Abstract: The object of the present invention is to provide a method and a process for producing 2-O-?-glucopyranosyl-L-ascorbic acid where 5-O-?-glucopyranosyl-L-ascorbic acid and 6-O-?-glucopyranosyl-L-ascorbic acid are not formed or formed in such a small amount that the formation of these can nor be detected. The present invention solves the above object by providing a process for producing 2-O-?-glucopyranosyl-L-ascorbic acid comprising the steps of allowing ?-isomaltosyl glucosaccharide-forming enzyme together with or without cyclomaltodextrin glucanotransferase (EC 2.4.1.19) to act on a solution comprising L-ascorbic acid and, an ?-glucosyl saccharide to form 2-O-?-glucopyranosyl-L-ascorbic acid and collecting the formed 2-O-?-glucopyranosyl-L-ascorbic acid.

Abstract: A method of utilizing the physiological activity of a rare saccharide, wherein physiological-activity sensitive cells are treated with the rare saccharide to modify the function of the cells. A composition containing, as an active ingredient, a rare saccharide which is introduced into physiological-activity sensitive cells and has an effect of modifying the function of the cells. The cells are human cells. The composition is a functional food, a drug, or a cosmetic. The rare saccharide is a rare saccharide belonging to aldose and/or ketose. The aldose is D-allose, and the cells are selected from the group consisting of cancer-cell proliferation inhibitory activity sensitive cells and active-oxygen production inhibitory activity sensitive cells. The ketose is D-psicose, and the cells are selected from the group consisting of chemokine secretion inhibitory activity sensitive cells, microglia migration inhibitory activity sensitive cells, and hypoglycemic activity sensitive cells.

Abstract: The present invention solves the object of the present invention by providing a DNA encoding an L-ribose isomerase which isomerizes L-ribose into L-ribulose and vice versa, and the process for producing a polypeptide by recombinant DNA techniques using the DNA.

Abstract: A polypeptide having &bgr;-fructofuranosidase activity is obtained by the expression of a microbial gene, which polypeptide contains the amino acid sequences of SEQ ID NO:1 and SEQ ID NO:2 in whole or in part as an amino acid sequence. This polypeptide is useful for producing fructofuranosyl transferred saccharides.

Abstract: The object of the present invention is to provide an &agr;-isomaltosylglucosaccharide-forming enzyme, process of the same, cyclotetrasaccharide, and saccharide composition comprising the saccharide which are obtainable by using the enzyme; and is solved by establishing an &agr;-isomaltosylglucosaccharide-forming enzyme which forms a saccharide, having a glucose polymerization degree of at least three and having both the &agr;-1,6 glucosidic linkage as a linkage at the non-reducing end and the &agr;-1,4 glucosidic linkage other than the linkage at the non-reducing end, by catalyzing the &agr;-glucosyl-transfer from a saccharide having a glucose polymerization degree of at least two and having the &agr;-1,4 glucosidic linkage as a linkage at the non-reducing end without substantially increasing the reducing power; &agr;-isomaltosyl-transferring method using the enzyme; method for forming &agr;-isomaltosylglucosaccharide; process for producing a cyclotetrasaccharide having the structure of cyclo{→6)-&a

Abstract: A polypeptide having &bgr;-fructofuranosidase activity is obtained by the expression of a microbial gene, which polypeptide contains the amino acid sequences of SEQ ID NO:1 and SEQ ID NO:2 in whole or in part as an amino acid sequence. This polypeptide is useful for producing fructofuranosyl transferred saccharides.

Abstract: Disclosed are a polypeptide having a &bgr;-fructofuranosidase activity obtainable by the expression of a microbial gene, a DNA encoding the polypeptide, a transformant obtained by introducing the DNA into an appropriate host, a process for producing the polypeptide comprising culturing the transformant to produce the polypeptide and collecting the produced polypeptide from the culture, and a method for fructofuranosyl transfer comprising a step of reacting a fructofuranosyl donor with a fructofuranosyl acceptor in the presence of the polypeptide.

Abstract: An L-ribose isomerase which isomerizes aldoses such as L-ribose, D-lyxose, D-talose, D-mannose, L-allose and L-gulose into their corresponding ketoses such as L-ribulose, D-xylulose, D-tagatose, D-fructose, L-psicose and L-sorbose. The enzymatic reaction is a reversible equilibrium reaction. The L-ribose isomerase can be obtained from microorganisms of the genus Acinetobacter.

Abstract: Disclosed are a recombinant thermostable enzyme, which converts maltose into trehalose and is stable up to a temperature of about 80.degree. C. even when incubated at pH 7.0 for 60 min, a preparation of the enzyme, a DNA encoding the enzyme, a recombinant DNA containing the DNA, a transformant, and an enzymatic conversion method of maltose by using the enzyme.

Abstract: An L-ribose isomerase which isomerizes aldoses such as L-ribose, D-lyxose, D-talose, D-mannose, L-allose and L-gulose into their corresponding ketoses such as L-ribulose, D-xylulose, D-tagatose, D-fructose, L-psicose and L-sorbose. The enzymatic reaction is a reversible equilibrium reaction. The L-ribose isomerase can be obtained from microorganisms of the genus Acinetobacter.

Abstract: Disclosed are a polypeptide having a .beta.-fructofuranosidase activity obtainable by the expression of a microbial gene, a DNA encoding the polypeptide, a transformant obtained by introducing the DNA into an appropriate host, a process for producing the polypeptide comprising culturing the transformant to produce the polypeptide and collecting the produced polypeptide from the culture, and a method for fructofuranosyl transfer comprising a step of reacting a fructofuranosyl donor with a fructofuranosyl acceptor in the presence of the polypeptide.

Abstract: A DNA encoding an enzyme, which forms non-reducing saccharides having trehalose structure as an end unit from amylaceous saccharides having a degree of glucose polymerization of 3 or higher, enables an industrial-scale production of a recombinant enzyme with such enzyme activity. Non-reducing saccharides obtainable by the recombinant enzyme can be used in a variety of food products, cosmetics, pharmaceuticals and feeds because of their substantial non-reducibility, mild and high-quality sweetness, adequate viscosity, and moisture-retaining ability.

Abstract: A DNA encoding an enzyme, which forms non-reducing saccharides having trehalose structure as an end unit from amylaceous saccharides having a degree of glucose polymerization of 3 or higher, enables an industrial-scale production of a recombinant enzyme with such enzyme activity. Non-reducing saccharides obtainable by the recombinant enzyme can be used in a variety of food products, cosmetics, pharmaceuticals and feeds because of their substantial non-reducibility, mild and high-quality sweetness, adequate viscosity, and moisture-retaining ability.

Abstract: A DNA encoding an enzyme, which forms non-reducing saccharides having trehalose structure as an end unit from amylaceous saccharides having a degree of glucose polymerization of 3 or higher, enables an industrial-scale production of a recombinant enzyme with such enzyme activity. Non-reducing saccharides obtainable by the recombinant enzyme can be used in a variety of food products, cosmetics, pharmaceuticals and feeds because of their substantial non-reducibility, mild and high-quality sweetness, adequate viscosity, and moisture-retaining ability.

Abstract: An L-ribose isomerase which isomerizes aldoses such as L-ribose, D-lyxose, D-talose, D-mannose, L-allose and L-gulose into their corresponding ketoses such as L-ribulose, D-xylulose, D-tagatose, D-fructose, L-psicose and L-sorbose. The enzymatic reaction is a reversible equilibrium reaction. The L-ribose isomerase can be obtained from microorganisms of the genus Acinetobacter.

Abstract: Disclosed are a DNA encoding an enzyme which releases trehalose from non-reducing saccharides having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher, recombinant DNA and enzyme, transformant, and their preparations and uses. These facilitate the industrial-scale production of trehalose with a relative easiness and low cost, and trehalose thus obtained can be satisfactorily used in a variety of food products, cosmetics and pharmaceuticals.

Abstract: Disclosed are a DNA encoding an enzyme which releases trehalose from non-reducing saccharides having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher, recombinant DNA and enzyme, transformant, and their preparations and uses. These facilitate the industrial-scale production of trehalose with a relative easiness and low cost, and trehalose thus obtained can be satisfactorily used in a variety of food products, cosmetics and pharmaceuticals.

Abstract: L-Ketohexoses such as L-fructose and L-tagatose are produced from L-psicose and L-sorbose as substrates by allowing D-ketohexose 3-epimerase to act on these substrates. The yield and the production cost of the produced L-fructose and L-tagatose are industrially acceptable. The enzyme is preparable from microorganisms, e.g. those of the genus Pseudomonas.

Abstract: Disclosed are a recombinant thermostable enzyme, which converts maltose into trehalose and is stable up to a temperature of about 80.degree. C. even when incubated at pH 7.0 for 60 min, a preparation of the enzyme, a DNA encoding the enzyme, a recombinant DNA containing the DNA, a transformant, and an enzymatic conversion method of maltose by using the enzyme.

Abstract: A recombinant enzyme, having a molecular weight of about 57,000-67,000 daltons on SDS-PAGE and a pI of about 4.1-5.1 on isoelectrophoresis, which converts maltose into trehalose and vice versa. Depending on the enzymatic conditions, the enzyme forms about 70 w/w % of trehalose when acts on maltose, while about 20 w/w % of maltose when acts on trehalose. The culture of a transformant, prepared by introducing into a host a recombinant DNA containing a DNA coding for the enzyme and a self-replicable vector, facilitates the industrial-scale production of trehalose.