Biomedical subjects

Hideshi Seki

Publications and source records attributed to Hideshi Seki.

9 recordsLinked to original sources

PubMed2006

Batch foam separation of a soluble protein.

Removal of protein dissolved in water by batch foam separation was conducted with using ovalbumin (OA) as a model protein in the light of wastewater treatment reducing organic loading. The removal efficiency had a maximum value near the i.e.p. of OA (pH 4.6); thus, most experiments were conducted at pH 4.6. Typical experimental conditions; superficial gas velocity, U(g): 1.97 x 10(-2)-5.37 x 10(-2)cm/s; initial bulk concentration of OA, C(i): ca. 0.05-0.25 g/L; liquid volume, V: 600 cm(3). A model estimating bulk concentration profile was proposed by taking into account a mass balance of the present system. The model predicted that OA could be removed perfectly, however, was not all removed experimentally. The residual OA concentration of the bulk liquid within the column reached plateau value, which correspond to ca. 18% of the initial OA concentration. The plateau value of the bulk concentration was attained for ca. 100-500 min with U(g)=1.97 x 10(-2)-5.37 x 10(-2)cm/s. Foaming ability test revealed that the foaming limit concentration of OA at pH 4.6 was 9.72 x 10(-3)g/L. These results suggested that OA molecules could be damaged by interaction of bubble surface in the dispersed phase, since there were the residual OA concentrations over the limit concentration. To take account of this phenomena and correct the model, average surface density, X(d), which should convert protein molecule into the denatured protein molecule, was introduced. The corrected model could explain well the time profile of OA bulk concentration.

Hydrogen-Ion Concentration↗

PubMed2006

Variation of saturated surface density of ovalbumin on bubble surface in continuous foam separation.

The adsorption of ovalbumin (OA) onto the bubble surfaces was studied with various pHs (3.5, 4.6, 6.0 and 8.0) by a continuous foam separation technique. From the value of the saturated surface density of adsorbed OA, the variation of effective diameter (D) of an OA molecule on the bubble surface was estimated for various pHs (3.5, 4.6, 6.0 and 8.0) of the OA solutions, assuming that the cross section of the OA molecules be circular and that the OA molecules adsorb on the bubble surface in a closest packing structure. The estimated variation of D with pH was attempted to explain based on a model modified from that proposed by Pujar and Zydney. The modified model could well reproduce the variation of the effective diameter with pH; the values of D calculated on the basis of the modified model almost agreed with that estimated from the saturated surface density in the present experimental pH range. From these, conclusion was drawn that the modified model presented in this study can express the variation in the effective diameter with pH.

Adsorption↗

PubMed2005

Biosorption of chromium(VI) and arsenic(V) onto methylated yeast biomass.

Yeast biomass was methylated in a 0.1 M HCl methyl alcohol solution at room temperature and the methylated yeast (MeYE) was applied to the adsorptive separation of Cr(VI) and As(V) anions from aqueous solutions. At near-neutral pH, while Cr(VI) and As(V) anions were scarcely adsorbed onto unmethylated yeast biomass, the amounts adsorbed increased with increasing methylation degree. The amount of Cr(VI) adsorbed onto MeYE was almost constant at pH 4-6 and decreased with increasing pH above pH 6. The amount of As(V) adsorbed onto MeYE was rather lower than that of Cr(VI) and it had a peak at about pH 7. A metal-binding model was used to describe the adsorption characteristics of Cr(VI) and As(V) on MeYE. The results showed that MeYE has two different types of adsorption sites. The saturated amount of Cr(VI) and As(V) adsorbed onto MeYE having methylation degree 0.94 was 0.55 mmol g(-1).

Adsorption↗

PubMed2004

Flocculation of diatomite by methylated milk casein in seawater.

A new biodegradable flocculant was prepared from a common and inexpensive protein. Milk casein was methylated in a 0.05 M HCl methyl alcohol solution at room temperature. The methylated milk casein (MeCS), having a methylation degree of 81%, was applied to the separation or flocculation of diatomite in seawater (pH 8.1+/-0.1) at room temperature (18-23 degrees C). The flocculating ability of MeCS was evaluated by a sedimentation balance method (cumulative measurement method). The diatomite suspension was effectively flocculated by the addition of a small amount of MeCS (0.25 wt% of the diatomite weight). The results of sedimentation analysis showed that the size-frequency curve had a very sharp and high peak; thus the diatomite floc formed by MeCS had a rather uniform size. The settling velocity of diatomite floc at the appropriate MeCS dosages (0.25-2 wt% of diatomite) was about 3 x 10(-3) ms(-1).

Animals↗

PubMed2004

Adsorption of egg albumin onto methylated yeast biomass.

A new biosorbent, methylated yeast (MeYE), was prepared for the adsorptive separation of proteins from aqueous solutions. Yeast was methylated in a 0.1 M HCl methyl alcohol solution at room temperature. About 80% of the carboxylic groups of yeast could be methylated within 9 h. The adsorption of egg albumin onto MeYE was studied to evaluate the protein adsorption ability of MeYE. At near neutral pH, egg albumin was scarcely adsorbed onto unmethylated yeast and the adsorbed amount of egg albumin increased with increasing methylation degree. The amount of egg albumin adsorbed onto MeYE increased with increasing pH from 4 to 7 and steeply decreased above pH 7. The Langmuir isotherm was applied to determine the apparent adsorption constant and the saturated adsorbed amount of egg albumin on MeYE. Both the apparent adsorption constant and the saturated adsorbed amount increased with the degree of methylation. The saturated adsorbed amount of egg albumin onto MeYE having methylation degree 77% was 8.41 x 10(-6) mol g(-1) or 0.378 gg(-1) at near neutral pH.

Adsorption↗

PubMed2003

Flocculation of diatomite by methylated egg albumin.

A common and inexpensive protein, egg albumin, was applied to the solid-liquid separation or flocculation of diatomite. Egg albumin was methylated in a 0.05 M HCl methyl alcohol solution at room temperature. About 90% of the carboxylic groups of egg albumin could be methylated within 24 h. The adsorption of egg albumin onto diatomite at pH 6.8 was remarkably enhanced by methylation. The adsorption constant of methylated egg albumin to diatomite at 30 degrees C was about 100-fold larger than that of native egg albumin; however, the adsorption constant of methylated egg albumin decreased to about 1/100 with temperature decreasing from 30 to 6 degrees C. The saturated adsorption amount of egg albumin was also increased by the methylation. The flocculating ability of methylated egg albumin was examined with a diatomite suspension at 6 and 30 degrees C in the pH range from pH 2 to 11. The diatomite suspension was effectively flocculated by the addition of small amounts of methylated egg albumin (only 0.5-1 wt% against diatomite) over a wide pH range from pH 3 to 10.

Adsorption↗

PubMed2002

Selective foam separation of binary protein solution by SDS complexation method.

A fundamental study about the selective foam separation of protein mixture was carried out. A solution containing two proteins, ovalbumin (OA) and lysozyme (LZ), and an anionic surfactant, sodium dodecyl sulfate (SDS), was adjusted to pH 6.0, which referred to an intermediate state between the isoelectric points of the proteins. The solution was processed by continuous foam separation. The results showed that a proper addition of SDS greatly improved the selective recovery of LZ to OA. The experimental data were well explained by a simple model that most of cationic protein molecules (LZ) are associated with SDS and the adsorption of all the species including LZ-SDS complexes are subjected to Langmuir adsorption isotherm. The results also showed that one of the Langmuir parameters, which means a kind of lyophillic property of adsorbed material, of LZ-SDS complexes was extremely large as compared with that of primary protein.

Absorption↗

PubMed2002

Adsorption of heavy metal ions to floc-type biosorbents.

Adsorption of cadmium and lead ions to floc-type biosorbents was reported in this work. Two types of biosorbents containing a marine microalga, Heterosigma akashiwo (Hada) Hada, or a purple non-sulfur bacterium, Rhodobacter sphaeroides, were prepared. The micro-organisms inactivated by steam sterilization were immobilized in casein floc and cross-linked with glutaraldehyde. In the present immobilizing method, we obtained the biosorbents comprising as much as 67% of micro-organism on a dry-weight basis. Simple metal-binding models were applied to explain the adsorption mechanism of bivalent metal ions to the biosorbents. The results showed that casein acted as both the immobilizing material and the adsorbent material. The adsorption of bivalent metal ions to the biosorbents was due to bidentate binding to the acidic sites on casein and monodentate binding to the acidic sites on micro-organisms. The metal-binding constants and the binding capacities of micro-organisms were scarcely influenced by immobilization.

Adsorption↗

PubMed2002

Kinetic study of metal biosorption to a brown alga, Kjellmaniella crassiforia.

A kinetic study of cadmium and lead biosorption to a brown alga, Kjellmaniella crassiforia, was carried out. The shrinking core model derived by M. Gopala Rao and A. K. Gupta (Chem. Eng. J.24, 181, (1982)) was modified and adapted for description of the rate process of cadmium and lead biosorption to the alga. The biosorption rate process was well described and average apparent diffusion coefficient of about 9 x 10(-6) cm(2) s(-1) was found for both cadmium and lead ions. The value was 20 to 50 times higher than the apparent diffusion coefficients of cadmium and lead ions in strong-acid resins like Dowex 50W-X8.

Adsorption↗