• 한국식품조리과학회지
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• 제24권3호
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• pp.304-311
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• 2008

This study examined Jeung-pyun(JP) Retrogradation in samples containing 3% whole protein, 7S protein, or 11S protein(w/w) that were stored at $4^{\circ}C$ for 6, 12, 24 and 72 hr. Rheometery and differential scanning calorimetry(DSC) were used in the analysis. The pH of the dough decreased during the fermentation process, but it increased after steaming. The JP prepared with soybean protein isolate(SPI) had higher pH than the control group. During storage the textural characteristics of the JP showed effects according to the additions of SPI. After 6 hr of storage, the JP samples containing soybean flour, whole protein, 7S protein, and 11S protein had lower hardness valuse. From 4 hr to 12 hr, higher springiness values were found in the samples containing whole protein, 7S protein and 11S protein. At 0 hr, the control group had the highest cohesiveness value, but after 24 hr it presented the lowest value. For gumminess, after 6 hr of storage, the control group offered the lowest value. Whereas after 12 hr of storage the whole protein group showed the highest value, and at 24 hr, the whole protein, 7S protein, and 11S protein groups had higher values. According to the DSC results, the 11S protein group had lower enthalpy values(${\bigtriangleup}H$) suggesting that adding 11S protein to JP might improve starch retrogradation. After 72 hr of storage, the control group had the highest onset temperature($T_{o}$) and peak temperature($T_{p}$) whereas the 7S and 11S protein JP samples had higher conclusion temperatures($T_{c}$). Therefore, based on the different analysis result between the control and treatment groups, the addition of SPI to Jp had effects on retrogradation.

• BMB Reports
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• 제41권3호
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• pp.217-222
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• 2008

Based on a five-letter model of the 20 amino acids, we propose a new 2-D graphical representation of protein sequence. Then we transform the 2-D graphical representation into a numerical characterization that will facilitate quantitative comparisons of protein sequences. As an application, we construct the phylogenetic tree of 56 coronavirus spike proteins. The resulting tree agrees well with the established taxonomic groups.

• Journal of Microbiology and Biotechnology
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• 제13권6호
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• pp.1018-1020
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• 2003

The complete 1,486 nucleotide sequence of a cryptic plasmid separated from Lactobacillus bifermentans strain A02 isolated from Kimchi has been determined. The plasmid, designated as pA021, encodes a 33,488 Da putative Rep protein. Based on the sequence similarity, the protein shows homology with coding protein of pRS1, a previously reported plasmid of Oenococcus oeni and the replication initiation protein (Rep) of the Staphylococcal pT181 plasmid family.

• 대한화장품학회:학술대회논문집
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• 대한화장품학회 2003년도 IFSCC Conference Proceeding Book I
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• pp.142-160
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• 2003

Most consumers have noted hair damage following coloring treatments. Proper evaluation of hair bleaching products must be performed using quantitative assessments of hair damage, though they are difficult, because of the slight fluctuations in hair composition. In the present study, we utilized a sensitive evaluation method for hair damage and found that the amount of soluble protein fraction extracted from hair under a reducing condition, termed labile protein, dramatically increased after bleaching.(omitted)

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2005년도 생물공학의 동향(XVII)
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• pp.737-738
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• 2005

• Journal of Plant Biology
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• 제36권3호
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• pp.301-304
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• 1993

Root nodule specific proteins of Alnus hirsuta were examined. SDS-PAGE pattern of the Alnus root nodule was simpler than that of soybean, showing five nodule specific proteins whose molecular weights were 48, 40, 36, 26 and 19 kD, respectively. Among them, 48 kD protein existed most abundantly and were composed of two subunits whose pI value were 4.0 and 4.3, respectively. The 48 kD protein seemed to be a heme containing protein based on reaction with diaminobenzidine. Although 19 kD protein was present in small amount, it was most similar to leghemoglobin in terms of its molecular weight.

• Journal of Dairy Science and Biotechnology
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• 제26권1호
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• pp.27-36
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• 2008

This review was written to introduce updated data on the structure and function of the major milk proteins identified as allergens, the characterization of their epitopes in each allergenic milk proteins, and the reduction of milk protein allergenicity. Most mammalian milk protein, even protein present at low concentration, are potential allergens. Epitopes identified in milk proteins are both conformational(structured epitope) and sequential epitopes(linear epitope), throughout the protein molecules. Epitopes on casein and whey proteins are reported to be sequential epitope and conformational epitopes, respectively. Conformational epitopes on whey protein are changed into sequential epitope by heat denaturation during heat treatment. Several methods have been proposed to reduce allergenicity of milk proteins. Most ideal and acceptable method to make hypoallergenic milk or formula, so far, is the hydrolysis of allergenic milk proteins by enzymes that has substrate specificity, such as pepsin, trypsin, or chymotrypsin. Commercial formulas based on milk protein hydrolysate are available for therapeutic purpose, hypoantigenic formula for infants from families with a history of milk allergy and hypoallergenic formula for infants with existing allergic symptoms.

• Bulletin of the Korean Chemical Society
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• 제31권5호
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• pp.1223-1227
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• 2010

In this study, the orientational behavior of thermotropic liquid crystals (LC) supported on a film of protein receptors was examined. Avidin was roller printed and covalently immobilized onto the surface of gold using NHS/EDC chemistry. The orientation of nematic 4-cyano-4'-pentylbiphenyl (5CB) was found to be parallel to the plane of the printed avidin surface before incubation with a solution of biotin. However, protein-receptor complexation induced a random orientation of 5CB, where protein-receptor complexes disturbed the nanoscale topography of the printed protein surface. Atomic force microscopy and ellipsometry was used to confirm printing and the specific interaction of proteins. These results demonstrate that the combination of LC and roller printing can be used to detect specific interactions between biomolecules by manipulating the orientational behavior of LC to the printed protein surfaces.

• Biotechnology and Bioprocess Engineering:BBE
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• 제6권4호
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• pp.212-230
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• 2001

Recent advances in recombinant DNA technology have resulted in development of many new protein drugs. Due to the unique properties of protein druges, they have to be delivered by parenteral injection Although delivery of protein drugs by other routes, such as pulmonary and nasal routes, has shown some promises, to date most protein drugs are administered by par-enteral routs. For long-term delivery of protein drugs by parenteral administration, they have been formulated into biodegradable microspheres. A number of microencapsulation methods have been developed, and the currently used microencapsulation methods are reviewed here, The microen-capsulation methods have been divided based on the method used. They are: solvent evapora-tion/extraction; phase separation (coacervation);spray drying; ionotropic gelation/polyelectrolyte complexation; interfacial polyumerization and supercritical fluid precipitation. Each method is de-scribed fro its applications, advantages, and limitations.

• 한국생물정보학회:학술대회논문집
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• 한국생물정보시스템생물학회 2005년도 BIOINFO 2005
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• pp.156-160
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• 2005

We introduce a fully automatic clustering method to classier candidate paralog clusters from a set of protein sequences within one genome. A set of protein sequences is represented as a set of nodes, each represented by the amino acid sequence for a protein with the sequence similarities among them constituting a set of edges in a graph of protein relationships. We use graph-based clustering methods to identify structurally consistent sets of nodes which are strongly connected with each other. Our results are consistent with those from current leading systems such as COG/KOG and KEGG based on manual curation. All the results are viewable at http://www.cs.rutgers.edu/${\sim}$seabee.