turanose has been researched along with trehalulose* in 4 studies
1 review(s) available for turanose and trehalulose
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Sucrose isomers as alternative sweeteners: properties, production, and applications.
In the daily diet, sweeteners play an indispensable role. Among them, sucrose, a widely occurring disaccharide in nature, is a commonly used sweetener. However, the intake of sucrose can cause a rapid increase in blood glucose, which leads to a number of health problems. Therefore, there is an urgent need for possible alternatives to sucrose. Currently, four naturally occurring sucrose isomers, trehalulose, turanose, leucrose, and isomaltulose are considered to be possible alternatives to sucrose due to their suitable sweetness, potential physiological benefits, and feasible production processes. This review covers the properties of these alternative sweeteners, including their structure, sweetness, hydrolysis rate, toxicology, and cariogenicity, and exhibits their potential applications in chronic diseases management, anti-inflammatory supplement, prebiotic dietary supplement, and stabilizing agent. The biosynthesis of these sucrose isomers using carbohydrate-active enzymes and their industrial production processes are also systematically summarized. Topics: Diet; Disaccharides; Food; Humans; Isomaltose; Isomerism; Sucrose; Sweetening Agents; Taste | 2019 |
3 other study(ies) available for turanose and trehalulose
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Comparative study on four amylosucrases from Bifidobacterium species.
Amylosucrase (ASase) is α-glucan-producing enzyme. Four putative ASase genes (bdas, blas, bpas, and btas) were cloned from Bifidobacterium sp. and expressed in Escherichia coli. All ASases from Bifidobacterium sp. (BAS) displayed typical ASase properties with slightly different characteristics. Among the BASs studied, BdAS and BpAS showed maximal enzyme activities at 35 and 30 °C, respectively, whereas BlAS and BtAS were maximally active at higher temperatures, i.e., 45 and 50 °C, respectively. BpAS exhibited optimum pH under slightly basic conditions (pH 8.0), while BdAS, BlAS, and BtAS preferred weakly acidic conditions (pH 5.0-6.0). All BASs showed higher isomerization activities. Particularly, BlAS produced more trehalulose than turanose. Although polymerization was the highest for BtAS, BtAS synthesized α-1, 4-glucans with a lower degree of polymerization than that of the other BASs. The versatile properties of the BASs described could contribute to the efficient production of highly valuable biomaterials for the agriculture, food, and pharmaceutical industries. Topics: Amino Acid Sequence; Bacterial Proteins; Bifidobacterium; Cloning, Molecular; Disaccharides; Enzyme Stability; Glucans; Glucosyltransferases; Hot Temperature; Sequence Homology; Substrate Specificity | 2020 |
Phosphorylation and metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-fructoses by Klebsiella pneumoniae.
Not only sucrose but the five isomeric alpha-D-glucosyl-D-fructoses trehalulose, turanose, maltulose, leucrose, and palatinose are utilized by Klebsiella pneumoniae as energy sources for growth, thereby undergoing phosphorylation by a phosphoenolpyruvate-dependent phosphotransferase system uniformly at 0-6 of the glucosyl moiety. Similarly, maltose, isomaltose, and maltitol, when exposed to these conditions, are phosphorylated regiospecifically at O-6 of their non-reducing glucose portion. The structures of these novel compounds have been established unequivocally by enzymatic analysis, acid hydrolysis, FAB negative-ion spectrometry, and 1H and 13C NMR spectroscopy. In cells of K. pneumoniae, hydrolysis of sucrose 6-phosphate is catalyzed by sucrose 6-phosphate hydrolase from Family 32 of the glycosylhydrolase superfamily. The five 6'-O-phosphorylated alpha-D-glucosyl-fructoses are hydrolyzed by an inducible (approximately 49-50 Kda) phospho-alpha-glucosidase from Family 4 of the glycosylhydrolase superfamily. Topics: alpha-Glucosidases; Amino Acid Sequence; beta-Fructofuranosidase; Carbohydrate Conformation; Chromatography, Thin Layer; Disaccharides; Fructose; Glycoside Hydrolases; Hydrolysis; Immunoblotting; Isomaltose; Isomerism; Klebsiella pneumoniae; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Molecular Structure; Phosphorylation; Sucrose | 2001 |
Amylosucrase from Neisseria polysaccharea: novel catalytic properties.
Amylosucrase is a glucosyltransferase that synthesises an insoluble alpha-glucan from sucrose. The catalytic properties of the highly purified amylosucrase from Neisseria polysaccharea were characterised. Contrary to previously published results, it was demonstrated that in the presence of sucrose alone, several reactions are catalysed, in addition to polymer synthesis: sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis - these two sucrose isomers being obtained by glucosyl transfer onto fructose. The effect of initial sucrose concentration on initial activity demonstrated a non-Michaelian profile never previously described. Topics: Catalysis; Chromatography, High Pressure Liquid; Disaccharides; Dose-Response Relationship, Drug; Fructose; Glucose; Glucosyltransferases; Hydrolysis; Isomerism; Kinetics; Magnetic Resonance Spectroscopy; Maltose; Neisseria; Polymers; Solubility; Sucrose; Trisaccharides | 2000 |