• Journal of Microbiology and Biotechnology
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• v.16 no.6
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• pp.983-987
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• 2006

The sole use of the glucanhydrolase (exhibiting both dextranase and amylase activities) from Lipomyces starkeyi hydrolyzed the soluble polysaccharides in sugar syrup more efficiently than a mixed treatment using both commercial dextranase and amylase. The glucanhydrolase treatment of stale sugar cane juice resulted in a yield of square, light-colored sugar crystals.

• Journal of the Korean Applied Science and Technology
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• v.34 no.3
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• pp.545-554
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• 2017

This study is concerned with the stability of liquid crystal forming emulsifier with localized depend on change of pH using liquid crystal forming agent of advanced company. The liquid crystal emulsifying agent was localized using Sugar Crystal-LC (bio-tech Co., Ltd., Korea), and comparative samples were measured by using Nikkomulese-LC (Nikko Camicarls, Japan) and Alacel-LC (Croda Camicarls, UK). Liquid crystal formation was confirmed microscopically to show the formation of liquid crystal structure at acidic (pH=4.2), neutral (pH=7.0) and alkaline (pH=11.7). The particles of the liquid crystal were observed with a polarizing microscope according to the stirring speed. The stirring time was all the same for 3 minutes with a homo-mixer, and the stirring speed was increased to 2500 rpm, 3500 rpm and 4500 rpm to observe the liquid crystal state. As a result, it was found that the Korean surfactant was more stable and clear liquid crystal structure was formed than the two foreign acids. In the case of the UK in acid zone, the emulsion particle size was uniform and unstable. In the case of Japanese surfactant, it has similar structure and performance to those of localized Korean. It was found that Korean surfactant had superior emulsifying performance in acid zone compared with foreign products. It is possible to develop various formulations such as liquid crystal cream, lotion, eye cream, etc. using Sugar Crystal-LC emulsifier as an application cosmetic field, and it is expected that it can be widely applied as emulsifying technology for skin care external application in the pharmaceutical industry and the pharmaceutical industry as well as the cosmetics industry.

• Bulletin of the Korean Chemical Society
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• v.33 no.6
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• pp.2028-2030
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• 2012

The single-crystal structure of $CaCl_2{\cdot}2C_6H_{12}O_6{\cdot}3H_2O$ was determined with Mr=525.34, a=16.054(7) ${\AA}$, b=7.864(4) ${\AA}$, c=10.909(5) ${\AA}$, ${\beta}=127.894(8)^{\circ}$, V=1086.9(9) ${\AA}^3$, C2, Z=2 and $R$=0.0227 for 1727 observed reflections. The fructose moiety of the complex exists as a ${\beta}$-D-pyranose. The calcium ion is surrounded by eight oxygen atoms, These are arranged in symmetry-related pairs derived from four sugar and two water molecules. Three nonvicinal hydroxyl groups of fructose are involved in calcium binding. All the hydroxyl groups and water molecules are involved in forming an extensive hydrogen-bond network.

• BMB Reports
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• v.41 no.1
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• pp.48-54
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• 2008

PM0188 is a newly identified sialyltransferase from P. multocida which transfers sialic acid from cytidine 5'-monophosphonuraminic acid (CMP-NeuAc) to an acceptor sugar. Although sialyltransferases are involved in important biological functions like cell-cell recognition, cell differentiation and receptor-ligand interactions, little is known about their catalytic mechanism. Here, we report the X-ray crystal structures of PM0188 in the presence of an acceptor sugar and a donor sugar analogue, revealing the precise mechanism of sialic acid transfer. Site-directed mutagenesis, kinetic assays, and structural analysis show that Asp141, His311, Glu338, Ser355 and Ser356 are important catalytic residues; Asp141 is especially crucial as it acts as a general base. These complex structures provide insights into the mechanism of sialyltransferases and the structure-based design of specific inhibitors.

• Molecules and Cells
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• v.27 no.1
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• pp.99-103
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• 2009

Ribose-5-phosphate isomerase A (RpiA) plays an important role in interconverting between ribose-5-phosphate (R5P) and ribulose-5-phosphate in the pentose phosphate pathway and the Calvin cycle. We have determined the crystal structures of the open form RpiA from Vibrio vulnificus YJ106 (VvRpiA) in complex with the R5P and the closed form with arabinose-5-phosphate (A5P) in parallel with the apo VvRpiA at $2.0{\AA}$ resolution. VvRpiA is highly similar to Escherichia coli RpiA, and the VvRpiA-R5P complex strongly resembles the E. coli RpiA-A5P complex. Interestingly, unlike the E. coli RpiA-A5P complex, the position of A5P in the VvRpiA-A5P complex reveals a different position than the R5P binding mode. VvRpiA-A5P has a sugar ring inside the binding pocket and a phosphate group outside the binding pocket: By contrast, the sugar ring of A5P interacts with the Asp4, Lys7, Ser30, Asp118, and Lys121 residues; the phosphate group of A5P interacts with two water molecules, W51 and W82.

• Korean Journal of Food Science and Technology
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• v.21 no.1
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• pp.75-79
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• 1989

The rheological properties of sugar and cocoa particle suspensions in cocoa butter under molten condition were analyzed with Haake rotationary viscometer. Both suspensions had yield value and showed rheopexy at low shear rate and thixotropy at high shear rate. Flow behaviors of the suspensions were analyzed with modified Casson model. Casson viscosity and yield value increased with increasing the concentration of sugar and cocoa particles. There was an obvious dependence of the Casson viscosity and yield value on the particle size distributions that was represented by the Sauter mean diameter of the particles. Casson viscosity and yield value of cocoa butter-sugar suspension increased with increasing the fineness of sugar particle crystal. With increasing the fineness of cocoa particle a decreasing Casson viscosity of cocoa butter-cocoa particle suspension was achieved, but the yield value did not change significantly with cocoa particle size. Therefore, it was predicted that the best rheological properties of chocolate could be obtained with the combination of coarse ground sugar $(d=36.30{\mu}m)$ and fine ground cocoa particle $(d=14.81{\mu}m)$ within the studied range.

• Food Science and Biotechnology
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• v.15 no.5
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• pp.721-727
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• 2006

This study was carried out to investigate the effect of hydrocolloids on the changes in physical properties of a model ice cream. The model ice cream contained water, sugar, skin milk powder, com oil, and 4 different hydrocolloid stabilizers (gelatin, pectin, hydroxyethylstarch, locust bean gum), was manufactured in a batch type freezer. The following physical characteristics of ice cream were examined: flow behavior, overrun, air cell size, ice crystal size, and melt resistance. With regard to flow behavior, all of aged mixes had a lower apparent viscosity relative to the mix before aging, and ice cream mix containing locust bean gum had the highest viscosity. Air cell size was observed to range from 20 to $38\;{\mu}m$, and ice cream with locust bean gum showed the largest size. There was an inverse correlation between overrun and air cell size. The ice crystal sizes of all samples ranged from 25 to $35\;{\mu}m$. Ice cream with added pectin contained the smallest ice crystal size, which was significantly difference from other stabilizers (p<0.05), and resulted in superior melt resistance with increased melting time compared to other samples.

• Journal of Microbiology and Biotechnology
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• v.19 no.11
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• pp.1421-1430
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• 2009

With an aim to evaluate dye decolorization by white rot fungus on natural living conditions, reproducing by solid-state fermentation, the process of triphenylmethane dyes decolorization using the white rot fungus P. ostreatus BP, cultivated on rice straw solid-state medium, has been demonstrated. Three typical dyes, including malachite green, bromophenol blue, and crystal violet, were almost completely decolorized by the fungus after 9 days of incubation. During the process of dye decolorization, the activities of enzyme secreted by the fungus, and the contents of soluble components, such as phenolic compounds, protein, and sugar, changed regularly. The fungus could produce ligninolytic, cellulolytic, and hemicellulolytic enzymes and laccase was the most dominant enzyme in solid-state medium. Laccase, laccase isoenzyme, and the laccase mediator could explain the decolorization of malachite green, bromophenol blue, and crystal violet by the fungus in solid-state medium, respectively. It is worth noting that the presence of the water-soluble phenolic compounds could stimulate the growth of fungus, enhance the production of laccase, and accelerate dye decolorization.

• Ocean and Polar Research
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• v.33 no.2
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• pp.159-169
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• 2011

Antifreeze proteins (AFPs) have ice binding affinity, depress freezing temperature and inhibit ice recystallization which protect cellular membranes in polar organisms. Recent structural studies of antifreeze proteins have significantly expanded our understanding of the structure-function relationship and ice crystal growth inhibition. Although AFPs (Type I-IV AFP from fish, insect AFP and Plant AFP) have completely different fold and no sequence homology, they share a common feature of their surface area for ice binding property. The conserved ice-binding sites are relatively flat and hydrophobic. For example, Type I AFP has an amphipathic, single ${\alpha}$-helix and has regularly spaced Thr-Ala residues which make direct interaction with oxygen atoms of ice crystals. Unlike Type I AFP, Type II and III AFP are compact globular proteins that contain a flat ice-binding patch on the surface. Type II and Type III AFP show a remarkable structural similarity with the sugar binding lectin protein and C-terminal domain of sialic acid synthase, respectively. Type IV is assumed to form a four-helix bundle which has sequence similarity with apolipoprotein. The results of our modeling suggest an ice-binding induced structural change of Type IV AFP. Insect AFP has ${\beta}$-helical structure with a regular array of Thr-X-Thr motif. Threonine residues of each Thr-X-Thr motif fit well into the ice crystal lattice and provide a good surface-surface complementarity. This review focuses on the structural characteristics and details of the ice-binding mechanism of antifreeze proteins.

• Bulletin of the Korean Chemical Society
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• v.14 no.2
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• pp.200-206
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• 1993

Structures of two polymorphs of ${\alpha},{\alpha}$-trehalose octaacetate monohydrate, $C_{28}H_{38}O_{19}\;{\cdot}\;H_2O$, have been studied by X-ray diffraction method. ${\alpha},{\alpha}$-trehalose (${\alpha}$-D-glucopyranosyl ${\alpha}$-D-glucopyranoside) is a nonreducing disaccharide. The polymorph I belongs to the monoclinic $P2_1$, and has unit cell parameters of a=10.725(l), b=15.110(4), c=11.199(5) ${\AA}$, ${\beta}=108.16(2)^{\circ}$ and Z=2. The polymorph II is orthorhombic $P2_12_12_1$, with a=13.684(4), b=15.802(4), c=17.990(9) ${\AA}$ and Z=4. The final R and R$_w$ values for monoclinic polymorph I are 0.043 and 0.048 and for orthorhombic polymorph II are 0.116 and 0.118, respectively. Those R values of polymorph II are high because the large thermal motions of acetyl groups and the poor quality of the crystal. The molecular conformations in the two polymorphs are similar. Both D-glucopyranosyl rings have chair $^4C_1$ conformations and atoms of glycosidic chain ${\alpha}(1{\rightarrow}1)$ linkage are coplanar. The primary acetate groups of the pyranose residues assume both gauche-trans conformations. The molecules of two polymorphs have pseudo-C$_2$ symmetry at glycosidic O(1) atom. The bond lengths and angles are normal compared with those in other acetylated sugar compounds. The molecules in the monoclinic crystal are held by the hydrogen bonds with the water molecules and by van der Waals forces.