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Kashihara, Japan

Takahara J.-I.,Nara Institute of Science and Technology | Hosoya K.,Ezaki Glico Co. | Sunako M.,Sanwa Cornstarch Co. | Hirohara S.,Nara Institute of Science and Technology | And 3 more authors.
Acta Biomaterialia

Heparin is an extracellular matrix polysaccharide. It is widely employed as an anticoagulant and can be used to form an anticoagulant surface on various medical devices such as renal dialysis devices to prevent thrombosis. However, heparin may cause hemorrhage and thrombocytopenia. Moreover, commercially available heparin may be contaminated with viruses and allergens of animal origin, as it is derived mainly from porcine or bovine tissue. To avoid these problems, we prepared succinated and sulfonated enzymatically synthesized amylose (SucESA and SulfESA, respectively) and assessed their anticoagulant activity. SucESA and SulfESA inhibited factor Xa activity in normal human plasma to an equal extent. However, SucESA strongly inhibited thrombin activity, whereas SulfESA only inhibited it slightly. These results suggest that SucESA inhibits the activities of both factor Xa (or its upstream coagulation factors) and thrombin and that SulfESA inhibits only factor Xa activity (or that of its upstream coagulation factors). SucESA and SulfESA with a high degree of substitution strongly inhibited factor Xa and thrombin activity compared with those of the derivatives with a low degree of substitution, even when present in high concentrations. This suggests that the density of the anion group determines the degree of inhibition of factor Xa and thrombin activity. SucESA, which has a high molecular weight, inhibited thrombin activity to a greater degree than low molecular weight SucESA. Because SucESA and SulfESA inhibited both purified factor Xa and thrombin irrespective of the presence of antithrombin, it is suggested that SucESA and SulfESA inhibit via direct action with both enzymes. © 2010 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved. Source

Sanwa Cornstarch Co. and Ezaki Glico Co. | Date: 2012-12-13

A disintegrant for tablets includes an -1,4-glucan having a degree of polymerization of not less than 180 and less than 1230 and a dispersity (weight average molecular weight Mw/number average molecular weight Mn) of not more than 1.25 or a modified product thereof. A binder for tablets includes an -1,4-glucan having a degree of polymerization of not less than 1230 and not more than 37000 and a dispersity of not more than 1.25, or a modified product thereof. A binding-disintegrating agent for tablets includes a low molecular weight -1,4-glucan or a modified product thereof, and a high molecular weight -1,4-glucan or a modified product thereof.

Asahi Kasei Corporation and Sanwa Cornstarch Co. | Date: 2015-07-16

Functional starch powder of 400% or more water retention capacity, 5 hr or more collapse time and 200 g or more gel indentation load.

Yamazaki T.,Ishinomaki Senshu University | Kikuchi N.,Ishinomaki Senshu University | Katoh M.,Tokushima University | Hirose T.,Ishinomaki Senshu University | And 3 more authors.
Applied Catalysis B: Environmental

Steam reforming reactions of reagent ethanol and of biomass-derived ethanol (bio-ethanol) over Pt catalysts supported on ZrO2 were studied. For steam reforming reactions at 673K of reagent ethanol with an H2O/C2H5OH molar ratio=3, the initial H2 yields were 20-29%. The major carbon-containing products were CH4, CO2, and CO. Small amounts of acetaldehyde, acetone, and ethylene were produced, showing that the partial ethanol steam reforming reaction (C2H5OH+H2O→CH4+CO2+2H2) occurred competitively with the ethanol decomposition reaction (C2H5OH→CH4+CO+H2).H2 formation for bio-ethanol was less than that obtained with reagent ethanol under the same conditions. The catalytic activity for the partial steam reforming reaction decreased rapidly; a similar decrease in the activity of the ethanol decomposition reaction was observed. The poisoning effect of sulfur compounds on the Pt sites was responsible for the deactivation of the bio-ethanol steam reforming reaction. © 2010 Elsevier B.V. Source

Shibanuma K.,Sanwa Cornstarch Co. | Degawa Y.,Sanwa Cornstarch Co. | Houda K.,Nara Seibu Hospital
European Journal of Nutrition

Purpose: l-Arabinose uncompetitively inhibits intestinal sucrase by forming an enzyme-inhibitor-substrate (EIS) complex. The transient period of the EIS complex affects the time span of inhibition. We determined the apparent transient period of the EIS complex of sucrase, l-arabinose, and sucrose both in vitro and in humans. Methods: Intestinal acetone powder (a source of sucrase), l-arabinose, and sucrose were mixed and injected into a dialysis membrane that was placed in a sucrose solution. The production rate of d-glucose and the release rate of l-arabinose from sucrase were determined. We also investigated the suppression of blood glucose levels by l-arabinose in 21 healthy volunteers. Sucrose (40 g) was ingested with or without l-arabinose (2 g), then blood glucose values were measured, which returned to steady-state conditions within 2 h. Volunteers were then given 90 g of commercial adzuki bean jelly containing 40 g sucrose as the sucrose load, and blood glucose values were measured again. Results: Addition of l-arabinose reduced the production rate of d-glucose compared to the rates measured in the absence of l-arabinose for several hours in vitro. l-Arabinose was released at a lower rate in the presence of sucrose than in its absence. Blood glucose values measured 2 h after sucrose was given with l-arabinose were significantly lower than those measured when l-arabinose was not given (Δ change in maximum value: with l-arabinose, 53.8 ± 19.7 mg/dL; without l-arabinose, 65.0 ± 17.7 mg/dL). Conclusion: The EIS complex of sucrase-l-arabinose-sucrose was maintained for several hours both in vitro and in humans. © 2010 Springer-Verlag. Source

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