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 is a recombinant thermostable enzyme which has a molecular weight of about 69,000-79,000 daltons and a pI of about 5.4-6.4, and forms non-reducing saccharides having a trehalose structure as an end unit from reducing amylaceous saccharides having a degree of glucose polymerization of at least 3. The enzyme has satisfactorily high thermostability, i.e. it is substantially not inactivated even when incubated in an aqueous solution (pH 7.0) at 85° C. for 60 min, and this facilitates the production of such non-reducing saccharides on an industrial scale and in a satisfactorily-high yield.

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: Disclosed is a recombinant thermostable enzyme which has a molecular weight of about 54,000-64,000 daltons and a pI of about 5.6-6.6, and releases trehalose from non-reducing saccharides having a trehalose structure as an end unit and a degree of glucose polymerization of at least 3. The enzyme has a satisfactorily-high thermostability, i.e. it is not substantially inactivated even when incubated in an aqueous solution (pH 7.0) at 85° C. for 60 min, and this facilitates the production of trehalose on an industrial scale and in a satisfactorily-high yield.

Abstract: Disclosed are a composition for inhibiting body odor which comprises trehalose and/or maltitol as an effective ingredient, a method for inhibiting body odor by using the composition, and an article incorporated with the composition.

Abstract: A kojibiose phosphorylase which hydrolyzes kojibiose in the presence of an inorganic phosphoric acid to form D-glucose and &bgr;-D-glucose-1-phosphoric acid, forms kojibiose and an inorganic phosphoric acid from &bgr;-D-glucose-1-phosphoric acid, and catalyzes the transfer reaction of glucosyl group to other saccharides using &bgr;-D-glucose-1-phosphoric acid as a saccharide donor. The enzyme is obtainable from natural sources such as microorganisms of the genus Thermoanaerobium, and obtainable by recombinant technology. Kojibiose phosphorylase is used to transfer glucose from glucose-1-phosphate to acceptor saccharides to produce &agr;-D-glucosyl-1(1→5)-L-sorbose, kojibiosylglucose, kojibiosylglucoside and kojibiosylfructoside.

Abstract: Disclosed are novel thermostable trehalose-releasing enzyme, and its preparations and uses. The enzyme is obtainable from the culture of microorganisms such as Sulfolobus acidocaldarius (ATCC 33909 and ATCC 49426) and Sulfolobus solfataricus (ATCC 35091 and ATCC 35092), and capable of hydrolyzing at a temperature of over 55.degree. C. the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher. Trehalose and compositions containing the same are extensively useful in food products, cosmetics and pharmaceuticals.

Abstract: A kojibiose phosphorylase which hydrolyzes kojibiose in the presence of an inorganic phosphoric acid to form D-glucose and .beta.-D-glucose-1-phosphoric acid, forms kojibiose and an inorganic phosphoric acid from .beta.-D-glucose-1-phosphoric acid, and catalyzes the transfer reaction of glucosyl group to other saccharides using .beta.-D-glucose-1-phosphoric acid as a saccharide donor. The enzyme is obtainable from natural sources such as microorganisms of the genus Thermoanaerobium, and obtainable by recombinant technology.

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 kojibiose phosphorylase which hydrolyzes kojibiose in the presence of an inorganic phosphoric acid to form D-glucose and .beta.-D-glucose-1-phosphoric acid, forms kojibiose and an inorganic phosphoric acid from .beta.-D-glucose-1-phosphoric acid, and catalyzes the transfer reaction of glucosyl group to other saccharides using .beta.-D-glucose-1-phosphoric acid as a saccharide donor. The enzyme is obtainable from natural sources such as microorganisms of the genus Thermoanaerobium, and obtainable by recombinant technology.

Abstract: Disclosed is a recombinant thermostable enzyme which has a molecular weight of about 54,000-64,000 daltons and a pI of about 5.6-6.6, and releases trehalose from non-reducing saccharides having a trehalose structure as an end unit and a degree of glucose polymerization of at least 3. The enzyme has a satisfactorily-high thermostability, i.e. it is not substantially inactivated even when incubated in an aqueous solution (pH 7.0) at 85.degree. C. for 60 min, and this facilitates the production of trehalose on an industrial scale and in a satisfactorily-high yield.

Abstract: Disclosed are novel non-reducing saccharide-forming enzyme, and its preparation and uses. The enzyme is obtainable from the culture of microorganisms such as Rhizobium sp. M-11 (FERM BP 4130) and Arthrobacter sp. Q36 (FERM BP-4316), and capable of forming non-reducing saccharides having a trehalose structure when allowed to act on reducing partial starch hydrolysates. Glucoamylase and .alpha.-glucosidase readily yield trehalose when allowed to act on the non-reducing saccharides. These non-reducing saccharides and trehalose are extensively useful in food products, cosmetics and pharmaceuticals.

Abstract: A thermostable trehalose phosphorylase which is obtainable from microorganisms of the genus Thermoanaerobium and which hydrolyzes trehalose in the presence of an inorganic phosphoric acid to form D-glucose and .beta.-D-glucose-1-phosphoric acid. The trehalose phosphorylase can be also prepared by recombinant DNA technology. When the enzyme is allowed to contact with .beta.-D-glucose-1-phosphoric acid as a saccharide donor in the presence of other saccharides, glucosyl-transferred saccharides including glucosyl-D-galactoside, which are conventionally known but scarcely obtainable, can be produced on an industrial-scale and in a relatively-low cost.

Abstract: Disclosed is a recombinant thermostable enzyme which has a molecular weight of about 69,000-79,000 daltons and a pI of about 5.4-6.4, and forms non-reducing saccharides having a trehalose structure as an end unit from reducing amylaceous saccharides having a degree of glucose polymerization of at least 3. The enzyme has satisfactorily high thermostability, i.e. it is substantially not inactivated even when incubated in an aqueous solution (pH 7.0) at 85.degree. C. for 60 min, and this facilitates the production of such non-reducing saccharides on an industrial scale and in a satisfactorily-high yield.

Abstract: A kojibiose phosphorylase which hydrolyzes kojibiose in the presence of an inorganic phosphoric acid to form .beta.-glucose and .beta.-D-glucose-1-phosphoric acid, forms kojibiose and an inorganic phosphoric acid from .beta.-D-glucose-1-phosphoric acid, and catalyzes the transfer reaction of glucosyl group to other saccharides using .beta.-D-glucose-1-phosphoric acid as a saccharide donor. The enzyme is obtainable from Thermoanaerobium brockii and obtainable by recombinant technology.

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 polypeptide possessing maltotetraose-forming amylase activity with a revealed amino acid sequence. The polypeptide has features that it acts on starch to mainly produce maltotetraose, and that it has a molecular weight of 50,000.+-.10,000 when electrophoresed on SDS-polyacrylamide gel.The polypeptide can be advantageously used in industrial process.

Abstract: Disclosed are novel non-reducing saccharide-forming enzyme, and its preparation and uses. The enzyme is obtainable from the culture of microorganisms such as Rhizobium sp. M-11 (FERM BP 4130) and Arthrobacter sp. Q36 (FERM BP-4316), and capable of forming non-reducing saccharides having a trehalose structure when allowed to act on reducing partial starch hydrolysates. Glucoamylase and .alpha.-glucosidase readily yield trehalose when allowed to act on the non-reducing saccharides. These non-reducing saccharides and trehalose are extensively useful in food products, cosmetics and pharmaceuticals.

Abstract: Disclosed is a recombinant thermostable enzyme which has a molecular weight of about 69,000-79,000 daltons and a pI of about 5.4-6.4, and forms non-reducing saccharides having a trehalose structure as an end unit from reducing amylaceous saccharides having a degree of glucose polymerization of at least 3. The enzyme has satisfactorily high thermostability, i.e. it is substantially not inactivated even when incubated in an aqueous solution (pH 7.0) at 85.degree. C. for 60 min, and this facilitates the production of such non-reducing saccharides on an industrial scale and in a satisfactorily-high yield.

Abstract: A thermostable trehalose phosphorylase which is obtainable from microorganisms of the genus Thermoanaerobium and which hydrolyzes trehalose in the presence of an inorganic phosphoric acid to form D-glucose and .beta.-D-glucose-1-phosphoric acid. The trehalose phosphorylase can be also prepared by recombinant DNA technology. When the enzyme is allowed to contact with .beta.-D-glucose-1-phosphoric acid as a saccharide donor in the presence of other saccharides, glucosyl-transferred saccharides including glucosyl-D-galactoside, which are conventionally known but scarcely obtainable, can be produced on an industrial-scale and in a relatively-low cost.