1109-28-0

Usage

Uses

1. Used in Pharmaceutical Applications:
Maltotriose is used as an anti-human immunodeficiency virus (HIV) agent, displaying potent and selective in vitro activity against human immunodeficiency virus type 1. It is prepared by modification of lysine e-amino groups, making it a promising candidate for the development of new antiviral therapies.
2. Used in Microbiology Research:
Maltotriose serves as a matrose regulon inducer in Escherichia coli, playing a crucial role in the study of bacterial metabolism and regulation. It has been used in research to investigate the influence of fourth-generation poly(propyleneimine) dendrimers on blood cells, contributing to the understanding of bacterial responses to various stimuli.
3. Used in Food Industry:
As a trisaccharide, Maltotriose can be utilized in the food industry for various purposes, such as a sweetener or a component in the production of other food products. Its unique properties may also contribute to the development of new food products with enhanced nutritional profiles or improved taste and texture.
4. Used in Chemical Research:
Maltotriose's chemical properties, including its white crystalline powder form, make it an interesting subject for chemical research. It can be used to study the properties of trisaccharides and their interactions with other molecules, potentially leading to the development of new materials or applications in various industries.

InChI:InChI=1/C18H32O16/c19-1-4-7(22)8(23)12(27)17(31-4)34-15-6(3-21)32-18(13(28)10(15)25)33-14-5(2-20)30-16(29)11(26)9(14)24/h4-29H,1-3H2/t4-,5-,6-,7-,8+,9-,10-,11-,12-,13-,14-,15-,16?,17-,18-/m1/s1

Upstream product

• 69-79-4 D-maltose 
• 7585-39-9 β‐cyclodextrin 
• 1184-46-9 D-maltohexaose 
• 104723-62-8 6-O-α-D-maltotriosyl-β-cyclodextrin 
• 112269-47-3 6-O-α-(6²-O-α-maltotriosyl)maltotriosyl-cG7 
• 112240-48-9 6^A,6^D-di-O-α-maltotriosyl-cG7 
• 112269-46-2 6-O-α-(6³-O-α-maltotriosyl)maltotriosyl-cG7 
• 2216-51-5 (-)-menthol 
• 118291-90-0 2-chloro-4-nitrophenol-α-D-maltotrioside 
• 1263-76-9 maltotetraose 
• 142831-49-0 O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-O-(α-D-glucopyranosyl)-(1->4)-α-D-glucopyranosyl-α-D-glucopyranoside 
• 9057-02-7 pullulan 
• 57-50-1 Sucrose 
• 754201-87-1 2,4-dinitrophenyl α-maltotrioside 

Downstream Products

• 50-99-7 D-glucose 
• 1141738-22-8 C₄₅H₆₃NO₁₉S 
• 1196681-94-3 C₄₄H₆₅N₅O₂₀ 
• 61139-07-9 1,2,3,6-tetra-O-acetyl-4-O-(2,3,6-tri-O-acetyl-4-O-(2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl)-α-D-glucopyranosyl)-D-glucopyranose 
• 17690-94-7 (2S,3R,4S,5R,6R)-6-(acetoxymethyl)-5-((2R,3R,4S,5R,6R)-3,4-diacetoxy-6-(acetoxymethyl)-5-((2R,3R,4S,5R,6R)-3,4,5-triacetoxy-6-(acetoxymethyl)tetrahydro-2H-pyran-2-yloxy)tetrahydro-2H-pyran-2-yloxy)tetrahydro-2H-pyran-2,3,4-triyl triacetate 
• 375372-11-5 acarviosyl-maltotetraose 
• 91-19-0 2,3-diethynylquinoxaline 
• 32706-29-9 2-(2',3'-dihydroxypropyl)quinoxaline 
• 42015-36-1 2-methyl-3-(2',3'-dihydroxypropyl)quinoxaline 
• 10058-19-2 6-O-α-D-Glucopyranosyl α-cyclodextrin 
• 499-40-1 isomaltose 

Related news

Characterization of maltose and MALTOTRIOSE (cas 1109-28-0) transport in the acarbose-producing bacterium Actinoplanes sp.08/16/2019

Acarbose, a pseudomaltotetraose, is produced by strains of the genus Actinoplanes. The compound is an inhibitor of α-glucosidases and is used in the treatment of patients suffering from type II diabetes. The benefits of acarbose for the producer are not known; however, a role as carbophor has b...detailed

MALTOTRIOSE (cas 1109-28-0) syrup preparation from pullulan using pullulanase08/15/2019

Pullulan production was carried out at shake-flask level and purified with isopropanol precipitation using single-step purification strategy. Purified pullulan obtained was used for preparing maltotriose syrup using pullulanase. Pullulanase was subjected to kinetic and thermodynamic characteriza...detailed

Preparation of MALTOTRIOSE (cas 1109-28-0) from fermentation broth by hydrolysis of pullulan using pullulanase08/13/2019

In this study, we prepared maltotriose from the fermentation broth of Auerobasidium Pullulans CJ001 isolated from the sea mud by hydrolysis of pullulan with pullulanase. The fermentation broth was centrifuged to remove the microorganisms and then hydrolysed by pullulanase. The optimal hydrolysis...detailed

Relevant academic research and scientific papers

Kinetics of maltooligosaccharide hydrolysis in subcritical water

The kinetics of the hydrolysis of maltooligosaccharides with a degree of polymerization (DP) of 3-6 in subcritical water was studied using a tubular reactor at temperatures between 200 and 260°C and at a constant pressure of 10 MPa. The maltooligosaccharide disappearance and product formation at residence times shorter than 50 s could be expressed by first-order kinetics. The rate constants for the hydrolysis of each maltooligosaccharide were evaluated. There was a tendency that the exo-site glucosidic bond was hydrolyzed faster than the endo-site one irrespective of the DP of the maltooligosaccharide. The hydrolysis of the maltooligosaccharides was consecutively preceded, and the time dependence of the hydrolysis for maltooligosaccharides with different DPs could be calculated by simultaneously solving the mass balance equations for all the possible saccharides.

Anomer-Selective Glucosylation of l-Menthol by Yeast α-Glucosidase

l-Menthol was glucosylated by the α-glucosidase (EC 3.2.1.20) of Saccharomyces cerevisiae using maltose as the glucosyl donor. When 50 mg of l-menthol and 1.6 M maltose in 10 mM citrate-phosphate buffer (pH 5.5) were incubated at 45°C, l-menthyl α-D-glucopyranoside (α-MenG) was α-anomer-selectively formed as a product. The specificity of the α-linkage was confirmed by 13C-NMR analysis. In the reaction mixture after 2 h, α-MenG was mainly accumulated in a crystalline form and the concentration of dissolved α-MenG was constant at 1.4 mM. The molar conversion yield of α-MenG produced based on the supplied l-menthol was maximally 30.7% at 48 h of reaction.

GLYCOSIDE COMPOUND

Compounds of formula (I″) wherein: R11, R12, R13, R14 and R15 are hydrogen, hydroxyl, C1-6 alkyl, C1-6 alkoxy, C1-6 alkyl-carbonyloxy, or a G-O— group, and at least one of R11, R12, R13, R14 and R15 is a G-O— group, wherein G is a saccharide residue,X1 is a single bond, or a methylene group, an ethylene group, a trimethylene group, a vinylene group or —CH═CH—CH2—,X2 is —CO—O— or —O—CO—,p and q are integer ofs 0 to 7, and p+q=0 to 8,Y1 is methylene, ethylene or an alkenylene group having a carbon number of 2 to 15 and 1 to 3 double bonds, andR16 and R17 are hydrogen, methyl or ethyl, or R16 and R17 form a C3-6 cycloalkyl group, are useful as GLP-1 secretion promoting agents.

Regioselective glucosylation of inositols catalyzed by Thermoanaerobacter sp. CGTase

Monoglucosylated products of l-chiro-, d-chiro-, muco-, and allo-inositol were synthesized by regioselective α-d-glucosylation with cyclodextrin glucosyl transferase from Thermoanaerobacter sp. after hydrolysis of by products with Aspergillus niger glucoamylase. While the reactions carried out with d-chiro-, muco-, and allo-inositol resulted in the regioselective formation of monoglucosylated products, two products were obtained in the reaction with l-chiro-inositol. Through the structural characterization of the glucosylated inositols here we demonstrated that the selectivity observed in the glucosylation of several inositols by Thermoanaerobacter sp. CGTase, is analogous to the specificity observed for the glucosylation of β-d-glucopyranose and equivalent glucosides.

Branched alpha-glucan, alpha-glucosyltransferase which forms the glucan, their preparation and uses

The present invention has objects to provide a glucan useful as water-soluble dietary fiber, its preparation and uses. The present invention solves the above objects by providing a branched α-glucan, which is constructed by glucose molecules and characterized by methylation analysis as follows: (1) Ratio of 2,3,6-trimethyl-1,4,5-triacetyl-glucitol to 2,3,4-trimethyl-1,5,6-triacetyl-glucitol is in the range of 1:0.6 to 1:4;(2) Total content of 2,3,6-trimethyl-1,4,5-triacetyl-glucitol and 2,3,4-trimethyl-1,5,6-triacetyl-glucitol is 60% or higher in the partially methylated glucitol acetates;(3) Content of 2,4,6-trimethyl-1,3,5-triacetyl-glucitol is 0.5% or higher but less than 10% in the partially methylated glucitol acetates; and(4) Content of 2,4-dimethyl-1,3,5,6-tetraacetyl-glucitol is 0.5% or higher in the partially methylated glucitol acetates; a novel α-glucosyltransferase which forms the branched α-glucan, processes for producing them, and their uses.

COMBINED USE OF DIPEPTIDYL PEPTIDASE IV INHIBITOR COMPOUND AND SWEETENER

The present invention provides a novel therapeutic or preventive method, a pharmaceutical composition and use thereof, that exhibit superior anti-obesity effects (body weight-reducing (losing) effects and/or body fat mass-reducing effects). Specifically, the present invention provides a pharmaceutical composition comprising the combination of a dipeptidyl peptidase 4 inhibitor and a sweetener having a GLP-1 secretion-stimulating action, as well as use thereof for the manufacture of a medicament. The present invention also provides a method for treating or preventing obesity, comprising administering an effective amount of (a) a dipeptidyl peptidase 4 inhibitor and (b) a sweetener having a GLP-1 secretion-stimulating action to a patient suffering from symptoms of obesity.

Molecular cloning and functional expression of a new amylosucrase from Alteromonas macleodii

The presence of amylosucrase in 12 Alteromonas and Pseudoalteromonas strains was examined. Two Alteromonas species (Alteromonas addita KCTC 12195 and Alteromonas macleodii KCTC 2957) possessed genes that had high sequence homology to known amylosucrases. Genomic clones containing the ASase analogs were obtained from A. addita and A. macleodii, and the deduced amino acid sequences of the corresponding genes (aaas and amas, respectively) revealed that they were highly similar to the ASases of Neisseria polysaccharea, Deinococcus radiodurans, and Deinococcus geothermalis. Functional expression of amas in Escherichia coli was successful, and typical ASase activity was detected in purified recombinant AMAS, whereas the purified recombinant AAAS was nonfunctional. Although maximum total activity of AMAS was observed at 45 °C, the ratio of transglycosylation to total activity increased as the temperature decreased from 55 to 25 °C. These results imply that transglycosylation occurs preferentially at lower temperatures while hydrolysis is predominant at higher temperatures.

Isolation and characterization of a novel thermostable neopullulanase-like enzyme from a hot spring in Thailand

A gene encoding a thermostable pullulan-hydrolyzing enzyme was isolated from environmental genomic DNA extracted from soil sediments of Bor Khleung hot spring in Thailand. Sequence comparison with related enzymes suggested that the isolated enzyme, designated Env Npu193A, was most likely a neopullulanase-like enzyme. Env Npu193A was expressed in Pichia pastoris as a monomeric recombinant protein. The purified Env Npu193A exhibited pH stability ranging from 3 to 9. More than 60% of enzyme activity was retained after incubation at 60°C for 1 h. Env Npu193A was found to hydrolyze various substrates, including pullulan, starch, and γ-cyclodextrin. The optimal working condition for Env Npu193A was at pH 7 at 75°C with Km and Vmax toward pullulan of 1.22 ± 0.3% and 23.24 ± 1.7 U/mg respectively. Env Npu193A exhibited distinct biochemical characteristics as compared with the previously isolated enzyme from the same source. Thus, a culture-independent approach with sequence-basing was found to be an effective way to discover novel enzymes displaying unique substrate specificity and high thermostability from natural bioresources.

ACCELERATOR FOR MINERAL ABSORPTION AND USE THEREOF

The present invention has an object to provide an accelerator for mineral absorption and a composition containing the accelerator. The object is solved by providing an accelerator for mineral absorption comprising cyclic tetrasaccharide and/or saccharide derivatives thereof and a composition containing the accelerator.

Expression, purification, and characterization of the maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

The maltooligosyltrehalose trehalohydrolase (MTHase) mainly cleaves the α-1,4-glucosidic linkage next to the α-1,1-linked terminal disaccharide of maltooligosyltrehalose to produce trehalose and the maltooligosaccharide with lower molecular mass. In this study, the treZ gene encoding MTHase was PCR-cloned from Sulfolobus solfataricus ATCC 35092 and then expressed in Escherichia coli. A high yield of the active wild-type MTHase, 13300 units/g of wet cells, was obtained in the absence of IPTG induction. Wild-type MTHase was purified sequentially using heat treatment, nucleic acid precipitation, and ion-exchange chromatography. The purified wild-type MTHase showed an apparent optimal pH of 5 and an optimal temperature at 85°C. The enzyme was stable at pH values ranging from 3.5 to 11, and the activity was fully retained after a 2-h incubation at 45-85°C. The kcat values of the enzyme for hydrolysis of maltooligosyltrehaloses with degree of polymerization (DP) 4-7 were 193, 1030, 1190, and 1230 s-1, respectively, whereas the kcat values for glucose formation during hydrolysis of DP 4-7 maltooligosaccharides were 5.49, 17.7, 18.2, and 6.01 s-1, respectively. The KM values of the enzyme for hydrolysis of DP 4-7 maltooligosyltrehaloses and those for maltooligosaccharides are similar at the same corresponding DPs. These results suggest that this MTHase could be used to produce trehalose at high temperatures.