Abstract: A crash energy absorption part for an automobile is provided in a front portion or a rear portion of an automotive body and absorbing crash energy when a crash load is input from a front or a rear of the automotive body, and includes: a top portion; a tubular member including a side wall portion continuous with the top portion via a shoulder part of a punch; and a resin applied or patched to at least an inner surface of the shoulder part of a punch of the tubular member. The resin has a thickness gradually changing in an axial direction from one end side toward other end side, a thickest portion of the thickness is 8 mm or less, and the resin is bonded to the inner surface with an adhesive strength of 10 MPa or more and is axially crushed when the crash load is input.

Abstract: The present invention provides an endoglucanase having excellent heat resistance. Specifically, the present invention provides an endoglucanase satisfying characteristics (A) and (B) below: (A) having an amino acid sequence that is at least 80% identical to the amino acid sequence of SEQ ID NO: 1; and (B) having at least one amino acid substitution selected from the group consisting of K214E, D254E, and S309P.

Abstract: The present invention provides an endoglucanase with excellent heat resistance. An endoglucanase having characteristics (A) to (C) below: (A) a polypeptide having an amino acid sequence that is at least 80% identical to the amino acid sequence of SEQ ID NO: 1; (B) the molecular weight of a polypeptide moiety being about 31 kDa; and (C) containing a sugar chain, and having a molecular weight measured by SDS-PAGE being about 39 kDa or more.

Abstract: The present invention has an object of providing a modified lipase having excellent stability and reactivity at a high temperature. Provided is a modified lipase with improved reactivity and/or stability at a high temperature, the modified lipase having an amino acid sequence including one or more amino acid substitutions which are selected from the group consisting of T130C-S153C, A249P, F259Y, S282P, S283Y and S300P in the amino acid sequence represented by SEQ ID NO: 1, or an amino acid sequence having 90% or more sequence identity therewith.

Abstract: Provided are: a reverse transcriptase mutant including an amino acid mutation at a position corresponding to position 55 of the amino acid sequence of wild-type reverse transcriptase derived from the Moloney murine leukemia virus, wherein the reverse transcriptase mutant is characterized in that the amino acid mutation is a substitution from threonine to another amino acid, and the other amino acid is selected from the group consisting of amino acids having a nonpolar aliphatic side chain and amino acids having a polar acidic functional group side chain; a nucleic acid that encodes the mutant; a method for producing the mutant and the nucleic acid that encodes the mutant; a method for synthesizing cDNA in which the mutant is used; and a composition and kit including the mutant.

Abstract: Provided are: a reverse transcriptase mutant including an amino acid mutation at a position corresponding to position 55 of the amino acid sequence of wild-type reverse transcriptase derived from the Moloney murine leukemia virus, wherein the reverse transcriptase mutant is characterized in that the amino acid mutation is a substitution from threonine to another amino acid, and the other amino acid is selected from the group consisting of amino acids having a nonpolar aliphatic side chain and amino acids having a polar acidic functional group side chain; a nucleic acid that encodes the mutant; a method for producing the mutant and the nucleic acid that encodes the mutant; a method for synthesizing cDNA in which the mutant is used; and a composition and kit including the mutant.

Abstract: It is found that a variant enzyme with an improved thermal stability can be obtained by substituting a specific amino acid in the amino acid sequence of a ketose 3-epimerase originated from Arthrobacter globiformis and that D-psicose can be efficiently produced.

Abstract: The present invention has an object of providing a modified lipase having excellent stability and reactivity at a high temperature. Provided is a modified lipase with improved reactivity and/or stability at a high temperature, the modified lipase having an amino acid sequence including one or more amino acid substitutions which are selected from the group consisting of T130C-S153C, A249P, F259Y, S282P, S283Y and S300P in the amino acid sequence represented by SEQ ID NO: 1, or an amino acid sequence having 90% or more sequence identity therewith.

Abstract: It is found that a variant enzyme with an improved thermal stability can be obtained by substituting a specific amino acid in the amino acid sequence of a ketose 3-epimerase originated from Arthrobacter globiformis and that D-psicose can be efficiently produced.

Abstract: An endoxylanase mutant has improved thermal stability. The endoxylanase mutant having endoxylanase activity includes an amino acid sequence at least including substitution of an amino acid residue at one or more positions selected from positions corresponding to position 35, position 44, position 62, position 63, position 101, and position 102 of an amino acid sequence of SEQ ID NO: 1 in an amino acid sequence of endoxylanase derived from a filamentous fungus.

Abstract: The present invention has a purpose of providing a technique for increasing the heat resistance of a ?-galactosidase. According to the present invention, in a reference ?-galactosidase amino acid sequence which shows a 90% or more identity to the amino acid sequence of SEQ ID NO: 4, proline is substituted for one or more amino acids selected from the group consisting of the following amino acids: (1) an amino acid corresponding to lysine at position 166 of the amino acid sequence of SEQ ID NO: 4, (2) an amino acid corresponding to glycine at position 307 of the amino acid sequence of SEQ ID NO: 4, and (3) an amino acid corresponding to alanine at position 833 of the amino acid sequence of SEQ ID NO: 4.

Abstract: Provided is a modified xylanase. The polypeptide has xylanase activity and has an amino acid sequence with deletion of at least 12 consecutive amino acid residues at the C-terminus of the amino acid sequence of SEQ ID NO: 1 or an amino acid sequence having at least 90% identity with the amino acid sequence of SEQ ID NO: 1.

Abstract: The disclosure provides a polypeptide with a mutation having cellobiohydrolase activity and improved thermal stability.

Abstract: Provided is a modified xylanase. The polypeptide has xylanase activity and has an amino acid sequence with deletion of at least 12 consecutive amino acid residues at the C-terminus of the amino acid sequence of SEQ ID NO: 1 or an amino acid sequence having at least 90% identity with the amino acid sequence of SEQ ID NO: 1.

Abstract: An object of the present invention is to provide a means for producing an archaeal protein by extracellular secretion. The system for secretory production of an archaeal protein uses a fungus belonging to the genus Talaromyces as a host.

Abstract: An endoxylanase mutant has improved thermal stability. The endoxylanase mutant having endoxylanase activity includes an amino acid sequence at least including substitution of an amino acid residue at one or more positions selected from positions corresponding to position 35, position 44, position 62, position 63, position 101, and position 102 of an amino acid sequence of SEQ ID NO: 1 in an amino acid sequence of endoxylanase derived from a filamentous fungus.

Abstract: The present invention has a purpose of providing a technique for increasing the heat resistance of a ?-galactosidase. According to the present invention, in a reference ?-galactosidase amino acid sequence which shows a 90% or more identity to the amino acid sequence of SEQ ID NO: 4, proline is substituted for one or more amino acids selected from the group consisting of the following amino acids: (1) an amino acid corresponding to lysine at position 166 of the amino acid sequence of SEQ ID NO: 4, (2) an amino acid corresponding to glycine at position 307 of the amino acid sequence of SEQ ID NO: 4, and (3) an amino acid corresponding to alanine at position 833 of the amino acid sequence of SEQ ID NO: 4.

Abstract: The disclosure provides a polypeptide with a mutation having cellobiohydrolase activity and improved thermal stability.

Abstract: An object of the present invention is to provide a means for producing an archaeal protein by extracellular secretion. The system for secretory production of an archaeal protein uses a fungus belonging to the genus Talaromyces as a host.

Abstract: The purpose of the present invention is to provide a novel xylanase having various excellent enzymological properties, and that is suitable for industrial applications. The polypeptide is selected from the group consisting of (a), (b), and (c) below: (a) a polypeptide comprising an amino acid sequence selected from SEQ ID NOs: 1 to 7; (b) a polypeptide having xylanase activity and comprising an amino acid sequence selected from SEQ ID NOs: 1 to 7, the amino acid sequence having substitution, deletion, insertion, and/or addition of one or several amino acid residues; and (c) a polypeptide having xylanase activity and comprising an amino acid sequence having at least 80% identity with an amino acid sequence selected from SEQ ID NOs. 1 to 7.