Abstract: A hyperthermostable endoglucanase including an endoglucanase catalytic domain, the endoglucanase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11, and having hydrolytic activity using carboxymethyl cellulose as a substrate at least under conditions of a temperature of 110° C. and a pH of 4.0; or (C) a polypeptide including an amino acid sequence having at least 70% sequence identity with the amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11, and having hydrolytic activity using carboxymethyl cellulose as a substrate at least under conditions of a temperature of 110° C. and a pH of 4.0.

Abstract: A thermostable ?-xylosidase, having a ?-xylosidase catalytic domain including: (A) a polypeptide including the amino acid sequence represented by SEQ ID NO: 1, 3 or 5, (B) a polypeptide including an amino acid sequence in which at least one amino acid has been deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, 3 or 5, and having hydrolysis activity against a substrate of p-nitrophenyl-?-D-xylopyranoside at least under conditions of 80° C. and pH 4.0, or (C) a polypeptide including an amino acid sequence having 80% or greater sequence identity with the amino acid sequence represented by SEQ ID NO: 1, 3 or 5, and having hydrolysis activity against a substrate of p-nitrophenyl-?-D-xylopyranoside at least under conditions of 80° C. and pH 4.0.

Abstract: A thermostable cellobiohydrolase including a cellobiohydrolase catalytic domain, the cellobiohydrolase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence obtained by deletion, substitution or addition of at least one amino acid of the amino acid sequence represented by SEQ ID NO: 1, and having at least a cellobiohydrolase activity under conditions of 75° C. and pH 5.5; (C) a polypeptide including an amino acid sequence having at least 85% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having at least a cellobiohydrolase activity under conditions of 75° C. and pH 5.

Abstract: A porous coordination polymer represented by the following formula (1), wherein, the ratio A/B of the diffraction peak intensity A of (001) plane to the diffraction peak intensity B of (110) plane is 0.8 or more and 5.8 or less, Fex(pz)[Ni1-yMy(CN)4]??(1) wherein, pz=pyrazine, 0.95?x<1.05, M=Pd, Pt, 0?y<0.15. The present invention also provides a gas detecting material and a lithium ion secondary battery having the porous coordination polymer.

Abstract: A negative electrode active material for a lithium ion secondary battery includes secondary particles formed by primary particles containing iron oxide that are linked in a chain.

Abstract: To provide an active material with high capacity, high initial charge-discharge efficiency, and high average discharge voltage. An active material according to the present invention includes a first active material and a second active material, wherein the ratio (?) of the second active material (B) to the total amount by mole of the first active material (A) and the second active material (B) satisfies 0.4 mol %???18 mol % [where ?=(B/(A+B))×100].

Abstract: To provide an active material having high capacity and excellent cycle characteristics. An active material has a layered crystal structure and is expressed by a compositional formula (1) LiyNiaCobMncMdOx (1), where the element M is at least one kind of element selected from the group consisting of Al, Si, Zr, Ti, Fe, Mg, Nb, Ba, and V; 1.9?(a+b+c+d+y)?2.1; 1.05?y?1.35; 0<a?0.3; 0<b?0.25; 0.3?c?0.7; 0?d?0.1; and 1.9?x?2.1, and wherein 0.69?Ni?/Ni??0.85, where Ni? is the Ni composition amount at a center portion of the active material primary particle, and Ni? is the Ni composition amount in the vicinity of a surface (in a width of 30 nm from the surface).

Abstract: A hyperthermostable endoglucanase including an endoglucanase catalytic domain, the endoglucanase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-cellobioside as a substrate at least under conditions of a temperature of 100° C. and a pH of 5.5; or (C) a polypeptide including an amino acid sequence having at least 70% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-cellobioside as a substrate at least under conditions of a temperature of 100° C. and a pH of 5.5.

Abstract: A hyperthermostable endoglucanase including an endoglucanase catalytic domain, the endoglucanase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11, and having hydrolytic activity using carboxymethyl cellulose as a substrate at least under conditions of a temperature of 110° C. and a pH of 4.0; or (C) a polypeptide including an amino acid sequence having at least 70% sequence identity with the amino acid sequence represented by SEQ ID NO: 3 or SEQ ID NO: 11, and having hydrolytic activity using carboxymethyl cellulose as a substrate at least under conditions of a temperature of 110° C. and a pH of 4.0.

Abstract: A thermostable ?-xylosidase, having a ?-xylosidase catalytic domain including: (A) a polypeptide including the amino acid sequence represented by SEQ ID NO: 1, 3 or 5, (B) a polypeptide including an amino acid sequence in which at least one amino acid has been deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, 3 or 5, and having hydrolysis activity against a substrate of p-nitrophenyl-?-D-xylopyranoside at least under conditions of 80° C. and pH 4.0, or (C) a polypeptide including an amino acid sequence having 80% or greater sequence identity with the amino acid sequence represented by SEQ ID NO: 1, 3 or 5, and having hydrolysis activity against a substrate of p-nitrophenyl-?-D-xylopyranoside at least under conditions of 80° C. and pH 4.0.

Abstract: A thermostable ?-glucosidase including a ?-glucosidase catalytic domain, the ?-glucosidase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-glucopyranoside as a substrate at least under conditions of a temperature of 85° C. and a pH of 7.5; or (C) a polypeptide including an amino acid sequence having at least 60% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-glucopyranoside as a substrate at least under conditions of a temperature of 85° C. and a pH of 7.5.

Abstract: A thermostable ?-glucosidase including a ?-glucosidase catalytic domain, the ?-glucosidase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-glucopyranoside as a substrate at least under conditions of a temperature of 75° C. and a pH of 7; or (C) a polypeptide including an amino acid sequence having at least 90% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-glucopyranoside as a substrate at least under conditions of a temperature of 75° C. and a pH of 7.

Abstract: A thermostable xylanase having a xylanase catalytic domain including: (A) a polypeptide including the amino acid sequence represented by SEQ ID NO: 1, (B) a polypeptide including an amino acid sequence in which at least one amino acid has been deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, and having xylanase activity at least under conditions of 85° C. and pH 6.0, or (C) a polypeptide including an amino acid sequence having 80% or greater sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having xylanase activity at least under conditions of 85° C. and pH 6.0.

Abstract: The thermostable cellobiohydrolase of the present invention is a polypeptide which has cellobiohydrolase activity at least under conditions of a temperature of 75° C. and a pH of 5.5, and which includes a polypeptide including an amino acid sequence represented by SEQ ID NO: 1, 3, 5, or 7, a polypeptide including an amino acid sequence in which one or several amino acids are deleted, substituted, or added in an amino acid sequence represented by SEQ ID NO: 1, 3, 5, or 7, or a polypeptide including an amino acid sequence having 80% or greater but less than 100% sequence identity with an amino acid sequence represented by SEQ ID NO: 1, 3, 5, or 7.

Abstract: A positive electrode material for a lithium ion secondary battery contains a first compound represented by Li3V2(PO4)3 and one or more second compounds selected from vanadium oxide and lithium vanadium phosphate.

Abstract: A thermostable ?-xylosidase including a ?-xylosidase catalytic domain, the ?-xylosidase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-xylopyranoside as a substrate at least under conditions of a temperature of 85° C. and a pH of 6.0; or (C) a polypeptide including an amino acid sequence having at least 80% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having hydrolytic activity using p-nitrophenyl-?-D-xylopyranoside as a substrate at least under conditions of a temperature of 85° C. and a pH of 6.0.

Abstract: A thermostable xylanase including a xylanase catalytic domain, the xylanase catalytic domain including: (A) a polypeptide comprising an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence in which at least one amino acid is deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1, and having xylanase activity at least under conditions of a temperature of 90° C. and a pH of 6.0; or (C) a polypeptide including an amino acid sequence having at least 75% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having xylanase activity at least under conditions of a temperature of 90° C. and a pH of 6.0.

Abstract: A negative electrode active material for a lithium ion secondary battery includes secondary particles formed by primary particles containing iron oxide that are linked in a chain.

Abstract: A negative electrode active material for a lithium ion secondary battery includes a network structure formed by at least some of iron oxide particles being linked to each other.

Abstract: A thermostable cellobiohydrolase including a cellobiohydrolase catalytic domain, the cellobiohydrolase catalytic domain including: (A) a polypeptide including an amino acid sequence represented by SEQ ID NO: 1; (B) a polypeptide including an amino acid sequence obtained by deletion, substitution or addition of at least one amino acid of the amino acid sequence represented by SEQ ID NO: 1, and having at least a cellobiohydrolase activity under conditions of 75° C. and pH 5.5; (C) a polypeptide including an amino acid sequence having at least 85% sequence identity with the amino acid sequence represented by SEQ ID NO: 1, and having at least a cellobiohydrolase activity under conditions of 75° C. and pH 5.