Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 13 de 13
Filter
Add more filters










Publication year range
1.
Acta Crystallogr E Crystallogr Commun ; 71(Pt 10): o719-20, 2015 Oct 01.
Article in English | MEDLINE | ID: mdl-26594441

ABSTRACT

The title compound, C6H12O6, was crystallized from an aqueous solution of equimolar mixture of d- and l-fructose (1,3,4,5,6-penta-hydroxy-hexan-2-one, arabino-hexulose or levu-lose), and it was confirmed that d-fructose (or l-fructose) formed ß-pyran-ose with a (2) C 5 (or (5) C 2) conformation. In the crystal, two O-H⋯O hydrogen bonds between the hy-droxy groups at the C-1 and C-3 positions, and at the C-4 and C-5 positions connect homochiral mol-ecules into a column along the a axis. The columns are linked by other O-H⋯O hydrogen bonds between d- and l-fructose mol-ecules, forming a three-dimensional network.

2.
Acta Crystallogr E Crystallogr Commun ; 71(Pt 5): o289-90, 2015 May 01.
Article in English | MEDLINE | ID: mdl-25995909

ABSTRACT

The title compound, C6H12O6, a C-3 position epimer of fructose, was crystallized from an aqueous solution of equimolar mixture of d- and l-psicose (1,3,4,5,6-penta-hydroxy-hexan-2-one, ribo-2-hexulose, allulose), and it was confirmed that d-psicose (or l-psicose) formed ß-pyran-ose with a (2) C 5 (or (5) C 2) conformation. In the crystal, an O-H⋯O hydrogen bond between the hy-droxy groups at the C-3 and C-2 positions connects homochiral mol-ecules into a column along the b axis. The columns are linked by other O-H⋯O hydrogen bonds between d- and l-psicose mol-ecules, forming a three-dimensional network. An intra-molecular O-H⋯O hydrogen bond is also observed. The cell volume of racemic ß-d,l-psicose [763.21 (6) Å(3)] is almost the same as that of chiral ß-d-psicose [753.06 Å(3)].

3.
Acta Crystallogr E Crystallogr Commun ; 71(Pt 2): o139, 2015 Feb 01.
Article in English | MEDLINE | ID: mdl-25878872

ABSTRACT

The title compound, C6H12O6, a C-3 position epimer of glucose, was crystallized from an equimolar mixture of d- and l-allose. It was confirmed that d-allose (l-allose) formed ß-pyran-ose with a (4) C 1 ((1) C 4) conformation in the crystal. In the crystal, molecules are linked by O-H⋯O hydrogen bond, forming a three-dimensional framework. The cell volume of the racemic ß-d,l-allose is 739.36 (3) Å(3), which is about 10 Å(3) smaller than that of chiral ß-d-allose [V = 751.0 (2) Å(3)].

4.
Acta Crystallogr E Crystallogr Commun ; 71(Pt 12): o993-4, 2015 Dec 01.
Article in English | MEDLINE | ID: mdl-26870568

ABSTRACT

The title compound, C6H12O5, was crystallized from an aqueous solution of 6-de-oxy-l-psicose (6-de-oxy-l-allulose, (3S,4S,5S)-1,3,4,5-tetra-hydroxy-hexan-2-one), and the mol-ecule was confirmed as α-furan-ose with a (3) T 4 (or E 4) conformation, which is a predominant tautomer in solution. This five-membered furan-ose ring structure is the second example in the field of the 6-de-oxy-ketohexose family. The cell volume of the title compound [742.67 (7) Å(3), Z = 4 at room temperature] is only 1.4% smaller than that of ß-d-psico-pyran-ose, C6H12O6 (753.056 Å(3), Z = 4 at room temperature).

5.
Acta Crystallogr Sect E Struct Rep Online ; 70(Pt 5): o569, 2014 May 01.
Article in English | MEDLINE | ID: mdl-24860374

ABSTRACT

The title compound, C6H12O6, a C-3 position epimer of d-galactose, crystallized from an aqueous solution, was confirmed as ß-d-pyran-ose with a (4) C 1 (C1) conformation. In the crystal, O-H⋯O hydrogen bonds between the hy-droxy groups at the C-1 and C-6 positions connect mol-ecules into a tape structure with an R 3 (3)(11) ring motif running along the a-axis direction. The tapes are connected by further O-H⋯O hydrogen bonds, forming a three-dimensional network.

6.
J Oleo Sci ; 60(8): 419-27, 2011.
Article in English | MEDLINE | ID: mdl-21768743

ABSTRACT

Various protein solutions were studied in order to quantify the emulsifying activity of proteins, and to explore oil-water interfacial tension, oil particle size analysis, and oil phase separation behaviors in protein-stabilized oil-in-water (O/W) emulsions. Three proteins, bovine serum albumin (BSA), ß-lactoglobulin (ß-lg), and ß-casein (ß-ca), were employed to disperse hexadecane in various pH and ionic strength solutions in a wide range of oil-water ratios. It was confirmed that the volume mean oil droplet diameter, d(43), changed depending on the oil content, the pH, the ionic strength, and the used protein. In a dilute protein solution (0.01 %) at pH 7, droplet size increased with oil content in so-called surfactant-poor regimes (e.g., above 5%, 10%, and 20% oil content for BSA, ß-lg, and ß-ca emulsion, respectively) but remained constant at ca. 10 mm, 6 mm, and 20 mm, respectively, in lower oil content surfactant-rich regimes. In surfactant-poor regimes, the most important factor determining the oil drop size was the threshold amount of protein adsorption onto the oil-water interface. In surfactant-rich regimes, on the other hand, it is suggested that drop size may be governed mainly by the mechanical strength of protein films covering the oil drops during emulsification, and this was quantified by the critical osmotic pressure, P(CR). In this study, the P(CR) was measured conveniently in the oil phase separation experiments for protein-stabilized emulsions using analytical photo-centrifugal apparatus. The correlation between the P(CR) and oil droplet size prepared by emulsification at different pH and ionic strength media is discussed.


Subject(s)
Centrifugation/methods , Emulsions/chemistry , Photochemistry/methods , Proteins/chemistry , Animals , Buffers , Caseins/chemistry , Cattle , Hydrogen-Ion Concentration , Lactoglobulins/chemistry , Oils/chemistry , Osmolar Concentration , Protein Stability , Serum Albumin, Bovine/chemistry , Sodium Chloride/chemistry , Surface Tension , Time Factors
7.
J Agric Food Chem ; 56(12): 4789-96, 2008 Jun 25.
Article in English | MEDLINE | ID: mdl-18517216

ABSTRACT

d-Psicose (Psi) might be an ideal sucrose (Suc) substitute for food products due to its sweet taste, easy processing, and functional properties (noncaloric and low glycemic response). In the present study, the effects of Psi on foaming properties of egg white (EW) protein and the quality of butter cookies were analyzed to find a better use of Psi in aerated food systems. The results showed that Psi could improve the foaming properties of EW protein with increasing whipping time in comparison to Suc and d-fructose (Fru). The addition of Psi to butter cookies, as partial replacement of Suc, had no influence on the cook loss while significantly contributing to a color change of the cookie crust through a nonenzymatic browning reaction. Furthermore, Psi-containing cookies possessed the highest antioxidant capacity in all tested cookies using two assays of radical scavenging activity and ferric reducing power. It was found that there was a close correlation between the crust color and the antioxidant activity of the cookie. The results suggest that the addition of Psi enhanced the browning reaction during cookie processing and, consequently, produced a strong antioxidant activity.


Subject(s)
Egg Proteins, Dietary/analysis , Fructose/pharmacology , Antioxidants/analysis , Butter , Chemical Phenomena , Chemistry, Physical , Cooking , Food Technology , Maillard Reaction , Viscosity
8.
J Colloid Interface Sci ; 316(2): 779-86, 2007 Dec 15.
Article in English | MEDLINE | ID: mdl-17897667

ABSTRACT

Bovine serum albumin (BSA) was used as an emulsifier to disperse corn oil in aqueous media with various protein concentration, pH, and ionic strength. Quantitative estimation was made on the homogenizing activity of BSA and dispersion stability of oil particles by measuring particle size, turbidity, and creaming rate. Dispersion stability strongly depended on pH and became a minimum around pH 5.0 which was the isoelectric point of BSA. The interfacial tension between BSA solution and corn oil was minimized at pH 5.0. Interesting results were obtained concerning the ionic-strength dependence of stability. When the ionic strength was set below 30 mM, the emulsions became more stable with the increase of BSA concentration at pH 6.7 but the opposite behavior (enhanced destabilization) was confirmed at pH 5.0 with the BSA content. In high ionic strength conditions (ca. > or = 80 mM NaCl), however, BSA-stabilized emulsions became fairly stable even at pH 5.0. These results suggested that BSA molecules having no net charge induced some attractive interactions (e.g., bridging or depletion) in low ionic strength but steric stabilization in high ionic strength, respectively.


Subject(s)
Corn Oil/chemistry , Proteins/chemistry , Serum Albumin, Bovine/chemistry , Animals , Cattle , Emulsions , Hydrogen-Ion Concentration , Osmolar Concentration , Particle Size , Sodium Chloride/chemistry , Solutions/chemistry , Surface Properties , Water/chemistry
9.
Biochem Biophys Res Commun ; 357(4): 1166-71, 2007 Jun 15.
Article in English | MEDLINE | ID: mdl-17466271

ABSTRACT

The effect of celecoxib, a cyclooxygenase-2 selective inhibitor, on a human cervical cancer cell line, HeLa cells, was examined. We found that celecoxib increased DNA ladder formation and the activity of caspase-3, indicating that celecoxib induced apoptosis in HeLa cells. Celecoxib suppressed the expression of an anti-apoptotic protein, survivin, in both protein and mRNA levels. The overexpression of survivin overrode caspase-3 activation induced by celecoxib. Subsequently, we performed luciferase reporter assay with the reporter vector containing human survivin promoter region and electrophoretic mobility shift assay and found that the -75 to -66 bp region relative to the initiating codon played an important role in celecoxib action to suppress survivin promoter activity. Our findings might provide a new insight into the anti-cancer effects of celecoxib.


Subject(s)
Apoptosis/drug effects , Gene Expression Regulation/drug effects , Gene Expression/drug effects , Microtubule-Associated Proteins/metabolism , Neoplasm Proteins/metabolism , Pyrazoles/administration & dosage , Signal Transduction/drug effects , Sulfonamides/administration & dosage , Celecoxib , HeLa Cells , Humans , Inhibitor of Apoptosis Proteins , Survivin
10.
Biochem Pharmacol ; 73(9): 1318-29, 2007 May 01.
Article in English | MEDLINE | ID: mdl-17270149

ABSTRACT

We investigated the effect of nonsteroidal anti-inflammatory drugs (NSAIDs) on human colon cancer cell lines to clarify the mechanisms underlying the chemopreventive effect of NSAIDs. Celecoxib, a selective cyclooxygenase-2 (COX-2) inhibitor, induced apoptosis and strongly reduced the expression of an anti-apoptotic protein, survivin, in both protein and mRNA levels in HCT-116 cells. Subsequently, we conducted luciferase reporter assay using a reporter gene driven by the human survivin promoter. A series of analyses using luciferase reporter constructs containing fragments of the survivin promoter and electrophoretic mobility shift assay indicated that the -75/-66 bp region relative to the initiating codon was involved in celecoxib action to suppress survivin promoter activity. Celecoxib also suppressed the activity of TOPflash, T-cell factor reporter plasmid, and the reporter gene driven by the human cyclin D1 promoter, suggesting that this compound inhibited the expression of Wnt/beta-catenin signaling target genes. Further, we found that other NSAIDs including indomethacin, resveratrol, and SC-560 induced apoptosis and suppressed the expression of survivin and the Wnt/beta-catenin signaling pathway in HCT-116 cells, indicating that these effects were likely to be common among NSAIDs. Moreover, NSAIDs (celecoxib, SC-560 and indomethacin) also suppressed the expression of cyclin D1 and survivin on other colon cancer cell lines (DLD-1 and SW-620). Our results suggested that NSAIDs could inhibit proliferation and induce apoptosis in colon cancer cells by inhibition of survivin expression and the Wnt/beta-catenin signaling pathway.


Subject(s)
Colonic Neoplasms/pathology , Gene Expression/drug effects , Microtubule-Associated Proteins/metabolism , Neoplasm Proteins/metabolism , Promoter Regions, Genetic/drug effects , Pyrazoles/pharmacology , Sulfonamides/pharmacology , Anti-Inflammatory Agents, Non-Steroidal/pharmacology , Celecoxib , Cyclin D1/metabolism , Humans , Inhibitor of Apoptosis Proteins , Microtubule-Associated Proteins/antagonists & inhibitors , Microtubule-Associated Proteins/genetics , Neoplasm Proteins/antagonists & inhibitors , Neoplasm Proteins/genetics , RNA, Messenger/metabolism , Signal Transduction/drug effects , Survivin , TCF Transcription Factors/metabolism , Tumor Cells, Cultured , Wnt Proteins/metabolism , beta Catenin/genetics , beta Catenin/metabolism
11.
Langmuir ; 21(13): 5731-7, 2005 Jun 21.
Article in English | MEDLINE | ID: mdl-15952816

ABSTRACT

Lyotropic phase behavior of the nonionic and the half-ionized oleyldimethylamine oxide (OlDMAO)/water systems was investigated using polarized light microscopy, small-angle X-ray diffraction, and differential scanning calorimetry. Nonionic OlDMAO formed isotropic micellar solution, nematic, hexagonal, cubic, and lamellar liquid crystalline phases as the surfactant concentration increased. In contrast, half-ionized OlDMAO (i.e., 1:1 mixture of the nonionic and the protonated species) had a greater tendency to form bilayer structures, and the phase diagram became quite similar to those of double-chained ionic surfactants rather than single-chained ones, despite the introduction of positive charges to the nonionic one. The preference of the bilayer structures in the half-ionized OlDMAO was interpreted in terms of the dimers stabilized by the hydrogen bond between the nonionic and protonated species. For alkyldimethylamine oxides with a saturated hydrocarbon chain (CnDMAO, chain length: n = 14, 16, and 18), the phase sequence of lyotropic liquid crystals was hardly affected by the protonation, but an elongation of the cylinders of the hexagonal phase was observed for the half-ionized C14DMAO. Consequently, it can be considered that the dominant bilayer formation of the half-ionized OlDMAO is attributed to the combined effect of the hydrogen-bonded dimer formation and the cis-double-bond configuration of the alkyl chain.

12.
J Colloid Interface Sci ; 268(1): 121-6, 2003 Dec 01.
Article in English | MEDLINE | ID: mdl-14611780

ABSTRACT

Dielectric measurements were carried out on suspensions of montmorillonite clay exchanged with three different counterions: sodium, ammonium, and tetramethylammonium (TMA). Only two dielectric absorption peaks could be identified for the clay sample with the TMA counterion, whereas three peaks were found for the two inorganic counterions. The dielectric process observed at around 10 GHz is due to the orientation of bulk water molecules, judging from the relaxation time and relaxation strength. The relaxation strength of the process occurring at around 10 MHz was compared with the coefficient of adiabatic compressibility obtained from ultrasound velocity measurements. The increase in the relaxation strength with decreasing compressibility indicates that the process at around 10 MHz is caused by the orientation of bound water molecules on the clay samples. The relaxation strength of the process occurring at around 10 MHz for the TMA sample was remarkably small. Furthermore, the network structure of the bound water molecules can be characterized by a property peculiar to the TMA sample, taking into account the value of its Cole-Cole parameter. Results for the relaxation strength of the process occurring at around 100 kHz were compared with those for electrophoretic mobility. This comparison revealed that discrimination between bound ions and ions in the diffuse double layer is important, and both the relaxation and electrophoretic results could be satisfactorily explained by surface polarization of the clay.

13.
J Agric Food Chem ; 51(17): 5154-61, 2003 Aug 13.
Article in English | MEDLINE | ID: mdl-12903984

ABSTRACT

The structural and antimicrobial functions of lysozyme reduced with food-compatible reducing agents-cysteine (Cys) and glutathione (GSH)-were investigated. The disulfide bonds were partially reduced by thiol-disulfide exchange reactions under heat-induced denaturing conditions from 55 to 90 degrees C. The results showed that treatment of lysozyme with Cys and GSH resulted in the introduction of new half-cystine residues (2-3 residues/mol of protein). The released SH groups, in turn, rendered the lysozyme molecule more flexible, being accompanied by a dramatic increase in the surface hydrophobicity and exposure of tryptophan residues. As a consequence, the resulting reduced lysozymes were more capable of binding to lipopolysaccharides (LPS) and permeabilizing the bacterial outer membrane, as evidenced by the liposome leakage experiment, than were native or heated lysozyme. Both reduced lysozymes displayed significantly higher antimicrobial activity than native or heated lysozyme against Salmonella enteritidis (SE) in sodium phosphate buffer (10 mM, pH 7.2) at 30 degrees C for 1 h. Their minimal inhibitory concentrations (MICs) against the tested bacteria were about 150- and 25-fold lower than their respective MICs of native or heated lysozyme. The results suggest that partially reduced lysozyme could be used as a potential antimicrobial agent for prevention of SE attack.


Subject(s)
Anti-Bacterial Agents/chemistry , Anti-Bacterial Agents/pharmacology , Food Additives , Muramidase/chemistry , Muramidase/pharmacology , Anti-Bacterial Agents/metabolism , Cysteine/chemistry , Glutathione/chemistry , Hot Temperature , Lipopolysaccharides/metabolism , Muramidase/metabolism , Oxidation-Reduction , Salmonella enteritidis/drug effects , Spectrometry, Fluorescence , Tryptophan/chemistry
SELECTION OF CITATIONS
SEARCH DETAIL
...