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 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 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 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 trehalose-releasing enzyme which specifically hydrolyzes 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. The molecular weight of the enzyme is about 57,000 to 68,000 daltons on SDS-PAGE, and the isoelectric point is about 3.3 to 4.6 on isoelectrophoresis. The enzyme is useful in an industrial-scale preparation of trehalose, and the trehalose prepared therewith can be readily incorporated into food products, as well as cosmetic- and pharmaceutical-compositions.

Abstract: Disclosed is a trehalose-releasing enzyme which specifically hydrolyzes 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. The molecular weight of the enzyme is about 57,000 to 68,000 daltons on SDS-PAGE, and the isoelectric point is about 3.3 to 4.6 on isoelectrophoresis. The enzyme is useful in an industrial-scale preparation of trehalose, and the trehalose prepared therewith can be readily incorporated into food products, as well as cosmetic- and pharmaceutical-compositions.

Abstract: A trehalose-releasing enzyme is obtained which specifically hydrolyzes 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. The molecular weight of the enzyme is about 57,000 to 68,000 daltons on SDS-PAGE, and the isoelectric point is about 3.3 to 4.6 on isoelectrophoresis. The enzyme is preferably obtained from Rhizobium sp. FERM BP-4130 or Arthrobacter sp. FERM BP-4316, and may also be obtained from members of the genera Brevibacterium and Micrococcus. The enzyme is useful in an industrial-scale preparation of trehalose, and the trehalose prepared therewith can be readily incorporated into food products, as well as cosmetic- and pharmaceutical-compositions.

Abstract: Disclosed is a novel non-reducing saccharide-forming enzyme. The enzyme can be obtained from the culture of microorganisms such as Rhizobium sp. M-11 (FERM BP 4130) and Arthrobacter sp. Q36 (FERM BP-4316), and is capable of forming non-reducing saccharides having a trehalose structure when allowed to act on reducing partial starch hydrolysates having a degree of polymerization of 3 or greater. Glucoamylase and .alpha.-glucosidase readily yield trehalose when allowed to act on the non-reducing saccharides. These non-reducing saccharides and trehalose are useful in food products, cosmetics and pharmaceuticals.