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: Non-reducing saccharides including alpha-glycosyl trehaloses, alpha-glycosyl alpha-glycosides and trehalose are easily produced by cultivating microorganisms capable of producing non-reducing saccharide-forming enzyme in nutrient culture media which contain reducing partial starch hydrolysates with glucose polymerization degrees of 3 or higher. The yields for these saccharides are significantly improved by further subjecting the reducing partial starch hydrolysates to starch-debranching enzyme and/or cyclomaltodextrin glucanotransferase in or not in culture media. The resultant non- or less-reducing saccharides commonly bear desirable properties in addition to a mild and gentle sweetness. Thus they would find extensive uses in a variety of compositions including food products, cosmetics and medicines.

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: 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: 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 industial 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.

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: 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.

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: 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 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 novel .alpha.-glycosyl derivative of a catecholamine or its salt, said .alpha.-glycosyl derivative being prepared by allowing a saccharide-transferring enzyme together with or without glucoamylase to act on a solution containing an .alpha.-glucosyl saccharide and one of catecholamines in order to form an .alpha.-glycosyl derivative of said catecholamines, and recovering the resultant .alpha.-glycosyl derivative. The .alpha.-glycosyl derivative overcomes conventional drawbacks of catecholamines, and does not substantially exhibit or have a reducing activity and undesirable toxicity, but has a relatively-high stability and exerts the inherent physiological activities of catecholamines in vivo. Thus, the .alpha.-glycosyl derivative is advantageously used as a variety of pharmaceuticals in the form of an injection, tablet, etc.

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. Also disclosed is a method of crystallizing trehalose from a 65 to 90% aqueous solution in the absence of organic solvent.

Abstract: Disclosed is a novel .alpha.-glycosyl derivative of a catecholamine or its salt, said .alpha.-glycosyl derivative being prepared by allowing a saccharide-transferring enzyme together with or without glucoamylase to act on a solution containing an .alpha.-glucosyl saccharide and one of catecholamines in order to form an .alpha.-glycosyl derivative of said catecholamines, and recovering the resultant .alpha.-glycosyl derivative. The .alpha.-glycosyl derivative overcomes conventional drawbacks of catecholamines, and does not substantially exhibit or have a reducing activity and undesirable toxicity, but has a relatively-high stability and exerts the inherent physiological activities of catecholamines in vivo. Thus, the .alpha.-glycosyl derivative is advantageously used as a variety of pharmaceuticals in the form of an injection, tablet, etc.

Abstract: Disclosed is a novel .alpha.-glycosyl derivative of a catecholamine or its salt, said .alpha.-glycosyl derivative being prepared by allowing a saccharide-transferring enzyme together with or without glucoamylase to act on a solution containing an .alpha.-glucosyl saccharide and one of catecholamines in order to form an .alpha.-glycosyl derivative of said catecholamines, and recovering the resultant .alpha.-glycosyl derivative. The .alpha.-glycosyl derivative overcomes conventional drawbacks of catecholamines, and does not substantially exhibit or have a reducing activity and undesirable toxicity, but has a relatively-high stability and exerts the inherent physiological activities of catecholamines in vivo. Thus, the .alpha.-glycosyl derivative is advantageously used as a variety of pharmaceuticals in the form of an injection, tablet, etc.

Abstract: Disclosed is a novel .alpha.-glycosyl derivative of a catecholamine or its salt, said .alpha.-glycosyl derivative being prepared by allowing a saccharide-transferring enzyme together with or without glucoamylase to act on a solution containing an .alpha.-glycosyl saccharide and one of catecholamines in order to form an .alpha.-glycosyl derivative of said catecholamines, and recovering the resultant .alpha.-glycosyl derivative. The .alpha.-glycosyl derivative overcomes conventional drawbacks of catecholamines, and does not substantially exhibit or have a reducing activity and undesirable toxicity, but has a relatively-high stability and exerts the inherent physiological activities of catecholamines in vivo. Thus, the .alpha.-glycosyl derivative is advantageously used as a variety of pharmaceuticals in the form of an injection, tablet, etc.