Abstract: The present invention provides a method for efficiently producing an industrially useful protein in coryneform bacteria, and more particularly, a method for efficiently producing a protein for which secretion was difficult using conventional protein secretion pathways. In particular, the present invention provides a method for efficiently producing heterologous proteins comprising culturing coryneform bacteria containing an genetic construction containing a promoter sequence which functions in coryneform bacteria, a nucleic acid sequence encoding a Tat system-dependent signal peptide region, and a nucleic acid sequence encoding a heterologous protein, in the direction from 5?-end to 3?-end, and secretory producing the heterologous protein by coryneform bacteria.

Abstract: The present invention provides a dairy product with smooth oral sensation and suppressed acidic taste and bitter taste and a method for manufacturing the same, wherein a protein deamidating enzyme is added to raw milk to act on the milk protein in the raw milk.

Abstract: The present invention provides a protein deamidating enzyme that is added to a food material containing muscle protein and acts on the same to produce high-quality foods.

Abstract: The present invention provides a dairy product with smooth oral sensation and suppressed acidic taste and bitter taste and a method for manufacturing the same, wherein a protein deamidating enzyme is added to raw milk to act on the milk protein in the raw milk.

Abstract: The present invention discloses a method for producing foods and/or beverage having improved taste and/or flavour, comprising reacting a microbial aminopeptidase on a protein material optionally under the co-existence of a protease, wherein said aminopeptidase has the properties of: (a) having an activity of catalyzing the reaction of specifically releasing a glutamic acid and an aspartic acid from the N-terminal of a peptide and/or a protein; (b) having 50% or more activity at pH6.0-9.0 as compared with the activity at the optimum pH; (c) having 40% or more activity after heating at 25-60° C., pH7.5 for 30 minutes as compared with the activity of the non-heated enzyme; (d) having a molecular weight of about 40-60 kD as measured by SDS-PAGE and about 300-480 kD as measured by native-PAGE; (e) having a hydrolyzing activity of the aminopeptidase toward Glu-Glu dipeptide is 5 U/mg or more, preferably 10 U/mg or more.

Abstract: The present invention provides a method for efficiently producing an industrially useful protein in coryneform bacteria, and more particularly, a method for efficiently producing a protein for which secretion was difficult using conventional protein secretion pathways. In particular, the present invention provides a method for efficiently producing heterologous proteins comprising culturing coryneform bacteria containing an genetic construction containing a promoter sequence which functions in coryneform bacteria, a nucleic acid sequence encoding a Tat system-dependent signal peptide region, and a nucleic acid sequence encoding a heterologous protein, in the direction from 5?-end to 3?-end, and secretory producing the heterologous protein by coryneform bacteria.

Abstract: The present invention discloses a method for producing foods and/or beverage having improved taste and/or flavour, comprising reacting a microbial aminopeptidase on a protein material optionally under the co-existence of a protease, wherein said aminopeptidase has the properties of: (a) having an activity of catalyzing the reaction of specifically releasing a glutamic acid and an aspartic acid from the N-terminal of a peptide and/or a protein; (b) having 50% or more activity at pH6.0-9.0 as compared with the activity at the optimum pH; (c) having 40% or more activity after heating at 25-60° C., pH7.5 for 30 minutes as compared with the activity of the non-heated enzyme; (d) having a molecular weight of about 40-60 kD as measured by SDS-PAGE and about 300-480 kD as measured by native-PAGE; (e) having a hydrolyzing activity of the aminopeptidase toward Glu-Glu dipeptide is 5 U/mg or more, preferably 10 U/mg or more.

Abstract: Disclosed are a protein having a transglutaminase activity, which comprises a sequence ranging from serine residue at the second position to proline residue at the 331st position in an amino acid sequence represented by SEQ ID No. 1 wherein the N-terminal amino acid of the protein corresponds to serine residue at the second position of SEQ ID No. 1, a DNA encoding the protein, a transformant having the DNA, and a process for producing a protein having a transglutaminase activity, which comprises the steps of culturing the transformant in a medium. The protein can be produced in a large amount with the transformant using a host such as E. coli.

Abstract: Disclosed are a protein having a transglutaminase activity, which comprises a sequence ranging from serine residue at the second position to proline residue at the 331st position in an amino acid sequence represented by SEQ ID No. 1 wherein the N-terminal amino acid of the protein corresponds to serine residue at the second position of SEQ ID No. 1, a DNA encoding the protein, a transformant having the DNA, and a process for producing a protein having a transglutaminase activity, which comprises the steps of culturing the transformant in a medium. The protein can be produced in a large amount with the transformant using a host such as E. coli.

Abstract: Disclosed are a protein having a transglutaminase activity, which comprises a sequence ranging from serine residue at the second position to proline residue at the 331st position in an amino acid sequence represented by SEQ ID No. 1 wherein the N-terminal amino acid of the protein corresponds to serine residue at the second position of SEQ ID No. 1, a DNA encoding the protein, a transformant having the DNA, and a process for producing a protein having a transglutaminase activity, which comprises the steps of culturing the transformant in a medium. The protein can be produced in a large amount with the transformant using a host such as E. coli.

Abstract: Disclosed are a protein having a transglutaminase activity, which comprises a sequence ranging from serine residue at the second position to proline residue at the 331st position in an amino acid sequence represented by SEQ ID No. 1 wherein the N-terminal amino acid of the protein corresponds to serine residue at the second position of SEQ ID No. 1, a DNA encoding the protein, a transformant having the DNA, and a process for producing a protein having a transglutaminase activity, which comprises the steps of culturing the transformant in a medium. The protein can be produced in a large amount with the transformant using a host such as E. coli.

Abstract: Disclosed are cDNA encoding a new aminopeptidase derived from germinated soybeans, a recombinant expression vector containing the DNA, a transformant obtained by the transformation with the expression vector, and a method of producing an aminopeptidase by culturing the transformed product. According to the present invention, a cDNA can be obtained encoding the amino acid sequence of aminopeptidase GX suitable for producing a highly hydrolized product from a starting material containing a protein and peptide having a high acidic amino acid content. Using the cDNA, a recombinant aminopeptidase can be mass-produced with E. coli or the like. By using the cDNA, it is also possible to produce aminopeptidase GX by using a host other than E. coli. In addition, hydrohized products having high glutamic acid content and aspartic acid content and also excellent seasoning properties can be obtained from soybean protein by combining GX thus produced with protease D3 and leucine aminopeptidase DLAP.

Abstract: Disclosed are a protein having a transglutaminase activity, which comprises a sequence ranging from serine residue at the second position to proline residue at the 331st position in an amino acid sequence represented by SEQ ID No. 1 wherein the N-terminal amino acid of the protein corresponds to serine residue at the second position of SEQ ID No. 1, a DNA encoding the protein, a transformant having the DNA, and a process for producing a protein having a transglutaminase activity, which comprises the steps of culturing the transformant in a medium. The protein can be produced in a large amount with the transformant using a host such as E. coli.