69429-19-2

Upstream product

• 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 
• 9004-34-6 cellulose 
• 2216-51-5 (-)-menthol 
• 118291-90-0 2-chloro-4-nitrophenol-α-D-maltotrioside 
• 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 
• 59-56-3 α-D-glucopyranosyl-1-phosphate 
• 528-50-7 cellobiose 
• 2106-10-7 1-deoxy-1-fluoro-α-D-glucose 
• 3482-57-3 p-nitrophenyl β-D-cellobioside 
• 1263-76-9 maltotetraose 
• 1184-46-9 D-maltohexaose 
• 754201-87-1 2,4-dinitrophenyl α-maltotrioside 

Downstream Products

• 32860-62-1 α-D-glucopyranosyl-(1->4)-α-D-glucopyranosyl-(1->4)-D-glucitol 
• 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 
• 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 
• 3458-28-4 D-Mannose 
• 492-61-5 β-D-glucose 
• 492-62-6 alpha-D-glucopyranose 
• 7322-31-8 β-D-mannose 
• 17690-94-7 cellotriose undecaacetate 
• 76821-26-6 maltotriose peracetate 

Relevant academic research and scientific papers

Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis

Lignocellulose feedstock constitutes the most abundant carbon source in the biosphere; however, its recalcitrance remains a challenge for microbial conversion into biofuel and bioproducts. Bacillus licheniformis is a microbial mesophilic bacterium capable of secreting a large number of glycoside hydrolase (GH) enzymes, including a glycoside hydrolase from GH family 9 (BlCel9). Here, we conducted biochemical and biophysical studies of recombinant BlCel9, and its low-resolution molecular shape was retrieved from small angle X-ray scattering (SAXS) data. BlCel9 is an endoglucanase exhibiting maximum catalytic efficiency at pH?7.0 and 60?°C. Furthermore, it retains 80% of catalytic activity within a broad range of pH values (5.5–8.5) and temperatures (up to 50?°C) for extended periods of time (over 48?h). It exhibits the highest hydrolytic activity against phosphoric acid swollen cellulose (PASC), followed by bacterial cellulose (BC), filter paper (FP), and to a lesser extent carboxymethylcellulose (CMC). The HPAEC-PAD analysis of the hydrolytic products demonstrated that the end product of the enzymatic hydrolysis is primarily cellobiose, and also small amounts of glucose, cellotriose, and cellotetraose are produced. SAXS data analysis revealed that the enzyme adopts a monomeric state in solution and has a molecular mass of 65.8?kDa as estimated from SAXS data. The BlCel9 has an elongated shape composed of an N-terminal family 3 carbohydrate-binding module (CBM3c) and a C-terminal GH9 catalytic domain joined together by 20 amino acid residue long linker peptides. The domains are closely juxtaposed in an extended conformation and form a relatively rigid structure in solution, indicating that the interactions between the CBM3c and GH9 catalytic domains might play a key role in cooperative cellulose biomass recognition and hydrolysis.

Hydrolysis behaviors of sugarcane bagasse pith in subcritical carbon dioxide-water

The aim of this study was to describe the hydrolysis behavior of sugarcane bagasse pith (SCBP) in subcritical CO2-water. The hydrolysis was carried out in a batch reactor using different temperatures (160 to 260 °C), liquid to solid ratios (20:1 to 100:1), CO2 pressures (0 to 7.3 MPa), stirring speeds (0 to 500 rpm) and reaction times (0 to 40 min). The highest total reducing sugar yield (43.6%) was obtained at 200 °C, liquid to solid ratio 30:1, 2 MPa CO2, 500 rpm and 50 min. Two-dimensional heteronuclear single quantum coherence (2D HSQC) nuclear magnetic resonance (NMR), scanning electron microscopy (SEM) and Fourier transform infrared spectrometry (FT-IR) were used to help elucidate the physical and chemical characteristics of the raw material and residual solid particles, with results consistent with the removal of hemicellulose during hydrolysis. The changes in the concentration of products with time were analyzed to understand product distribution through high-performance liquid chromatography (HPLC) and to infer the reaction mechanism.

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.

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.

Analysis of mono- and oligosaccharides in ionic liquid containing matrices

Ionic liquids (ILs), that is, salts with melting points 100 °C, have recently attracted a lot of attention in biomass processing due to their ability to dissolve lignocellulosics. In this work, we studied how two imidazolium-based, hydrophilic, cellulose dissolving ionic liquids 1,3-dimethylimidazolium dimethylphosphate [DMIM]DMP and 1-ethyl-3- methylimidazolium acetate [EMIM]AcO affect the usually employed analytical methods for mono- and oligosaccharides, typical products from hydrolytic treatments of biomass. HPLC methods were severely hampered by the presence of ILs with loss of separation power and severe baseline problems, making their use for saccharide quantification extremely challenging. Problems in DNS photometric assay and chromatography were also encountered at high ionic liquid concentrations and many capillary electrophoresis (CE) methods did not allow an efficient analysis of saccharides in these matrices. In this paper we describe an optimized CE method with pre-column derivatization for the qualitative and quantitative analysis of mono- and oligosaccharides in sample matrices containing moderate (20-40% (v/v)) concentrations of ILs. The IL content and type in the sample matrix was found to affect both peak shape and quantification parameters. Generally, the presence of high IL concentrations (≥20% (v/v)) had a dampening effect on the detection of the analytes. IL in lower concentrations of 20% (v/v) was, however, found to improve peak shape and/or separation in some cases. The optimized CE method has good sensitivity in moderate concentrations of the ionic liquids used, with limits of detection of 5 mg/L for cellooligomers up to the size of cellotetraose and 5-20 mg/L for cellopentaose and cellohexaose, depending on the matrix. The method was used for analysing the action of a commercial β-glucosidase in ILs and for analysing saccharides in the IL containing hydrolysates from the hydrolysis of microcrystalline cellulose with Trichoderma reesei endoglucanase Cel5A. According to the results, [DMIM]DMP and [EMIM]AcO] showed clear differences in enzyme inactivation.

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.

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.