118396-93-3

Basic information

• Product Name: GALACTOSE BETA1,4-GALACTOSE BETA1,4-GLUCOSE
• Synonyms: GALACTOSE BETA1,4-GALACTOSE BETA1,4-GLUCOSE;GAL-BETA1,4GAL-BETA1,4GLC;B4-GALACTOSYL-LACTOSE;4-O-(4-O-B-D-GALACTOPYRANOSYL)-B-D-GALACTOPYRANOSYL)-D-GLUCOPYRANOSE;beta-globotriose;β-D-Gal-(1-4)-β-D-Gal-(1-4)-D-Glc, 4-O-(4-O-β-D-Galactopyranosyl-β-D-galactopyranosyl)-D-glucopyranose
• CAS NO: 118396-93-3
• Molecular Formula: C₁₈H₃₂O₁₆
• Molecular Weight: 504.44
• Mol File: 118396-93-3.mol

Chemical Properties

• Boiling Point: 865.2±65.0 °C(Predicted)
• Appearance: /
• Density: 1.80±0.1 g/cm3(Predicted)
• Storage Temp.: −20°C
• PKA: 12.02±0.70(Predicted)
• CAS DataBase Reference: GALACTOSE BETA1,4-GALACTOSE BETA1,4-GLUCOSE(CAS DataBase Reference)
• NIST Chemistry Reference: GALACTOSE BETA1,4-GALACTOSE BETA1,4-GLUCOSE(118396-93-3)
• EPA Substance Registry System: GALACTOSE BETA1,4-GALACTOSE BETA1,4-GLUCOSE(118396-93-3)

Safety Data

• Hazardous Substances Data: 118396-93-3(Hazardous Substances Data)

Upstream product

• 118291-90-0 2-chloro-4-nitrophenol-α-D-maltotrioside 
• 1263-76-9 Maltotetraose 
• 1263-76-9 O-β-D-mannopyranosyl-(1-4)-O-β-D-mannopyranosyl-(1-4)-O-β-D-mannopyranosyl-(1-4)-D-mannopyranose 
• 3482-57-3 p-nitrophenyl β-D-cellobioside 
• 2106-10-7 1-deoxy-1-fluoro-α-D-glucose 
• 528-50-7 cellobiose 
• 59-56-3 α-D-glucopyranosyl-1-phosphate 
• 9004-34-6 cellulose 
• 1184-46-9 D-maltohexaose 
• 104723-62-8 6-O-α-D-maltotriosyl-β-cyclodextrin 
• 1668-09-3 maltopentaose 
• 66451-58-9 4-nitrophenyl α-maltotrioside 
• 2216-51-5 (-)-menthol 
• 1263-76-9 maltotetraose 

Downstream Products

• 32860-62-1 α-D-glucopyranosyl-(1->4)-α-D-glucopyranosyl-(1->4)-D-glucitol 
• 492-62-6 alpha-D-glucopyranose 
• 1668-09-3 Maltopentaose 
• 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 
• 345319-76-8 5-O-α-D-glucopyranosyl-(+)-catechin 
• 345319-75-7 (+)-catechin 7-α-O-glucoside 
• 50-99-7 D-glucose 
• 21675-39-8 (2S,3R,4R,5R)-2,3,5,6-Tetrahydroxy-4-((2S,3S,4S,5S,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-hexanoic acid 
• 15548-43-3 O-β-D-mannopyranosyl-(1->4)-D-mannopyranose 
• 530-26-7 D-Mannose 
• 642-99-9 mannonic acid 

Relevant articles and documents

Supercritical water treatment for cello-oligosaccharide production from microcrystalline cellulose

Microcrystalline cellulose was treated in supercritical water at 380 °C and at a pressure of 250 bar for 0.2, 0.4, and 0.6 s. The yield of the ambient-water-insoluble precipitate and its average molar mass decreased with an extended treatment time. The highest yield of 42 wt % for DP2-9 cello-oligosaccharides was achieved after the 0.4 s treatment. The reaction products included also 11 wt % ambient-water-insoluble precipitate with a DPw of 16, and 6.1 wt % monomeric sugars, and 37 wt % unidentified degradation products. Oligo- and monosaccharide-derived dehydration and retro-aldol fragmentation products were analyzed via a combination of HPAEC-PAD-MS, ESI-MS/MS, and GC-MS techniques. The total amount of degradation products increased with treatment time, and fragmented (glucosyln-erythrose, glucosyln-glycolaldehyde), and dehydrated (glucosyln-levoglucosan) were identified as the main oligomeric degradation products from the cello-oligosaccharides.

Characterization and mechanism of action of Microbacterium imperiale glucan 1,4-α-maltotriohydrolase

In this study, glucan 1,4-α-maltotriohydrolase (AMTS) from Microbacterium imperiale was purified and characterized. Hydrolysis by AMTS was affected by starch structure (e.g., amylose versus amylopectin) and hydrolysis time. During the initial phase of hydrolysis of maltooligosaccharides (G4-G7), AMTS displayed a unique transfer specificity to the transfer of maltotriosyl units. After extensive hydrolysis, maltotriose became the major end product, followed by glucose and maltose. Maltotetraose (G4) was the smallest donor in transglycosylation reactions by AMTS. This is the first study that reports transglycosylation activity of AMTS on maltooligosaccharides. The results of this study suggest that high purity maltotriose can be produced by the hydrolytic action of AMTS on starch.

Hydrolysis of konjac glucomannan by Trichoderma reesei mannanase and endoglucanases Cel7B and Cel5A for the production of glucomannooligosaccharides

In this paper we describe the enzymatic hydrolysis of konjac glucomannan for the production of glucomannooligosaccharides using purified Trichoderma reesei mannanase, endoglucanases EGI (Tr Cel7b) and EGII (Tr Cel5a). Hydrolysis with each of the three enzymes produced a different pattern of oligosaccharides. Mannanase was the most selective of the three enzymes in the hydrolysis of konjac mannan and over 99% of the formed oligosaccharides had mannose as their reducing end pyranosyl unit. Tr Cel5A hydrolysate shared similarities with mannanase and Tr Cel7B hydrolysates and the enzyme had the lowest substrate specificity of the studied enzymes. The hydrolysate of Tr Cel7B contained a series of oligosaccharides with non-reducing end mannose (M) and reducing end glucose (G) (MG, MMG, MMMG, and MMMMG). These oligosaccharides were isolated from the hydrolysate by size exclusion chromatography in relatively high purity (86-95%) and total yield (23% of substrate). The isolated oligosaccharides were characterized using acid hydrolysis and HPAEC-PAD (carbohydrate composition), HPLC-RI and HPAEC-MS (to determine the DP of purified oligosaccharides), enzymatic hydrolysis (determination of non-reducing end carbohydrate) and NMR (both 1D and 2D, to verify structure and purity of purified compounds). Hydrolysis of konjac mannan with a specific enzyme, such as T. reesei Cel7B or mannanase, followed by fractionation with SEC offers the possibility to produce glucomannooligosaccharides with defined structure. The isolated oligosaccharides can be utilised as analytical standards, for determination of bioactivity of oligosaccharides with defined structure or as substrates for defining substrate specificity of novel carbohydrate hydrolyzing enzymes.

Structural and biochemical analyses of glycoside hydrolase families 5 and 26 β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis

The microbial deconstruction of the plant cell wall is a key biological process that is of increasing importance with the development of a sustainable biofuel industry. The glycoside hydrolase families GH5 (PaMan5A) and GH26 (PaMan26A) endo-β-1,4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradation of lignocellulosic biomass. In this study, P. anserina mannanases were further subjected to detailed comparative analysis of their substrate specificities, active site organization, and transglycosylation capacity. Although PaMan5A displays a classical mode of action, PaMan26A revealed an atypical hydrolysis pattern with the release of mannotetraose and mannose from mannopentaose resulting from a predominant binding mode involving the -4 subsite. The crystal structures of PaMan5A and PaMan26A were solved at 1.4 and 2.85 A resolution, respectively. Analysis of the PaMan26A structure supported strong interaction with substrate at the -4 subsite mediated by two aromatic residues Trp-244 and Trp-245. The PaMan26A structure appended to its family 35 carbohydrate binding module revealed a short and proline-rich rigid linker that anchored together the catalytic and the binding modules.

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.

The kinetics of p-nitrophenyl-β-d-cellobioside hydrolysis and transglycosylation by Thermobifida fusca Cel5Acd

The hydrolysis of p-nitrophenyl-β-1,4-cellobioside (pNP-G2) by the catalytic domain of the retaining-family 5-2 endocellulase Cel5A from Thermobifida fusca (Cel5Acd) was studied. The dominant reaction pathway involves hydrolysis of the aglyconic bond, producing cellobiose (G2) and a 'reporter' species p-nitrophenol (pNP), which was monitored spectrophotometrically to track the reaction. We also detected the production of cellotriose (G3) and p-nitrophenyl-glucoside (pNP-G1), confirming the presence of a competing transglycosylation pathway. We use a mechanistic model of hydrolysis and transglycosylation to derive an expression for the rate of pNP-formation as a function of enzyme concentration, substrate concentration, and several lumped kinetics parameters. The derivation assumes that the quasi-steady-state assumption (QSSA) applies for three intermediate species in the mechanism; we determine conditions under which this assumption is rigorously justified. We integrate the rate expression and compare its integral form to pNP-versus-time data collected for a range of enzyme and substrate concentrations. The integral comparison gives a stringent test of the mechanistic model, and it serves to quantify the lumped kinetics parameters with good statistical precision, particularly a previously unidentified parameter that determines the selectivity of hydrolysis versus transglycosylation. The integrated rate expression accounts well for pNP-versus-time data under all circumstances we have investigated.

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.

Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum

Inverting cellobiose phosphorylase (CtCBP) and cellodextrin phosphorylase (CtCDP) from Clostridium thermocellum ATCC27405 of glycoside hydrolase family 94 catalysed reverse phosphorolysis to produce cellobiose and cellodextrins in 57% and 48% yield from α-d-glucose 1-phosphate as donor with glucose and cellobiose as acceptor, respectively. Use of α-d-glucosyl 1-fluoride as donor increased product yields to 98% for CtCBP and 68% for CtCDP. CtCBP showed broad acceptor specificity forming β-glucosyl disaccharides with β-(1→4)- regioselectivity from five monosaccharides as well as branched β-glucosyl trisaccharides with β-(1→4)-regioselectivity from three (1→6)-linked disaccharides. CtCDP showed strict β-(1→4)-regioselectivity and catalysed linear chain extension of the three β-linked glucosyl disaccharides, cellobiose, sophorose, and laminaribiose, whereas 12 tested monosaccharides were not acceptors. Structure analysis by NMR and ESI-MS confirmed two β-glucosyl oligosaccharide product series to represent novel compounds, i.e. β-d-glucopyranosyl-[(1→4)- β-d-glucopyranosyl]n-(1→2)-d-glucopyranose, and β-d-glucopyranosyl-[(1→4)-β-d-glucopyranosyl]n- (1→3)-d-glucopyranose (n = 1-7). Multiple sequence alignment together with a modelled CtCBP structure, obtained using the crystal structure of Cellvibrio gilvus CBP in complex with glucose as a template, indicated differences in the subsite +1 region that elicit the distinct acceptor specificities of CtCBP and CtCDP. Thus Glu636 of CtCBP recognized the C1 hydroxyl of β-glucose at subsite +1, while in CtCDP the presence of Ala800 conferred more space, which allowed accommodation of C1 substituted disaccharide acceptors at the corresponding subsites +1 and +2. Furthermore, CtCBP has a short Glu496-Thr500 loop that permitted the C6 hydroxyl of glucose at subsite +1 to be exposed to solvent, whereas the corresponding longer loop Thr637-Lys648 in CtCDP blocks binding of C6-linked disaccharides as acceptors at subsite +1. High yields in chemoenzymatic synthesis, a novel regioselectivity, and novel oligosaccharides including products of CtCDP catalysed oligosaccharide oligomerisation using α-d-glucosyl 1-fluoride, all together contribute to the formation of an excellent basis for rational engineering of CBP and CDP to produce desired oligosaccharides.

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.