$ was still a little higher that heating for 10sec at 72$^{\circ}C$. IgG denaturation of heat treatment at 100$^{\circ}C$ for 10sec was lower than at 85$^{\circ}C$ for 30min. We investigated the changes of IgG concentrations of kinds of market milk different with heating processing. This result showed that IgG denaturation ratio by ultra high temperature pasteurization (UHT) was higher than long time low temperature pasteurization (LTLT). On the other hands, IgG content by spray drying was 14.5mg/g and freezing drying was 10.8mg/g. It showed that denaturation of protein content by freezing drying was more than spray drying.

• Journal of Applied Biological Chemistry
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• v.58 no.2
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• pp.97-100
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• 2015

The thermostable pectinase gene TmPec isolated from Thermotoga maritima was introduced into the NdeI site of pRSET-B vector and expressed in its intact form in Escherichia coli BL21. The overexpressed intact form of pectinase (TmPecN protein) was partially purified by heat-denaturation procedure. TmPecN showed the highest activity between 85 and $95^{\circ}C$, and at approximately pH 6.5. Enzyme activity was stably maintained at temperatures below $85^{\circ}C$. In the presence of $Ca^{2+}$, pectinase activity of TmPecN increased to 128.4% of normal level. In contrast, $Ba^{2+}$, $Zn^{2+}$, and $Mn^{2+}$ strongly inhibited TmPecN activity. We conclude that the biochemical properties of the intact form of TmPecN are comparable to those of the recombinant protein TmPec reported previously.

• Journal of Dairy Science and Biotechnology
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• v.35 no.4
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• pp.270-285
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• 2017

Among milk proteins, caseins are not subjected to chemical changes during heat treatment of milk; however, whey proteins are partially denatured following heat treatment. The degree of whey protein denaturation by heat treatment is decreased in the order of high temperature short time (HTST) > low temperature long time (LTLT) > direct-ultra-high temperature (UHT) > indirect-UHT. As a result of heat treatment, several changes, including variations in milk nitrogen, interactions between beta-lactoglobulin and k-casein, variations in calcium sulfate and casein micelle size, and delay of milk coagulation by chymosin action, were observed. Lysine, an important essential amino acid found in milk, was partially inactivated during heat treatment. Therefore, the available amount of lysine decreased slightly (1~4% decrease) after heat treatment, However, the influence of heat treatment on the nutritional value of milk was negligible. Nutritional value and nitrogen balance did not differ significantly between UHT and LTLT in milk. In conclusion, our results showed that heat treatment of milk did not alter protein quality. Whey proteins denatured to a limited extent during the heat treatment process, and the nutritional value and protein quality were unaffected by heat treatment.

• Microbiology and Biotechnology Letters
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• v.13 no.1
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• pp.7-11
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• 1985

In order to investigate the biological activity of ginseng saponins, the effects of ginseng saponins on the reaction catalyzed by bacterial a-amylase were studied and the results obtained were summerized as follows. Bacterial ${\alpha}$-amylase activity was increased by the addition of protopanaxadiol (diol), protopanaxatriol (triol) and total saponin. Preincubation of ${\alpha}$-amylase with diol saponin at $40^{\circ}C$ for 3 min increased ${\alpha}$-amylase activity to the degree of 120%. In the protective effect on the heat denaturation of the enzyme, triol saponin protected the heat denaturation for 5 min at $60^{\circ}C$, but diol saponin accelerated the heat denaturation. The hydrolyzates of diol and triol saponin increased the enzyme activity more than the intact diol and triol saponin. In the catalysis system of bacterial ${\alpha}$-amylase, the addition of diol and triol saponin reduced the substrate inhibition in the presence of high concentration of the substrate.

• Archives of Pharmacal Research
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• v.22 no.5
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• pp.485-490
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• 1999

The mechanism of action of fish oil (FO), currently used in different chronic inflammatory conditions such as rheumatoid arthritis (RA), is not completely understood, although it is thought that it could alter the metabolism of endogenous autacoids. In addition, we hypothesized that the known capability of fatty acids (FA) of stabilizing serum albumin and perhaps other proteins, may be of pharmacological relevance considering that it is shared by other anti-rheumatic agents (e.g. nonsteroidal antiinflammatory drugs). Thus, we studied the effect of oral administration of FO and corn oil (CO), a vegetable oil with a different composition, on the stability of rat serum proteins, evaluated buy a classical in vitro method based on heat-induced protein denaturation. FO, and, to a lower extent, CO inhibited heat-induced denaturation of rat serum (RS): based on the inhibitory activity (EC50) of the major fatty acids against heat-induced denaturation of RS in vitro, it was possible to speculate the in vivo effects of palmitic acid (C16:0) and eicosapentaenoic acid (EPA, C20:5, n-3) may be more relevant than that of linolenic acid (C18:2). To better investigate this phenomenon, we extracted albumin from the serum of animals treated or not with FO with a one-step affinity chromatography technique, obtaining high purity rat serum albumin preparations (RSA-CTRL and RSA-FO), as judged by SDS-PAGE with Coomassie blue staining. When these RSA preparations were heated at $70^{\circ}C$ for 30 min, it was noted that RSA-FO was much more stable than RSA-CTRL, presumably due to higher number of long chain fatty acids (FA) such as palmitic acid or EPA. In conclusion, we provided evidences that oral administration of FO in the rat stabilizes serum albumin, due to an increase in the number of protein bound long chain fatty acids (e.g. palitic acid and EPA). We speculate that the stabilization of serum albumin and perhaps other proteins could prevent changes of antigenicity due to protein denaturation and glycosylation, which may trigger pathological autoimmune responses, suggesting that this action may be involved in the mode of action of FO in RA and other chronic inflammatory diseases.

• Molecules and Cells
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• v.23 no.2
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• pp.123-131
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• 2007

Extracellular stresses induce heat shock response and render cells resistant to lethal stresses. Heat shock response involves induction of heat shock proteins (Hsps). Recently the roles of Hsps in neurodegenerative diseases and cancer are attracting increasing attention and have accelerated the study of heat shock response mechanism. This review focuses on the stress sensing steps, molecules involved in Hsps production, diseases related to Hsp malfunctions, and the potential of proteomics as a tool for understanding the complex signaling pathways relevant to these events.

• BMB Reports
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• v.41 no.2
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• pp.108-111
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• 2008

Some proteins of E. coli are stable at temperatures significantly higher than $49^{\circ}C$, the maximum temperature at which the organism can grow. The heat stability of such proteins would be a property which is inherent to their structures, or it might be acquired by evolution for their specialized functions. In this study, we describe the identification of 17 heat-stable proteins from E. coli. Approximately one-third of these proteins were recognized as having functions in the protection of other proteins against denaturation. These included chaperonin (GroEL and GroES), molecular chaperones (DnaK and FkpA) and peptidyl prolyl isomerases (trigger factor and FkpA). Another common feature was that five of these proteins (GroEL, GroES, Ahpc, RibH and ferritin) have been shown to form a macromolecular structure. These results indicated that the heat stability of certain proteins may have evolved for their specialized functions, allowing them to cope with harsh environments, including high temperatures.

• Genomics & Informatics
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• v.7 no.1
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• pp.26-31
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• 2009

Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell's danger signaling cascade. Heat shock protein, Hsp20 is a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria. It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species.

• Preventive Nutrition and Food Science
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• v.3 no.2
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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.

• 연구논문집
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• s.33
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• pp.17-25
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• 2003

In this work, thermal design of a PCR chip for LOC is systematically conducted. From the numerical simulation of a PCR chip based on the finite volume method, how to control the average temperature of a PCR chip and the temperature difference between the denaturation zone and the annealing zone is presented. The average temperature is shown to be controlled by adjusting heat input and a cooler as well as a heater is shown to be necessary to obtain three individual temperature zones for polymerase chain reaction. To reduce the time required, a heat sink for the cooler is not included in the calculation domain for the PCR chip and heat sink design is conducted separately by using a compact modeling method, the porous medium approach.