Abstract: Provided is a laminate that has excellent low-temperature impact resistance and bursting pressure strength at high temperatures despite having a thick modified polyolefin layer. The laminate has two or more layers including an (a) layer and a (b) layer, the (a) layer includes an aliphatic polyamide composition (A), and the (b) layer includes a modified polyolefin (B). The modified polyolefin (B) includes a unit derived from a monomer based on an ?-olefin having 2-10 carbon atoms, and a unit derived from an unsaturated compound having at least one functional group selected from the group consisting of: unsaturated compounds having at least one group selected from the group consisting of a carboxyl group, a hydroxyl group, an epoxy group, an amino group, an amide group, an imide group, a nitrile group, a thiol group, and an isocyanate group; and derivatives of unsaturated compounds having a carboxyl group. The Shore hardness (D scale) of the modified polyolefin (B) as measured according to ASTM D2240 is 30-61.

Abstract: A non-oriented electrical steel sheet according to an embodiment of the present invention is a non-oriented electrical steel sheet including a base metal steel sheet and a composite coating film that is formed on surfaces of the base metal steel sheet and includes Zn-containing phosphate and an organic resin, wherein the non-oriented electrical steel sheet contains crystalline aluminum phosphate showing diffraction lines belonging to ICDD No. 01-074-3256 when the composite coating film is measured by a wide-angle X-ray diffraction method.

Abstract: A lighting apparatus that can easily change light distribution is provided. In an LED lighting apparatus in which an LED as a light source, and a reflector having a reflecting surface in a shape of a curved surface of revolution are accommodated in an apparatus main body, the reflector is made separable into a base end side and a tip end side of the reflecting surface, and a tip end of the base end side part is protruded from the apparatus main body .

Abstract: A switching power supply device includes a case, a board that has circuit parts containing a switching element mounted thereon and is accommodated in the case, and a heat sink that is provided in the case so as to partition the inside of the case into a part mount chamber having the board accommodated therein and an air flow path through which air flows. The switching element of the circuit parts is mounted on the board while brought into contact with a surface of the heat sink that faces the part mount chamber, and cooled through the heat sink by the air flowing in the air flow path.

Abstract: A switching power supply device includes a case, a board that has circuit parts containing a switching element mounted thereon and is accommodated in the case, and a heat sink that is provided in the case so as to partition the inside of the case into a part mount chamber having the board accommodated therein and an air flow path through which air flows. The switching element of the circuit parts is mounted on the board while brought into contact with a surface of the heat sink that faces the part mount chamber, and cooled through the heat sink by the air flowing in the air flow path.

Abstract: The present application discloses a molded article, and a process for preparing a molded article consisting essentially of (i) high molecular weight linear ?-1,4-glucan and (ii) low molecular weight linear ?-1,4-glucan, wherein the process comprises the step of: adding the low molecular weight linear ?-1,4-glucan to a solution comprising the high molecular weight linear ?-1,4-glucan to gel the solution, wherein the low molecular weight linear ?-1,4-glucan has a degree of polymerization of greater than or equal to 180 and less than 620, and has a molecular weight distribution of not greater than 1.25 and, the high molecular weight linear ?-1,4-glucan has a degree of polymerization of greater than or equal to 620 and less than 37000, and has a molecular weight distribution of not greater than 1.25.

Abstract: A sucrose phosphorylase (SP) having improved thermostability obtained by modifying a natural SP and a method for producing the SP having improved thermostability is provided. This SP having improved thermostability has an amino acid residue which is different from that of the natural sucrose phosphorylase, in at least one position selected from the group consisting of a position corresponding to position 14, a position corresponding to position 29 and a position corresponding to position 44 in motif sequence 1; a position corresponding to position 7, a position corresponding to position 19, a position corresponding to position 23 and a position corresponding to position 34 in motif sequence 2; and a position corresponding to position 19 in motif sequence 3, and wherein the enzyme activity of the SP having improved thermostability at 37° C., after heating the SP having improved thermostability in 20 mM Tris buffer (pH 7.0) at 55° C.

Abstract: The present invention provides a biodegradable article formed from enzyme-synthesized amylose using phosphorylase, wherein the enzyme-synthesized amylose is composed of glucose monomers exclusively bonded by ?-1,4-glucosidic likage and has a weight average molecular weight of not less than 100 kDa, preferable not less than 600 kDa. The enzyme-synthesized amylose employed in the present invention has a molecular weight distribution (Mw/Mn) of not more than 1.25 and can be chemically modified if desired. The biodegradable article of the present invention can be produced by (a) the enzyme-synthesized amylose and/or its modified one, or a combination of the amylose (a) and another polymer material (b).

Abstract: An ?-glucan phosphorylase having improved thermostability, which obtained by modifying natural ?-glucan phosphorylase, and a method for producing this ?-glucan phosphorylase having improved thermostability are provided. The natural ?-glucan phosphorylase is derived from a plant, this ?-glucan phosphorylase having improved thermostability has an amino acid residue which is different from that of the natural ?-glucan phosphorylase in at least one position selected from the group consisting of a position corresponding to position 4 in a motif sequence 1L or 1H, a position corresponding to position 4 in a motif sequence 2, and a position corresponding to position 7 in a motif sequence 3L or 3H, and wherein the enzyme activity of ?-glucan phosphorylase having improved thermostability at 37° C., after heating in a 20 mM citrate buffer (pH 6.7) at 60° C. for 10 minutes, is 20% or more of the enzyme activity of the ?-glucan phosphorylase having improved thermostability at 37° C., before heating.

Abstract: An ?-glucan phosphorylase having improved thermostability, which obtained by modifying natural ?-glucan phosphorylase, and a method for producing this ?-glucan phosphorylase having improved thermostability are provided. The natural ?-glucan phosphorylase is derived from a plant, this ?-glucan phosphorylase having improved thermostability has an amino acid residue which is different from that of the natural ?-glucan phosphorylase in at least one position selected from the group consisting of a position corresponding to position 4 in a motif sequence 1L or 1H, a position corresponding to position 4 in a motif sequence 2, and a position corresponding to position 7 in a motif sequence 3L or 3H, and wherein the enzyme activity of ?-glucan phosphorylase having improved thermostability at 37° C., after heating in a 20 mM citrate buffer (pH 6.7) at 60° C. for 10 minutes, is 20% or more of the enzyme activity of the ?-glucan phosphorylase having improved thermostability at 37° C., before heating.

Abstract: An ?-glucan phosphorylase having improved thermostability, which obtained by modifying natural ?-glucan phosphorylase, and a method for producing this ?-glucan phosphorylase having improved thermostability are provided. The natural ?-glucan phosphorylase is derived from a plant, this ?-glucan phosphorylase having improved thermostability has an amino acid residue which is different from that of the natural ?-glucan phosphorylase in at least one position selected from the group consisting of a position corresponding to position 4 in a motif sequence 1L or 1H, a position corresponding to position 4 in a motif sequence 2, and a position corresponding to position 7 in a motif sequence 3L or 3H, and wherein the enzyme activity of ?-glucan phosphorylase having improved thermostability at 37° C., after heating in a 20 mM citrate buffer (pH 6.7) at 60° C. for 10 minutes, is 20% or more of the enzyme activity of the ?-glucan phosphorylase having improved thermostability at 37° C., before heating.

Abstract: A sucrose phosphorylase (SP) having improved thermostability obtained by modifying a natural SP and a method for producing the SP having improved thermostability is provided. This SP having improved thermostability has an amino acid residue which is different from that of the natural sucrose phosphorylase, in at least one position selected from the group consisting of a position corresponding to position 14, a position corresponding to position 29 and a position corresponding to position 44 in motif sequence 1; a position corresponding to position 7, a position corresponding to position 19, a position corresponding to position 23 and a position corresponding to position 34 in motif sequence 2; and a position corresponding to position 19 in motif sequence 3, and wherein the enzyme activity of the SP having improved thermostability at 37° C., after heating the SP having improved thermostability in 20 mM Tris buffer (pH 7.0) at 55° C.

Abstract: The present invention provides a composition for adsorbing or trapping an undesired material, wherein the composition comprises a functional ?-1,4-glucan as an active ingredient. Specifically, ?-1,4-glucan is allowed to be functionalized to provide said composition for adsorbing or trapping an undesired material. There are provided a composition comprising a functional ?-1,4-glucan, all or a part of which is in a form of V-type crystal or an amorphous form, as well as an article comprising the composition as a functional material.

Abstract: A first method for producing glucan comprises the step of allowing a reaction solution containing sucrose, a primer, inorganic phosphate or glucose-1-phosphate, sucrose phosphorylase, and glucan phosphorylase to react to produce glucans. The maximum value of the sucrose-phosphate ratio of the reaction solution from the start of the reaction to the end of the reaction is no more than about 17. A second method for producing glucan comprises the step of allowing a reaction solution containing sucrose, a primer, inorganic phosphate or glucose-1-phosphate, sucrose phosphorylase, and glucan phosphorylase to react to produce glucans. The reaction is conducted at a temperature of about 40 C to about 70 C.

Abstract: A disintegrant for tablets consisting of 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 consisting of 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 consisting of 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, wherein the low molecular weight ?-1,4-glucan has a degree of polymerization of not less than 180 and less than 1230 and a dispersity of not more than 1.25, and wherein the high molecular weight ?-1,4-glucan has a degree of polymerization of not less than 1230 and not less than 37000 and a dispersity of not more than 1.25.

Abstract: An ?-glucan phosphorylase having improved thermostability, which obtained by modifying natural ?-glucan phosphorylase, and a method for producing this ?-glucan phosphorylase having improved thermostability are provided. The natural ?-glucan phosphorylase is derived from a plant, this ?-glucan phosphorylase having improved thermostability has an amino acid residue which is different from that of the natural ?-glucan phosphorylase in at least one position selected from the group consisting of a position corresponding to position 4 in a motif sequence 1L or 1H, a position corresponding to position 4 in a motif sequence 2, and a position corresponding to position 7 in a motif sequence 3L or 3H, and wherein the enzyme activity of ?-glucan phosphorylase having improved thermostability at 37° C., after heating in a 20 mM citrate buffer (pH 6.7) at 60° C. for 10 minutes, is 20% or more of the enzyme activity of the ?-glucan phosphorylase having improved thermostability at 37° C., before heating.

Abstract: The present invention discloses a molded article containing high molecular weight ?-1,4-glucan and/or its modification, and low molecular weight ?-1,4-glucan and/or its modification. The low molecular weight ?-1,4-glucan has the degree of polymerization of greater than or equal to 180 and less than 620. And the high molecular weight ?-1,4-glucan has the degree of polymerization of greater than or equal to 620 and less than 37000. The high molecular weight ?-1,4-glucan may preferably have a molecular weight distribution of not greater than 1.25, and the low molecular weight ?-1,4-glucan may preferably have a molecular weight distribution of not greater than 1.25. The present invention also discloses a process for preparing the molded article, wherein the process comprises the step of adding the low molecular weight ?-1,4-glucan and/or its modification to a solution comprising the high molecular weight ?-1,4-glucan and/or its modification to gel the solution.

Abstract: A first method for producing glucan comprises the step of allowing a reaction solution containing sucrose, a primer, inorganic phosphate or glucose-1-phosphate, sucrose phosphorylase, and glucan phosphorylase to react to produce glucans. The maximum value of the sucrose-phosphate ratio of the reaction solution from the start of the reaction to the end of the reaction is no more than about 17. A second method for producing glucan comprises the step of allowing a reaction solution containing sucrose, a primer, inorganic phosphate or glucose-1-phosphate, sucrose phosphorylase, and glucan phosphorylase to react to produce glucans. The reaction is conducted at a temperature of about 40 C to about 70 C.

Abstract: The present invention provides a biodegradable article formed from enzyme-synthesized amylose using phosphorylase, wherein the enzyme-synthesized amylose is composed of glucose monomers exclusively bonded by &agr;-1,4-glucosidic likage and has a weight average molecular weight of not less than 100 kDa, preferable not less than 600 kDa. The enzyme-synthesized amylose employed in the present invention has a molecular weight distribution (Mw/Mn) of not more than 1.25 and can be chemically modified if desired.

Abstract: A method for activating a denatured protein, includes the steps of: adding a detergent to the denatured protein to allow a protein-detergent complex to be formed; and adding high-molecular weight amylose to the protein-detergent complex so that the high-molecular weight amylose removes the detergent.